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Conserved domains on  [gi|158187554|ref|NP_001103367|]
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short transient receptor potential channel 2 [Mus musculus]

Protein Classification

transient-receptor-potential channel family protein( domain architecture ID 1750128)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

Gene Ontology:  GO:0070588|GO:0005262|GO:0070679
PubMed:  20025796|18535090|20861159
SCOP:  4000366
TCDB:  1.A.4

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 23-761 3.62e-140

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


The actual alignment was detected with superfamily member TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 434.51  E-value: 3.62e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554   23 TLLRAIQEGQLGLVQQLLEsssdasgagpgGPLRNVEESEDRSWREAL-NLAIRLGHEVITDVLLanvKFDFR-QIHEAL 100
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLE-----------EPKKLNINCPDRLGRSALfVAAIENENLELTELLL---NLSCRgAVGDTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  101 LVAVDTNQPAVVRRLLARLErekgrKVDTKSFSLaFFDSSIDGSRFAPGVTPLTLACQKDLYEIAQLLMDQGHTIarphP 180
Cdd:TIGR00870  86 LHAISLEYVDAVEAILLHLL-----AAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASV----P 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  181 VSCACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASED--AMLAAFQLSRELRRLARKEPEFKPQYIALESLCQDY 258
Cdd:TIGR00870 156 ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDpaDILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  259 GFELLGMCRNQSEVTAVLNDLGEDSETepeaeglgQAFEEGIPNLARLRLAVNYNQKQFVAHPICQQVLSSIWCGNLAGW 338
Cdd:TIGR00870 236 ALSLLDKLRDSKELEVILNHQGLTPLK--------LAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGW 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  339 RGSTTIWKLFVAFLIFLTMPFLCIGYWLAPKSQLGRLLKIPVLKFLLHSASYLWFLIFLLGESLVMETQLSTFKGR--SQ 416
Cdd:TIGR00870 308 RRKQSVLELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDLRVtgLQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  417 SVWETSLHMIWVTGFLWFECKEVWIEGLRSYLLDWWNFLDVVILSLYLASFALRlllaglaYMHCrdasdsTTCRYFTTA 496
Cdd:TIGR00870 388 QTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDR-------PFAI------LFVTQAFLV 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  497 ERSEWRTEDPQFLAEVLFAVTSMLSFTRLAYILPAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPYQ 575
Cdd:TIGR00870 455 LREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMIlGDILRFLFIYAVVLFGFACGLNQLYQYYD 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  576 ESEKLGNFN-----------------ETFQFLFWTMFGMEEhtVVDMPQFLVpEFVGRAMYGIFTIVMVIVLLNMLIAMI 638
Cdd:TIGR00870 535 ELKLNECSNpharscekqgnaystlfETSQELFWAIIGLGD--LLANEHKFT-EFVGLLLFGAYNVIMYILLLNMLIAMM 611

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  639 TNSFQKIEDDADVEWKFARSKLYLSYFREGLTLPVPFNILPSPKAAFYLVRRIFRFLC--CGSSCCKAKKSDYPPIGTft 716
Cdd:TIGR00870 612 GNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGkkRQRWCRRVEEVNWTTWER-- 689

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 158187554  717 npgaRAGSAGEGERVSYrlRVIKALVQRYI--ETARREFEETRRKDL 761
Cdd:TIGR00870 690 ----KAETLIEDGLHYQ--RVMKRLIKRYVlaEQRPRDDEGTTEEET 730
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 23-761 3.62e-140

