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Conserved domains on  [gi|31543776|ref|NP_035615|]
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steroidogenic acute regulatory protein, mitochondrial precursor [Mus musculus]

Protein Classification

steroidogenic acute regulatory protein( domain architecture ID 10172357)

steroidogenic acute regulatory protein (STAR) plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone

Gene Symbol:  STAR
Gene Ontology:  GO:0008289|GO:0120020|GO:0006694
PubMed:  31927098|18922149

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 69-277 3.18e-153

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


:

Pssm-ID: 176914  Cd Length: 209  Bit Score: 426.17  E-value: 3.18e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  69 DQELSYIQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNP 148
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 149 NVKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHP 228
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 31543776 229 LAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEAS 277
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
 
Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 69-277 3.18e-153

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 426.17  E-value: 3.18e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  69 DQELSYIQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNP 148
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 149 NVKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHP 228
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 31543776 229 LAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEAS 277
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 76-280 2.66e-71

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 218.45  E-value: 2.66e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776     76 QQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPD--VGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNPNVKEI 153
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776    154 KVLQRIGKDTVITHELAAAAAGnLVGPRDFVSVRCTKR--RGSTCVLAGMATHFGEMPEqSGVIRAEHGPTCMVLHPLAG 231
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAG-PVSPRDFVFVRYWREdeDGSYAVVDVSVTHPTSPPE-SGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 31543776    232 SPSktKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEASPAS 280
Cdd:smart00234 159 GPS--KVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
75-280 1.74e-67

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 208.80  E-value: 1.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776    75 IQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNPNVKEIK 154
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776   155 VLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKR-RGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLAGSP 233
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 31543776   234 SktKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEASPAS 280
Cdd:pfam01852 161 S--KVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
PLN00188 PLN00188
enhanced disease resistance protein (EDR2); Provisional
 135-249 8.60e-03

enhanced disease resistance protein (EDR2); Provisional


Pssm-ID: 215094 [Multi-domain]  Cd Length: 719  Bit Score: 37.48  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  135 ELVDRMEAMG-EWNPNVKEIKVLQRI-GKDTVITHELAAAAAGNLVGPRDFVSVRCTKRR--GSTCVLAGMATHFGEMPe 210
Cdd:PLN00188 244 ELVMSMDGTRfEWDCSFQYGSLVEEVdGHTAILYHRLQLDWFPMFVWPRDLCYVRYWRRNddGSYVVLFRSREHENCGP- 322

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 31543776  211 QSGVIRA--EHG-----PtcmvLHPLAGSPsKTKLTWLLSIDLKGW 249
Cdd:PLN00188 323 QPGFVRAhlESGgfnisP----LKPRNGRP-RTQVQHLMQIDLKGW 363
 
Name Accession Description Interval E-value
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 69-277 3.18e-153

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 426.17  E-value: 3.18e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  69 DQELSYIQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNP 148
Cdd:cd08905   1 EAEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 149 NVKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHP 228
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 31543776 229 LAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEAS 277
Cdd:cd08905 161 LAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 69-276 2.37e-103

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 299.66  E-value: 2.37e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  69 DQELSYIQQGEVAMQKALGILNNQeGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNP 148
Cdd:cd08868   1 SQELEYLKQGAEALARAWSILTDP-GWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 149 NVKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHP 228
Cdd:cd08868  80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 31543776 229 LAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEA 276
Cdd:cd08868 160 LPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIAT 207
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 76-280 2.66e-71

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 218.45  E-value: 2.66e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776     76 QQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPD--VGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNPNVKEI 153
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPGrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776    154 KVLQRIGKDTVITHELAAAAAGnLVGPRDFVSVRCTKR--RGSTCVLAGMATHFGEMPEqSGVIRAEHGPTCMVLHPLAG 231
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAG-PVSPRDFVFVRYWREdeDGSYAVVDVSVTHPTSPPE-SGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 31543776    232 SPSktKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEASPAS 280
Cdd:smart00234 159 GPS--KVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
75-280 1.74e-67

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 208.80  E-value: 1.74e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776    75 IQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNPNVKEIK 154
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776   155 VLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKR-RGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLAGSP 233
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 31543776   234 SktKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEASPAS 280
Cdd:pfam01852 161 S--KVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 70-274 1.06e-58

Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176915  Cd Length: 209  Bit Score: 186.22  E-value: 1.06e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  70 QELSYIQQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPMDRLYEELVDRMEAMGEWNPN 149
Cdd:cd08906   2 QEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 150 VKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPL 229
Cdd:cd08906  82 VSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKS 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 31543776 230 AGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRL 274
Cdd:cd08906 162 ASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRI 206
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 81-272 1.39e-29

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 110.51  E-value: 1.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  81 AMQKALGILNNQEGWKKESQqENGDEVLSKMVPDVG-KVFRLEVVVDQPMDRLYEELVDrMEAMGEWNPNVKEIKVLQRI 159
Cdd:cd00177   3 AIEELLELLEEPEGWKLVKE-KDGVKIYTKPYEDSGlKLLKAEGVIPASPEQVFELLMD-IDLRKKWDKNFEEFEVIEEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 160 GKDTVITHelAAAAAGNLVGPRDFVSVRCTKRRG-STCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLagSPSKTKL 238
Cdd:cd00177  81 DEHTDIIY--YKTKPPWPVSPRDFVYLRRRRKLDdGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPL--DPGKTKV 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 31543776 239 TWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRK 272
Cdd:cd00177 157 TYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRK 190
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 76-274 1.55e-26

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 102.93  E-value: 1.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  76 QQGEVAMQKALGILNNQEGWKKESQQENGDEVLSKMVPDVGKVFRLEVVVDQPmdrlYEELVDRMEAM-----GEWNPNV 150
Cdd:cd08867   5 VIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDAL----PEKVIDVIIPPcgglrLKWDKSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 151 KEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKR-RGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPL 229
Cdd:cd08867  81 KHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRyEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 31543776 230 AGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRL 274
Cdd:cd08867 161 KGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 74-276 2.34e-20

Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy.


Pssm-ID: 176912  Cd Length: 208  Bit Score: 86.43  E-value: 2.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  74 YIQQGEVAMQKALGILNNQEGWKkesQQENGDEVLSKMVPDV---GKVFRLEVVVDQPMDRLYEELvdRMEAMG---EWN 147
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWK---TCRRTNEVAVSWRPSAefaGNLYKGEGIVYATLEQVWDCL--KPAAGGlrvKWD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 148 PNVKEIKVLQRIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGmATHFGE--MPEQSGVIRAEHGPTCMV 225
Cdd:cd08903  78 QNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSN-ATNVEHplCPPQAGFVRGFNHPCGCF 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 31543776 226 LHPLAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFANHLRKRLEA 276
Cdd:cd08903 157 CEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 83-271 1.30e-14

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176913  Cd Length: 204  Bit Score: 70.71  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  83 QKALGILNNQEGWK--KESQQENGDEVLSKMVPdvGKVFRLEVVVDQPMDRLYEELVdRMEAMGEWNPNVKEIKVLQRIG 160
Cdd:cd08904  12 QEVLGYSRDTSGWKvvKTSKKITVSWKPSRKYH--GNLYRVEGIIPESPAKLIQFMY-QPEHRIKWDKSLQVYKMLQRID 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 161 KDTVITHELAAAAAGNLVGPRDFVSVRCTKR-RGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLAGSPSKTKLT 239
Cdd:cd08904  89 SDTFICHTITQSFAMGSISPRDFVDLVHIKRyEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPAYSKLV 168

                       170       180       190
                ....*....|....*....|....*....|..
gi 31543776 240 WLLSIDLKGWLPKTIINQVLSQTQIEFANHLR 271
Cdd:cd08904 169 MFVQPELRGNLSRSVIEKTMPTNLVNLILDAK 200
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 92-275 2.60e-13

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 66.91  E-value: 2.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  92 QEGWKkESQQENGDEVLSKMVPDVG-KVFRLEVVVDQPMDRLYEELVDrMEAMGEWNPNVKEIKVLQRIGKDTVITHELA 170
Cdd:cd08876  16 DGDWQ-LVKDKDGIKVYTRDVEGSPlKEFKAVAEVDASIEAFLALLRD-TESYPQWMPNCKESRVLKRTDDNERSVYTVI 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 171 AAaagnlvgP-----RDFVS-VRCTKR--RGSTCVLAGMATHFGemPEQSGVIRAEHGPTCMVLHPLAGSpsKTKLTWLL 242
Cdd:cd08876  94 DL-------PwpvkdRDMVLrSTTEQDadDGSVTITLEAAPEAL--PEQKGYVRIKTVEGQWTFTPLGNG--KTRVTYQA 162

                       170       180       190
                ....*....|....*....|....*....|...
gi 31543776 243 SIDLKGWLPKTIINQVLSQTQIEFANHLRKRLE 275
Cdd:cd08876 163 YADPGGSIPGWLANAFAKDAPYNTLENLRKQLK 195
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 95-275 9.27e-08

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.


