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Conserved domains on  [gi|2217361332|ref|XP_047274688|]
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inositol 1,4,5-trisphosphate receptor type 3 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 164-378 4.60e-161

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 495.33  E-value: 4.60e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  164 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 243
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  244 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 323
Cdd:cd23289     81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361332  324 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 378
Cdd:cd23289    161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-609 6.00e-83

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 270.99  E-value: 6.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  414 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMREQNILKQVFG---ILKAPFrekggEGPLVRLEELSDQKNAP 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  488 YQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 564
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361332  565 -REPRFLDYLSDLCVSNHIAIPVTQELICKCVLDpkNSDILIRTEL 609
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-169 9.09e-67

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


The actual alignment was detected with superfamily member pfam08709:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 225.45  E-value: 9.09e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332    1 MNRYSAQKQYWKAKQTKQDKEKIADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPA 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332   81 LLEKNAMRVTLDATGN-EGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNAGcKEVNSVNCNTSW 158
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 2217361332  159 KINLFMQFRDH 169
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1804-1913 1.87e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 142.28  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1804 TSVLIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1882
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217361332 1883 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1913
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans super family cl37996
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2204-2467 6.30e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


The actual alignment was detected with superfamily member pfam00520:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 43.79  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2204 IVALILRSiYYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIRgykamvmDMEFLYHVGYILTSVLGLFAHE 2277
Cdd:pfam00520   16 TIFLALET-YFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR-------SPWNILDFVVVLPSLISLVLSS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2278 -----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGF-LFLKDDFILEVDRLPNNH 2345
Cdd:pfam00520   88 vgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqLFGGKLKTWENPDNGRTN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2346 stasplgmphgaaafvdtcsgdkmdcvsglsvpevleedreldsteraCDTLLMCIVTVMNhgLRNGGGVGDILRKPSkD 2425
Cdd:pfam00520  168 ------------------------------------------------FDNFPNAFLWLFQ--TMTTEGWGDIMYDTI-D 196

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2217361332 2426 ESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2467
Cdd:pfam00520  197 GKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1130-1242 9.72e-04

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


The actual alignment was detected with superfamily member pfam01365:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 42.96  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1130 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTP 1195
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361332 1196 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHLLATHGRHVQYLDFL 1242
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 164-378 4.60e-161

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 495.33  E-value: 4.60e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  164 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 243
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  244 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 323
Cdd:cd23289     81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361332  324 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 378
Cdd:cd23289    161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-609 6.00e-83

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 270.99  E-value: 6.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  414 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMREQNILKQVFG---ILKAPFrekggEGPLVRLEELSDQKNAP 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  488 YQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 564
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361332  565 -REPRFLDYLSDLCVSNHIAIPVTQELICKCVLDpkNSDILIRTEL 609
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 173-371 1.12e-71

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 238.03  E-value: 1.12e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  173 VLKGGDVVRLFHAEQEKFLTCDEYKGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGN 252
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  253 YLAAEENPsykgdasdpkaagmGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLC 332
Cdd:pfam02815   81 YLHSHEEQ--------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVC 146

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2217361332  333 TNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIV 371
Cdd:pfam02815  147 TGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-169 9.09e-67

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 225.45  E-value: 9.09e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332    1 MNRYSAQKQYWKAKQTKQDKEKIADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPA 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332   81 LLEKNAMRVTLDATGN-EGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNAGcKEVNSVNCNTSW 158
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 2217361332  159 KINLFMQFRDH 169
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1804-1913 1.87e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 142.28  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1804 TSVLIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1882
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217361332 1883 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1913
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
52-106 1.84e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 1.84e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217361332    52 GDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTL--DATGNEGSWLFIQPF 106
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
171-227 6.10e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 6.10e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217361332   171 EEVLKGGDVVRLFHAEQEKFLTCDEYK------GKLQVFLRTtlrqsaTSATSSNALWEVEVV 227
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYG------NPAIDANTLWLIEPV 57
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2204-2467 6.30e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 43.79  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2204 IVALILRSiYYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIRgykamvmDMEFLYHVGYILTSVLGLFAHE 2277
Cdd:pfam00520   16 TIFLALET-YFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR-------SPWNILDFVVVLPSLISLVLSS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2278 -----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGF-LFLKDDFILEVDRLPNNH 2345
Cdd:pfam00520   88 vgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqLFGGKLKTWENPDNGRTN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2346 stasplgmphgaaafvdtcsgdkmdcvsglsvpevleedreldsteraCDTLLMCIVTVMNhgLRNGGGVGDILRKPSkD 2425
Cdd:pfam00520  168 ------------------------------------------------FDNFPNAFLWLFQ--TMTTEGWGDIMYDTI-D 196