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 434.51  E-value: 3.62e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554   23 TLLRAIQEGQLGLVQQLLEsssdasgagpgGPLRNVEESEDRSWREAL-NLAIRLGHEVITDVLLanvKFDFR-QIHEAL 100
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLE-----------EPKKLNINCPDRLGRSALfVAAIENENLELTELLL---NLSCRgAVGDTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  101 LVAVDTNQPAVVRRLLARLErekgrKVDTKSFSLaFFDSSIDGSRFAPGVTPLTLACQKDLYEIAQLLMDQGHTIarphP 180
Cdd:TIGR00870  86 LHAISLEYVDAVEAILLHLL-----AAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASV----P 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  181 VSCACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASED--AMLAAFQLSRELRRLARKEPEFKPQYIALESLCQDY 258
Cdd:TIGR00870 156 ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDpaDILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  259 GFELLGMCRNQSEVTAVLNDLGEDSETepeaeglgQAFEEGIPNLARLRLAVNYNQKQFVAHPICQQVLSSIWCGNLAGW 338
Cdd:TIGR00870 236 ALSLLDKLRDSKELEVILNHQGLTPLK--------LAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGW 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  339 RGSTTIWKLFVAFLIFLTMPFLCIGYWLAPKSQLGRLLKIPVLKFLLHSASYLWFLIFLLGESLVMETQLSTFKGR--SQ 416
Cdd:TIGR00870 308 RRKQSVLELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDLRVtgLQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  417 SVWETSLHMIWVTGFLWFECKEVWIEGLRSYLLDWWNFLDVVILSLYLASFALRlllaglaYMHCrdasdsTTCRYFTTA 496
Cdd:TIGR00870 388 QTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDR-------PFAI------LFVTQAFLV 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  497 ERSEWRTEDPQFLAEVLFAVTSMLSFTRLAYILPAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPYQ 575
Cdd:TIGR00870 455 LREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMIlGDILRFLFIYAVVLFGFACGLNQLYQYYD 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  576 ESEKLGNFN-----------------ETFQFLFWTMFGMEEhtVVDMPQFLVpEFVGRAMYGIFTIVMVIVLLNMLIAMI 638
Cdd:TIGR00870 535 ELKLNECSNpharscekqgnaystlfETSQELFWAIIGLGD--LLANEHKFT-EFVGLLLFGAYNVIMYILLLNMLIAMM 611

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  639 TNSFQKIEDDADVEWKFARSKLYLSYFREGLTLPVPFNILPSPKAAFYLVRRIFRFLC--CGSSCCKAKKSDYPPIGTft 716
Cdd:TIGR00870 612 GNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGkkRQRWCRRVEEVNWTTWER-- 689

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 158187554  717 npgaRAGSAGEGERVSYrlRVIKALVQRYI--ETARREFEETRRKDL 761
Cdd:TIGR00870 690 ----KAETLIEDGLHYQ--RVMKRLIKRYVlaEQRPRDDEGTTEEET 730
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
 183-242 2.28e-27

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 105.36  E-value: 2.28e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  183 CACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASEDAMLAAFQLSRELRRLARKEP 242
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 535-654 6.86e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 6.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 535 LGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPyQESEKLGNFNE-------TFQfLFWTMFGMEEHTVVDMP 606
Cdd:cd22192  447 LGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQT-EDPDSLGHFYDfpmtlfsTFE-LFLGLIDGPANYTVDLP 524

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 158187554 607 QFLvpefvgRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWK 654
Cdd:cd22192  525 FMY------KVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-172 5.64e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  24 LLRAIQEGQLGLVQQLLESssdasGAGPggplrnveESEDRSWREALNLAIRLGHEVITDVLL---ANVKFDFRQIHEAL 100
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEA-----GADV--------NARDKDGETPLHLAAYNGNLEIVKLLLeagADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158187554 101 LVAVDTNQPAVVRRLLarlerEKGRKVDTKSfslaffdssidgsrfAPGVTPLTLACQKDLYEIAQLLMDQG 172
Cdd:COG0666  158 HLAAANGNLEIVKLLL-----EAGADVNARD---------------NDGETPLHLAAENGHLEIVKLLLEAG 209
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 23-761 3.62e-140