Pssm-ID: 176911  Cd Length: 202  Bit Score: 51.49  E-value: 9.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  95 WKKESQQENGdevlskmvpdvgKVFRLEVVVDQPMDRLYEELVD---RMEamgeWNPNVKEIKVLQRIGKDTVITHELAA 171
Cdd:cd08902  37 WRKPSEEFGG------------YLYKAQGVVEDVYNRIVDHIRPgpyRLD----WDSLMTSMDIIEEFEENCCVMRYTTA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 172 AAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEM-PEqsgVIRAEHGPTCMVLHPLAGSPSKTKLTWLLSIDLKGWL 250
Cdd:cd08902 101 GQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEArPN---FVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGML 177

                       170       180
                ....*....|....*....|....*
gi 31543776 251 PKTIINQVLSQTQIEFANHLRKRLE 275
Cdd:cd08902 178 PQSAVDTAMASTLVNFYSDLKKALK 202
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 93-258 1.61e-05

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 44.94  E-value: 1.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  93 EGWKkESQQENGDEVLSKMVPDVG----KVFRleVVVDQPMDRLYEELVDrMEAMGEWNPNVKEIKVLQRIGKDTVITHE 168
Cdd:cd08871  23 DGWK-LKYNKNNVKVWTKNPENSSikmiKVSA--IFPDVPAETLYDVLHD-PEYRKTWDSNMIESFDICQLNPNNDIGYY 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 169 LAAAAAGnlVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLagSPSKTKLTWLLSIDLKG 248
Cdd:cd08871  99 SAKCPKP--LKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPT--GPKGCTLTYVTQNDPKG 174

                       170
                ....*....|
gi 31543776 249 WLPKTIINQV 258
Cdd:cd08871 175 SLPKWVVNKA 184
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 94-248 7.99e-03

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 36.52  E-value: 7.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  94 GWKKESQQeNGDEVLSKMVPDvG---KVFRLEVVVDQPMdrlyEELVDRMeaMGE---WNPNVKEIKVLQRIGKDTVITH 167
Cdd:cd08869  20 GWVSVSSS-DHVELAFKKVDD-GhplRLWRASTEVEAPP----EEVLQRI--LRErhlWDDDLLQWKVVETLDEDTEVYQ 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776 168 ELAAAAAGNLvgPRDFVSVRCTKR--RGSTCVLAGMATHFGEmPEQSGVIRAEHGPTCMVLHPLagSPSKTKLTWLLSID 245
Cdd:cd08869  92 YVTNSMAPHP--TRDYVVLRTWRTdlPKGACVLVETSVEHTE-PVPLGGVRAVVLASRYLIEPC--GSGKSRVTHICRVD 166


                ...
gi 31543776 246 LKG 248
Cdd:cd08869 167 LRG 169
PLN00188 PLN00188
enhanced disease resistance protein (EDR2); Provisional
 135-249 8.60e-03

enhanced disease resistance protein (EDR2); Provisional


Pssm-ID: 215094 [Multi-domain]  Cd Length: 719  Bit Score: 37.48  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31543776  135 ELVDRMEAMG-EWNPNVKEIKVLQRI-GKDTVITHELAAAAAGNLVGPRDFVSVRCTKRR--GSTCVLAGMATHFGEMPe 210
Cdd:PLN00188 244 ELVMSMDGTRfEWDCSFQYGSLVEEVdGHTAILYHRLQLDWFPMFVWPRDLCYVRYWRRNddGSYVVLFRSREHENCGP- 322

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 31543776  211 QSGVIRA--EHG-----PtcmvLHPLAGSPsKTKLTWLLSIDLKGW 249
Cdd:PLN00188 323 QPGFVRAhlESGgfnisP----LKPRNGRP-RTQVQHLMQIDLKGW 363
 
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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