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Conserved domains on  [gi|1207159053|ref|XP_021324495|]
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stAR-related lipid transfer protein 4 isoform X1 [Danio rerio]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 12-202 1.48e-105

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08902:

Pssm-ID: 472699  Cd Length: 202  Bit Score: 301.87  E-value: 1.48e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  12 LKDTLISYHQLEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILETPE 91
Cdd:cd08902    10 LQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  92 QGCCVVKYTTSGQLWNIISPREFVDFSYTSECERGLLSCGVSVDREQHSSGCVRGFNHACGWFCVP-TDDPSLSLLTGYI 170
Cdd:cd08902    90 ENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPlKDNPSHSLLTGYI 169

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207159053 171 QTDLRGHLPRAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd08902   170 QTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 12-202 1.48e-105

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: 301.87  E-value: 1.48e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  12 LKDTLISYHQLEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILETPE 91
Cdd:cd08902    10 LQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  92 QGCCVVKYTTSGQLWNIISPREFVDFSYTSECERGLLSCGVSVDREQHSSGCVRGFNHACGWFCVP-TDDPSLSLLTGYI 170
Cdd:cd08902    90 ENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPlKDNPSHSLLTGYI 169

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207159053 171 QTDLRGHLPRAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd08902   170 QTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 21-204 1.09e-21

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 87.87  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053   21 QLEDADWRLSKRSK--DVSVWQRASQEFSGSLYKAQGRVRGDPQQIV-DFLRPGARRLDWDSMMTSMEILETPEQGCCVV 97
Cdd:smart00234  14 AASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIY 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053   98 KYTTSGQlWNIISPREFVDFSYTSECERG-LLSCGVSVDREQH--SSGCVRGfNHACGWFCVPTDDPSLSLLTGYIQTDL 174
Cdd:smart00234  94 HYVSKFA-AGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSppESGYVRA-ENLPSGLLIEPLGNGPSKVTWVSHADL 171

                          170       180       190
                   ....*....|....*....|....*....|
gi 1207159053  175 RGHLPRAAVDTAMASGLITFFSDLQRALDA 204
Cdd:smart00234 172 KGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
START pfam01852
START domain;
21-203 3.14e-20

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 83.99  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  21 QLEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIV-DFLRPGARRLDWDSMMTSMEILETPEQGCCVVKY 99
Cdd:pfam01852  15 LSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVaELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 100 TTSGQLWNIISPREFVDFSYTSECERG-LLSCGVSVDREQH--SSGCVRGFNHACGwFCVPTDDPSLSLLTGYIQTDLRG 176
Cdd:pfam01852  95 VAALVAPSPLSPRDFVFLRYWRRLGGGvYVIVDRSVTHPQFppSSGYVRAERLPSG-YLIQPCGNGPSKVTWVSHADLKG 173

                         170       180
                  ....*....|....*....|....*..
gi 1207159053 177 HLPRAAVDTAMASGLITFFSDLQRALD 203
Cdd:pfam01852 174 WLPSWLLRSLYKSGMPEGAKTWVATLQ 200
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 12-202 1.48e-105

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: 301.87  E-value: 1.48e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  12 LKDTLISYHQLEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILETPE 91
Cdd:cd08902    10 LQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  92 QGCCVVKYTTSGQLWNIISPREFVDFSYTSECERGLLSCGVSVDREQHSSGCVRGFNHACGWFCVP-TDDPSLSLLTGYI 170
Cdd:cd08902    90 ENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPlKDNPSHSLLTGYI 169

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207159053 171 QTDLRGHLPRAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd08902   170 QTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 10-202 1.91e-71

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: 215.79  E-value: 1.91e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  10 QALKDTLISYHQLEDAdWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRP--GARRLDWDSMMTSMEIL 87
Cdd:cd08867     8 EKLANEALQYINDTDG-WKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpcGGLRLKWDKSLKHYEVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  88 ETPEQGCCVVKYTTSGQLWNIISPREFVDFSYTSECE-RGLLSCGVSVDREQH--SSGCVRGFNHACGWFCVPTDD-PSL 163
Cdd:cd08867    87 EKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEdNQWSSSGKSVDIPERppTPGFVRGYNHPCGYFCSPLKGsPDK 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207159053 164 SLLTGYIQTDLRGHLPRAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd08867   167 SFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 10-204 2.40e-43

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: 144.21  E-value: 2.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  10 QALKDTLISYHQLEDAdWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRP--GARRLDWDSMMTSMEIL 87
Cdd:cd08903     8 ESVADKMLLYRRDESG-WKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPaaGGLRVKWDQNVKDFEVV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  88 ETPEQGCCVVKYTTSGQLWNIISPREFVDFSYTSECERG-LLSCGVSVDRE--QHSSGCVRGFNHACGWFCVPT-DDPSL 163
Cdd:cd08903    87 EAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGtISSNATNVEHPlcPPQAGFVRGFNHPCGCFCEPVpGEPDK 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1207159053 164 SLLTGYIQTDLRGHLPRAAVDTAMASGLITFFSDLQRALDA 204
Cdd:cd08903   167 TQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 23-202 5.68e-39

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: 132.46  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  23 EDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILETPEQGCCVVKYTTS 102
Cdd:cd00177    13 EPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 103 GQLwnIISPREFVDFSYT-SECERGLLSCGVSVDREQH--SSGCVRGFNHACGWFCVPTDDPSlSLLTGYIQTDLRGHLP 179
Cdd:cd00177    93 PPW--PVSPRDFVYLRRRrKLDDGTYVIVSKSVDHDSHpkEKGYVRAEIKLSGWIIEPLDPGK-TKVTYVLQVDPKGSIP 169