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2217361332 2426 ESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2467
Cdd:pfam00520  197 GKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1130-1242 9.72e-04

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 42.96  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1130 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTP 1195
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361332 1196 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHLLATHGRHVQYLDFL 1242
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 55-123 5.95e-03

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 40.39  E-value: 5.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361332   55 VKYGSVIQLLHMKSNKYLTVNKRlPALLEKNAMRVTldATGNEGSWLFIQPFWKLRSNGDNVVVGDKVI 123
Cdd:cd23276     66 VRDGDEVRLLHKETNRYLRTHDA-AAPVTSKHKEVS--AYPDENEDGDDNDLWVVEIVKDEGKLEDKRI 131
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 164-378 4.60e-161

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 495.33  E-value: 4.60e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  164 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 243
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  244 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 323
Cdd:cd23289     81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361332  324 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 378
Cdd:cd23289    161 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 164-378 1.78e-133

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467748 [Multi-domain]  Cd Length: 204  Bit Score: 415.99  E-value: 1.78e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  164 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 243
Cdd:cd23277      1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  244 RFKHLATGNYLAAEENPSYKGDASdpkaagmgaqgRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRN 323
Cdd:cd23277     81 RFKHLATGQYLAAEVDPDPTPDPT-----------RSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVPRS 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217361332  324 SYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 378
Cdd:cd23277    150 SYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 158-378 1.83e-127

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 399.80  E-value: 1.83e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  158 WKINLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAG 237
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  238 HWNGLYRFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQGRTGR-RNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKT 316
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKkRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361332  317 DSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 378
Cdd:cd23288    161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 164-383 5.03e-113

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) and similar proteins; ITPR1, also called IP3 receptor isoform 1 (IP3R 1), or InsP3R1, or type 1 inositol 1,4,5-trisphosphate receptor, or type 1 InsP3 receptor, is an intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. It is involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. It plays a role in endoplasmic reticulum (ER) stress-induced apoptosis. ITPR1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467758 [Multi-domain]  Cd Length: 222  Bit Score: 358.23  E-value: 5.03e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  164 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 243
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  244 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGAQ--GRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVP 321
Cdd:cd23287     81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQdaSRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217361332  322 RNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEIRDLDF 383
Cdd:cd23287    161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-609 6.00e-83

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 270.99  E-value: 6.00e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  414 LLEDLVFFVSDVPNN---GQNVLDIMVTKPNRERQKLMREQNILKQVFG---ILKAPFrekggEGPLVRLEELSDQKNAP 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPF-----TGALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  488 YQHMFRLCYRVLRHSQEDYRKNQEHIAKQFGMMQSQIGYDILAE---DTITALLHNNRKLLEKHITKTEVETFVSLVRKN 564
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2217361332  565 -REPRFLDYLSDLCVSNHIAIPVTQELICKCVLDpkNSDILIRTEL 609
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 173-371 1.12e-71

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 238.03  E-value: 1.12e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  173 VLKGGDVVRLFHAEQEKFLTCDEYKGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLYRFKHLATGN 252
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  253 YLAAEENPsykgdasdpkaagmGAQGRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPRNSYVRLRHLC 332
Cdd:pfam02815   81 YLHSHEEQ--------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVC 146

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2217361332  333 TNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIV 371
Cdd:pfam02815  147 TGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-169 9.09e-67