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 434.51  E-value: 3.62e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554   23 TLLRAIQEGQLGLVQQLLEsssdasgagpgGPLRNVEESEDRSWREAL-NLAIRLGHEVITDVLLanvKFDFR-QIHEAL 100
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLE-----------EPKKLNINCPDRLGRSALfVAAIENENLELTELLL---NLSCRgAVGDTL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  101 LVAVDTNQPAVVRRLLARLErekgrKVDTKSFSLaFFDSSIDGSRFAPGVTPLTLACQKDLYEIAQLLMDQGHTIarphP 180
Cdd:TIGR00870  86 LHAISLEYVDAVEAILLHLL-----AAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASV----P 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  181 VSCACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASED--AMLAAFQLSRELRRLARKEPEFKPQYIALESLCQDY 258
Cdd:TIGR00870 156 ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDpaDILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  259 GFELLGMCRNQSEVTAVLNDLGEDSETepeaeglgQAFEEGIPNLARLRLAVNYNQKQFVAHPICQQVLSSIWCGNLAGW 338
Cdd:TIGR00870 236 ALSLLDKLRDSKELEVILNHQGLTPLK--------LAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGW 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  339 RGSTTIWKLFVAFLIFLTMPFLCIGYWLAPKSQLGRLLKIPVLKFLLHSASYLWFLIFLLGESLVMETQLSTFKGR--SQ 416
Cdd:TIGR00870 308 RRKQSVLELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRTDLRVtgLQ 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  417 SVWETSLHMIWVTGFLWFECKEVWIEGLRSYLLDWWNFLDVVILSLYLASFALRlllaglaYMHCrdasdsTTCRYFTTA 496
Cdd:TIGR00870 388 QTPLEMLIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDR-------PFAI------LFVTQAFLV 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  497 ERSEWRTEDPQFLAEVLFAVTSMLSFTRLAYILPAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPYQ 575
Cdd:TIGR00870 455 LREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRGNQHLGPLQIMIGRMIlGDILRFLFIYAVVLFGFACGLNQLYQYYD 534

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  576 ESEKLGNFN-----------------ETFQFLFWTMFGMEEhtVVDMPQFLVpEFVGRAMYGIFTIVMVIVLLNMLIAMI 638
Cdd:TIGR00870 535 ELKLNECSNpharscekqgnaystlfETSQELFWAIIGLGD--LLANEHKFT-EFVGLLLFGAYNVIMYILLLNMLIAMM 611

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  639 TNSFQKIEDDADVEWKFARSKLYLSYFREGLTLPVPFNILPSPKAAFYLVRRIFRFLC--CGSSCCKAKKSDYPPIGTft 716
Cdd:TIGR00870 612 GNTYQLIADDADEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGkkRQRWCRRVEEVNWTTWER-- 689

                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*..
gi 158187554  717 npgaRAGSAGEGERVSYrlRVIKALVQRYI--ETARREFEETRRKDL 761
Cdd:TIGR00870 690 ----KAETLIEDGLHYQ--RVMKRLIKRYVlaEQRPRDDEGTTEEET 730
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
 183-242 2.28e-27

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 105.36  E-value: 2.28e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  183 CACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASEDAMLAAFQLSRELRRLARKEP 242
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 390-650 4.62e-20

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: 90.40  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  390 YLWFLIFLLGESLVMETQLSTFKGRSQ--SVWETsLHMIWVTGFLWFECKEVWIEGL-RSYLLDWWNFLDVVILSLYLAS 466
Cdd:pfam00520   4 FELFILLLILLNTIFLALETYFQPEEPltTVLEI-LDYVFTGIFTLEMLLKIIAAGFkKRYFRSPWNILDFVVVLPSLIS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  467 FALRLLlaglaymhcrdasdsttcryfttaersewrtedpqflaeVLFAVTSMLSFTRLAYILPAHESLGTLQI---SIG 543
Cdd:pfam00520  83 LVLSSV---------------------------------------GSLSGLRVLRLLRLLRLLRLIRRLEGLRTlvnSLI 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  544 KMIDDMIRFMFILMIILTAFLCGLNNIYVPYQESEKLGNFNET--------FQFLFWTMFGMEEHTVVDMPQFLVPEFVG 615
Cdd:pfam00520 124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTnfdnfpnaFLWLFQTMTTEGWGDIMYDTIDGKGEFWA 203