                         170       180
                  ....*....|....*....|...
gi 1207159053 180 RAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd00177   170 KSLVNSAAKKQLASFLKDLRKAK 192
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 27-199 5.54e-34

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: 120.01  E-value: 5.54e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  27 WRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILETPEQGCCVVKYTTSGQLW 106
Cdd:cd08904    24 WKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAM 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 107 NIISPREFVDFSYTS--ECERGLLScGVSVDREQH--SSGCVRGFNHACGWFCVP-TDDPSLSLLTGYIQTDLRGHLPRA 181
Cdd:cd08904   104 GSISPRDFVDLVHIKryEGNMNIVS-SVSVEYPQCppSSNYIRGYNHPCGYVCSPlPENPAYSKLVMFVQPELRGNLSRS 182

                         170
                  ....*....|....*...
gi 1207159053 182 AVDTAMASGLITFFSDLQ 199
Cdd:cd08904   183 VIEKTMPTNLVNLILDAK 200
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 21-204 1.09e-21

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 87.87  E-value: 1.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053   21 QLEDADWRLSKRSK--DVSVWQRASQEFSGSLYKAQGRVRGDPQQIV-DFLRPGARRLDWDSMMTSMEILETPEQGCCVV 97
Cdd:smart00234  14 AASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIY 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053   98 KYTTSGQlWNIISPREFVDFSYTSECERG-LLSCGVSVDREQH--SSGCVRGfNHACGWFCVPTDDPSLSLLTGYIQTDL 174
Cdd:smart00234  94 HYVSKFA-AGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSppESGYVRA-ENLPSGLLIEPLGNGPSKVTWVSHADL 171

                          170       180       190
                   ....*....|....*....|....*....|
gi 1207159053  175 RGHLPRAAVDTAMASGLITFFSDLQRALDA 204
Cdd:smart00234 172 KGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
START pfam01852
START domain;
21-203 3.14e-20

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 83.99  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  21 QLEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIV-DFLRPGARRLDWDSMMTSMEILETPEQGCCVVKY 99
Cdd:pfam01852  15 LSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVaELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 100 TTSGQLWNIISPREFVDFSYTSECERG-LLSCGVSVDREQH--SSGCVRGFNHACGwFCVPTDDPSLSLLTGYIQTDLRG 176
Cdd:pfam01852  95 VAALVAPSPLSPRDFVFLRYWRRLGGGvYVIVDRSVTHPQFppSSGYVRAERLPSG-YLIQPCGNGPSKVTWVSHADLKG 173

                         170       180
                  ....*....|....*....|....*..
gi 1207159053 177 HLPRAAVDTAMASGLITFFSDLQRALD 203
Cdd:pfam01852 174 WLPSWLLRSLYKSGMPEGAKTWVATLQ 200
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 22-200 3.92e-14

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: 67.76  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  22 LEDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVD--FLRPgARRLDWDSMMTSMEILETPEQGCCVVKY 99
Cdd:cd08868    21 LTDPGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNelVLNV-ESLPSWNPTVLECKIIQVIDDNTDISYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 100 TTSGQLWNIISPREFVDFSYTSECERGLLSCGVSVdreQHSS-----GCVRGFNHACGWFCVP-TDDPSLSLLTGYIQTD 173
Cdd:cd08868   100 VAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSV---EHPAmpptkNYVRGENGPGCWILRPlPNNPNKCNFTWLLNTD 176

                         170       180
                  ....*....|....*....|....*..
gi 1207159053 174 LRGHLPRAAVDTAMASGLITFFSDLQR 200
Cdd:cd08868   177 LKGWLPQYLVDQALASVLLDFMKHLRK 203
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 77-202 1.10e-07

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: 50.25  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  77 WDSMMTSMEILETPEQGCCVVKYTTSGQLWNIISPREFVDFSYTSECERGLLSCGVSVDREQH--SSGCVRGFNHACGWF 154
Cdd:cd08906    78 WNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKppLSKYVRGENGPGGFV 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207159053 155 CVP-TDDPSLSLLTGYIQTDLRGHLPRAAVDTAMASGLITFFSDLQRAL 202
Cdd:cd08906   158 VLKsASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRI 206
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 21-204 1.46e-06

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: 47.14  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053  21 QLEDADWRLSKRSKDVsvwqrasqefsGSLYKAQGRVRGDPQQIVDFLRPGARRL-DWDSMMTSMEILETPEQGCCVVKY 99
Cdd:cd08905    32 VAENGDKVLSKVVPDI-----------GKVFRLEVVVDQPLDNLYSELVDRMEQMgEWNPNVKEVKILQRIGKDTLITHE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207159053 100 TTSGQLWNIISPREFVDFSYTseCERG--LLSCGVSVDR----EQhsSGCVRGFNH-ACGWFCVPTDDPSLSLLTGYIQT 172
Cdd:cd08905   101 VAAETAGNVVGPRDFVSVRCA--KRRGstCVLAGMATHFglmpEQ--KGFIRAENGpTCIVLRPLAGDPSKTKLTWLLSI 176

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1207159053 173 DLRGHLPRAAVDTAMASGLITFFSDLQRALDA 204
Cdd:cd08905   177 DLKGWLPKSIINQVLSQTQVDFANHLRQRMAS 208
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 23-89 1.08e-04

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: 41.49  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207159053  23 EDADWRLSKRSKDVSVWQRASQEFSGSLYKAQGRVRGDPQQIVDFLRPGARRLDWDSMMTSMEILET 89
Cdd:cd08876    15 PDGDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDASIEAFLALLRDTESYPQWMPNCKESRVLKR 81
 
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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