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 225.45  E-value: 9.09e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332    1 MNRYSAQKQYWKAKQTKQDKEKIADVvllqkLQHAAQMEQKQNdtenkkvhgdvVKYGSVIQLLHMKSNKYLTVNKRLPA 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332   81 LLEKNAMRVTLDATGN-EGSWLFIQPFWKLRSNGDNVVVGDKVILNPVNAGQPLH-ASNYELSDNAGcKEVNSVNCNTSW 158
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 2217361332  159 KINLFMQFRDH 169
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1804-1913 1.87e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 142.28  E-value: 1.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1804 TSVLIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDIMCGSttgglgllglyINEDNVGLVIQTLET 1882
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217361332 1883 LTEYCQGPCHENQTCIvtHESNGIDIITALI 1913
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 168-374 1.11e-29

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 118.26  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  168 DHLEEVLKGGDVVRLFHAEQEKFLTC----DEYKGKLQVFLRTTLRQ-----SATSATSSNALWEVEVVHhDPCRGGAGH 238
Cdd:cd23280      1 KENENFLKGGDVVRLFHKELEAYLSAegsfVDEVLTEDVHLRVRPVDdrkprTLFPPTSGDTFWQIEKED-TPLKGGVIK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  239 WNGLYRFKHLATGNYLAAEENpsykgdasdpkaagmgaqgrtgrrnageKIKYCLVAVPHGNDIASLFELDPTTLQKTDS 318
Cdd:cd23280     80 WGDQCRLRHLPTGKYLAVDDK----------------------------TGNGKVVLTSDPSDPSTVFRLHPVTKETSEE 131

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217361332  319 fVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLM---------LGTCPTKEDKEAFAIVSVP 374
Cdd:cd23280    132 -VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLswdgaklrkVSLSLERQDDDAFTIQEVD 195
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 177-349 5.06e-26

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 106.70  E-value: 5.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  177 GDVVRLFHAEQEKFLTCDEY-----KGKLQVFLRTTLRQsatsaTSSNALWEVEVVHHDPcrGGAGHWNGLYRFKHLATG 251
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKnyptgSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  252 NYLAAEENPSykgdasdpkaagmgaqgrtgrrNAGEKIKYCLVAVPHGnDIASLFELDPT-TLQKTDSFVPRNSYVRLRH 330
Cdd:cd23263     74 KYLSSEEGKK----------------------SPKSNHQEVLCLTDNP-DKSSLFKFEPIgSTKYKQKYVKKDSYFRLKH 130

                          170
                   ....*....|....*....
gi 2217361332  331 LCTNTWIQSTNVPIDIEEE 349
Cdd:cd23263    131 VNTNFWLHSHEKKFNINNK 149
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
52-106 1.84e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 1.84e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217361332    52 GDVVKYGSVIQLLHMKSNKYLTVNKRLPALLEKNAMRVTL--DATGNEGSWLFIQPF 106
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
171-227 6.10e-05

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 6.10e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217361332   171 EEVLKGGDVVRLFHAEQEKFLTCDEYK------GKLQVFLRTtlrqsaTSATSSNALWEVEVV 227
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYG------NPAIDANTLWLIEPV 57
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 176-259 6.42e-05

MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also called RYRs) are intracellular Ca(2+) release channels located on the sarco/endoplasmic reticulum (SR/ER). They release calcium Ca(2+) intracellular stores to activate critical functions including muscle contraction and neurotransmitter release. The family includes three closely homologous proteins, RyR1, RyR2 and RyR3. RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RYR2 is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells. RyR1 and RyR2 release Ca2+ from the ER in response to excitation of muscle membranes to promote muscle contraction. RYR3 is involved in force production and calcium handling in extraocular muscle. RYRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467749 [Multi-domain]  Cd Length: 180  Bit Score: 46.15  E-value: 6.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  176 GGDVVRLFHAEQEKFLTCDEYKGKLQVFlRTTLRQSATSATSSNALWEVEVVHHDPCrGGAGHWNGLYRFKHLATGNYLA 255
Cdd:cd23278      1 GGDVLRLFHGHMDECLTIPAAGSKEDQH-RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRYLA 78


                   ....
gi 2217361332  256 AEEN 259
Cdd:cd23278     79 LTED 82
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 155-254 6.84e-05

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 46.17  E-value: 6.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  155 NTSWKI---NLFMQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKlqvFLRTTLRQSA----TSATSSNALWEVEVV 227
Cdd:cd23276     44 NNWWQIlkpRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAAP---VTSKHKEVSAypdeNEDGDDNDLWVVEIV 120