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 158187554  616 RAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDAD 650
Cdd:pfam00520 204 YIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 535-654 6.86e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 6.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 535 LGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPyQESEKLGNFNE-------TFQfLFWTMFGMEEHTVVDMP 606
Cdd:cd22192  447 LGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIFQT-EDPDSLGHFYDfpmtlfsTFE-LFLGLIDGPANYTVDLP 524

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 158187554 607 QFLvpefvgRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWK 654
Cdd:cd22192  525 FMY------KVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-172 5.64e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  24 LLRAIQEGQLGLVQQLLESssdasGAGPggplrnveESEDRSWREALNLAIRLGHEVITDVLL---ANVKFDFRQIHEAL 100
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEA-----GADV--------NARDKDGETPLHLAAYNGNLEIVKLLLeagADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158187554 101 LVAVDTNQPAVVRRLLarlerEKGRKVDTKSfslaffdssidgsrfAPGVTPLTLACQKDLYEIAQLLMDQG 172
Cdd:COG0666  158 HLAAANGNLEIVKLLL-----EAGADVNARD---------------NDGETPLHLAAENGHLEIVKLLLEAG 209
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 517-657 1.67e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 58.35  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 517 TSMLSFTRlayilpAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYvPYQESEKLGNFN-------ETFQ 588
Cdd:cd21882  420 CNVLYYTR------GFQMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASAFVILF-QTEDPNKLGEFRdypdallELFK 492

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158187554 589 FlFWTMFGMEEHTVVDMPqflvpeFVGRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWKFAR 657
Cdd:cd21882  493 F-TIGMGDLPFNENVDFP------FVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-172 1.52e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  62 EDRSWREALNLAIRLGHEVITDVLL---ANVKFDFRQIHEALLVAVDTNQPAVVRRLLarlerEKGRKVDTKSFSlaffd 138
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLeagADVNARDKDGETPLHLAAYNGNLEIVKLLL-----EAGADVNAQDND----- 152

                         90       100       110
                 ....*....|....*....|....*....|....
gi 158187554 139 ssidgsrfapGVTPLTLACQKDLYEIAQLLMDQG 172
Cdd:COG0666  153 ----------GNTPLHLAAANGNLEIVKLLLEAG 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-130 3.93e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 3.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554   24 LLRAIQEGQLGLVQQLLESSSDASGAGPGGplrnveesedrswREALNLAIRLGHEVITDVLLANVKFDFRQIHE-ALLV 102
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNG-------------RTALHLAAKNGHLEIVKLLLEHADVNLKDNGRtALHY 67

                          90       100
                  ....*....|....*....|....*...
gi 158187554  103 AVDTNQPAVVRRLLarlerEKGRKVDTK 130
Cdd:pfam12796  68 AARSGHLEIVKLLL-----EKGADINVK 90
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 507-676 6.03e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 49.79  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 507 QFLAEVLFAV----TSMLSFTRlayilpAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVP--YQES-- 577
Cdd:cd22193  411 EYLACLVLALalgwANMLYYTR------GFQSMGIYSVMIQKVIlRDLLRFLFVYLLFLFGFAVALVSLIEKcsSDKKdc 484

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 578 EKLGNFNETFQFLFWTMFGMEEHTVVDMPQFLVPEFVGRAMYGIFTIVMvivLLNMLIAMITNSFQKIEDDADVEWKFAR 657
Cdd:cd22193  485 SSYGSFSDAVLELFKLTIGMGDLEFQENSTYPAVFLILLLTYVILTFVL---LLNMLIALMGETVNNVSKESKRIWKLQR 561