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217361332  228 hHDPCRGGAGHWNGL---YRFKHLATGNYL 254
Cdd:cd23276    121 -KDEGKLEDKRIKPLttrFRLRNKKTGCYL 149
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 171-258 8.97e-05

MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, also called RYR-1, or skeletal muscle calcium release channel, or skeletal muscle ryanodine receptor, or skeletal muscle-type ryanodine receptor, or type 1 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. It can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. It is required for normal embryonic development of muscle fibers and skeletal muscle, as well as for normal heart morphogenesis, skin development and ossification during embryogenesis. RYR-1 forms homotetramer and can also form heterotetramers with RYR-2. RYR-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467761 [Multi-domain]  Cd Length: 192  Bit Score: 46.03  E-value: 8.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  171 EEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQvfLRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFK 246
Cdd:cd23290      5 EGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLRIR 77

                           90
                   ....*....|..
gi 2217361332  247 HLATGNYLAAEE 258
Cdd:cd23290     78 HVTTGRYLALTE 89
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
234-287 1.20e-04

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 1.20e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 2217361332   234 GGAGHWNGLYRFKHLATGNYLAAEENPsykgdasdPKAAGMGAQGRTGRRNAGE 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEK--------LPPWGDGQQEVTGYGNPAI 46
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 174-259 2.10e-04

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467763 [Multi-domain]  Cd Length: 187  Bit Score: 44.52  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332  174 LKGGDVVRLFHAEQEKfLTCDEYKgKLQVFLRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFKHLA 249
Cdd:cd23292      3 LLGGHVVRLFHGHDEC-LTIPSTD-QSDEQHRVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHLT 75

                           90
                   ....*....|
gi 2217361332  250 TGNYLAAEEN 259
Cdd:cd23292     76 TGHYLALTED 85
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
113-163 3.69e-04

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.40  E-value: 3.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217361332   113 GDNVVVGDKVILNPVNAGQPLHAS-NYELSDNAGCKEVNSV-----NCNTSWKINLF 163
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdEKLPPWGDGQQEVTGYgnpaiDANTLWLIEPV 57
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2204-2467 6.30e-04

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 43.79  E-value: 6.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2204 IVALILRSiYYLGIGPTLNILGALNLTNKIVFVVSFV------GNRGTFIRgykamvmDMEFLYHVGYILTSVLGLFAHE 2277
Cdd:pfam00520   16 TIFLALET-YFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFR-------SPWNILDFVVVLPSLISLVLSS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2278 -----------LFYSILLFDLIYREETLFNVIKSVTRNGRSILLTALLALILVYLFSIVGF-LFLKDDFILEVDRLPNNH 2345
Cdd:pfam00520   88 vgslsglrvlrLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqLFGGKLKTWENPDNGRTN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 2346 stasplgmphgaaafvdtcsgdkmdcvsglsvpevleedreldsteraCDTLLMCIVTVMNhgLRNGGGVGDILRKPSkD 2425
Cdd:pfam00520  168 ------------------------------------------------FDNFPNAFLWLFQ--TMTTEGWGDIMYDTI-D 196

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2217361332 2426 ESLFPARVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2467
Cdd:pfam00520  197 GKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1130-1242 9.72e-04

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 42.96  E-value: 9.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217361332 1130 KKQQRLLKNMDAHKVML---DLLQIPY-----------DKGDAKMMEILRYTHQFLQKFCAGNPGNQALLHKHLHLFLTP 1195
Cdd:pfam01365   32 RQRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217361332 1196 --------GLLeaETMQHIFLNNYQLC-SEISEPVLQHFVHLLATHGRHVQYLDFL 1242
Cdd:pfam01365  112 lgspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 55-123 5.95e-03

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 40.39  E-value: 5.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217361332   55 VKYGSVIQLLHMKSNKYLTVNKRlPALLEKNAMRVTldATGNEGSWLFIQPFWKLRSNGDNVVVGDKVI 123
Cdd:cd23276     66 VRDGDEVRLLHKETNRYLRTHDA-AAPVTSKHKEVS--AYPDENEDGDDNDLWVVEIVKDEGKLEDKRI 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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