                        170       180       190
                 ....*....|....*....|....*....|
gi 158187554 658 SKLYL-----------SYFREGLTLPVPFN 676
Cdd:cd22193  562 AITILefeksfpecmrKAFRSGRLLKVGLC 591
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 512-669 8.69e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.42  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 512 VLFAVTSM-LSFTRLAYILPAHESLGTLQISIGKMI-DDMIRFMFILMIILTAFLCGLNNIYVPYQESEKLGN------- 582
Cdd:cd22196  430 VAFMVISLaLGWANVLYYTRGFQQMGIYSVMIQKMIlRDICRFLFVYLVFLFGFSAALVTLIEDGPPKGDVNTsqkecvc 509

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 583 ------FNE---TFQFLFWTMFGMEEHTVVDMPQFlVPEFVgrAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEW 653
Cdd:cd22196  510 ksgynsYNSlysTCLELFKFTIGMGDLEFTENYKF-KEVFI--FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIW 586

                        170       180
                 ....*....|....*....|...
gi 158187554 654 KFARS-------KLYLSYFREGL 669
Cdd:cd22196  587 KLQRAitildleKSLLRCLRDRF 609
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 512-673 3.09e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 512 VLFAVTSM-LSFTRLAYILPAHESLGTLQISIGKMI-DDMIRFMFILMIILTAF---LCGLNNIYVPYQESEKLGNFNET 586
Cdd:cd22194  474 LACLVLAMaLGWANMLYYTRGFQSLGIYSVMIQKVIlNDVLKFLLVYILFLLGFgvaLASLIEDCPDDSECSSYGSFSDA 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554 587 FQFLFWTMFGMEEHTVVDMPQFlvPEfVGRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWKFARSKLYLSYFR 666
Cdd:cd22194  554 VLELFKLTIGLGDLEIQQNSKY--PI-LFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEK 630


                 ....*..
gi 158187554 667 eglTLPV 673
Cdd:cd22194  631 ---SLPE 634
Ank_2 pfam12796
Ankyrin repeats (3 copies);
70-172 3.08e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554   70 LNLAIRLGHEVITDVLL---ANVKFDFRQIHEALLVAVDTNQPAVVRRLLARlerekgrkvdtksfslaffdssIDGSRF 146
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLengADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----------------------ADVNLK 58

                          90       100
                  ....*....|....*....|....*.
gi 158187554  147 APGVTPLTLACQKDLYEIAQLLMDQG 172
Cdd:pfam12796  59 DNGRTALHYAARSGHLEIVKLLLEKG 84
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-172 3.86e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  69 ALNLAIRLGHEVITDVLL---ANVKFDFRQIHEALLVAVDTNQPAVVRRLLarlerEKGRKVDTKSfslaffdssidgsr 145
Cdd:COG0666   57 LLLAAALAGDLLVALLLLaagADINAKDDGGNTLLHAAARNGDLEIVKLLL-----EAGADVNARD-------------- 117

                         90       100
                 ....*....|....*....|....*..
gi 158187554 146 fAPGVTPLTLACQKDLYEIAQLLMDQG 172
Cdd:COG0666  118 -KDGETPLHLAAYNGNLEIVKLLLEAG 143
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 426-642 7.52e-03

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 38.80  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  426 IWVTGFLWF---ECKEVWIEGLRsYLLDWWNFLDVVILSLYLASfalrlllaglayMHCRDASDSTTCRYFTTAERSEWR 502
Cdd:pfam08016  16 VFVVFFLYFvveEILKIRKHRPS-YLRSVWNLLDLAIVILSVVL------------IVLNIYRDFLADRLIKSVEASPVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158187554  503 T---EDPQFLAEVLFAVTSMLSF---TRLAYILPAHESLGTLQISIGKMIDDMIRFMFILMIILTAFlcGLNNIYVPYQE 576
Cdd:pfam08016  83 FidfDRVAQLDNLYRIILAFLVFltwLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAY--AQFGYLLFGTQ 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158187554  577 SEKLGNFNETFQFLFWTMFGMEEHTVVdmpqFLVPEFVGRAMYGIFTIVMVIVLLNMLIAMITNSF 642
Cdd:pfam08016 161 APNFSNFVKSILTLFRTILGDFGYNEI----FSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
 
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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