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Conserved domains on  [gi|1831511535|ref|NP_001366874|]
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START domain-containing protein [Caenorhabditis elegans]

Protein Classification

START domain-containing protein( domain architecture ID 10172287)

START (steroidogenic acute regulatory protein (StAR)-related lipid transfer) domain-containing protein may bind lipids; similar to STARD10 that may play metabolic roles in sperm maturation or fertilization

CATH:  3.30.530.20
Gene Ontology:  GO:0008289
PubMed:  10322415|31927098
SCOP:  4002052

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-223 7.82e-124

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: 351.56  E-value: 7.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   3 VNVARVWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYM 82
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  83 IKQETIGTINPNNDVCYYSLNSVSPIRPRDFVMQRSWLETDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEK-EQ 161
Cdd:cd08871    81 IESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTgPK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511535 162 GCEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKLHKACLGYPEWKEKHHPTWKPWSVPEQ 223
Cdd:cd08871   161 GCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-223 7.82e-124

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: 351.56  E-value: 7.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   3 VNVARVWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYM 82
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  83 IKQETIGTINPNNDVCYYSLNSVSPIRPRDFVMQRSWLETDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEK-EQ 161
Cdd:cd08871    81 IESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTgPK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511535 162 GCEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKLHKACLGYPEWKEKHHPTWKPWSVPEQ 223
Cdd:cd08871   161 GCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START pfam01852
START domain;
7-208 4.13e-71

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 217.27  E-value: 4.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   7 RVWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQE 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  87 TIGTINPNNDVCYYSLNSV--SPIRPRDFVMQRSWLE-TDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG- 162
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVapSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGp 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831511535 163 CEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKlHKACLGYPEWK 208
Cdd:pfam01852 161 SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKT-WVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-208 1.40e-61

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 193.03  E-value: 1.40e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535    8 VWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIE--KSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQ 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   86 ETIGTINPNNDVCYYSLNSV-SPIRPRDFVMQRSWLE-TDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG- 162
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAaGPVSPRDFVFVRYWREdEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGp 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1831511535  163 CEVIYISHSDPKGKLPTWLVnRVTKVVAPKVIKKLHKACLGYPEWK 208
Cdd:smart00234 161 SKVTWVSHADLKGWLPHWLV-RSLIKSGLAEFAKTLVATLQKHCAK 205
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-223 7.82e-124

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: 351.56  E-value: 7.82e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   3 VNVARVWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYM 82
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  83 IKQETIGTINPNNDVCYYSLNSVSPIRPRDFVMQRSWLETDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEK-EQ 161
Cdd:cd08871    81 IESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTgPK 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511535 162 GCEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKLHKACLGYPEWKEKHHPTWKPWSVPEQ 223
Cdd:cd08871   161 GCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START pfam01852
START domain;
7-208 4.13e-71

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 217.27  E-value: 4.13e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   7 RVWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQE 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  87 TIGTINPNNDVCYYSLNSV--SPIRPRDFVMQRSWLE-TDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG- 162
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVapSPLSPRDFVFLRYWRRlGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGp 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1831511535 163 CEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKlHKACLGYPEWK 208
Cdd:pfam01852 161 SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKT-WVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-208 1.40e-61

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 193.03  E-value: 1.40e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535    8 VWEDSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIE--KSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQ 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535   86 ETIGTINPNNDVCYYSLNSV-SPIRPRDFVMQRSWLE-TDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG- 162
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAaGPVSPRDFVFVRYWREdEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGp 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1831511535  163 CEVIYISHSDPKGKLPTWLVnRVTKVVAPKVIKKLHKACLGYPEWK 208
Cdd:smart00234 161 SKVTWVSHADLKGWLPHWLV-RSLIKSGLAEFAKTLVATLQKHCAK 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 11-202 4.96e-48

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: 157.89  E-value: 4.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  11 DSDYEKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPdVSATVVYDVLHDSAYRAKWDKYMIKQETIGT 90
Cdd:cd00177     1 EEAIEELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIP-ASPEQVFELLMDIDLRKKWDKNFEEFEVIEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  91 INPNNDVCYYSLNSVSPIRPRDFVMQRSWLETDKDR-LICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG-CEVIYI 168
Cdd:cd00177    80 IDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGTyVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGkTKVTYV 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1831511535 169 SHSDPKGKLPTWLVNRVTKVVAPKVIKKLHKACL 202
Cdd:cd00177   160 LQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 25-199 1.93e-20

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: 86.17  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  25 EGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLpDVSATVVYDVLHDSAYRAKWDKYMIKQETIGTINPNNDVCYYSLNS 104
Cdd:cd08876    17 GDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEV-DASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSVYTVIDL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 105 VSPIRPRDFVMqRSWLETDKDRL-ICSHSVCHEDYPPA-KGCIRATVLiSGYLIKEKEQG--CEVIYISHSDPKGKLPTW 180
Cdd:cd08876    96 PWPVKDRDMVL-RSTTEQDADDGsVTITLEAAPEALPEqKGYVRIKTV-EGQWTFTPLGNgkTRVTYQAYADPGGSIPGW 173

                         170
                  ....*....|....*....
gi 1831511535 181 LVNRVTKVVAPKVIKKLHK 199
Cdd:cd08876   174 LANAFAKDAPYNTLENLRK 192
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 23-204 4.12e-15

Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may have a mitochondrial function.


Pssm-ID: 176919  Cd Length: 207  Bit Score: 72.14  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  23 DSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKY---MIKQETIGtinpnNDVCY 99
Cdd:cd08910    23 DGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYvkeLYEKECDG-----ETVIY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 100 YSLNSVSPIRPRDFVMQRSWLETD----KDRLICSHSVCHEDYPPAKGCIRatvlISGYLIK-----EKEQGCEVIYISH 170
Cdd:cd08910    98 WEVKYPFPLSNRDYVYIRQRRDLDvegrKIWVILARSTSLPQLPEKPGVIR----VKQYKQSlaiesDGKKGSKVFMYYF 173

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1831511535 171 SDPKGKLPTWLVNRVTKVVAPKVIKKLHKACLGY 204
Cdd:cd08910   174 DNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 22-204 1.48e-14

Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176920  Cd Length: 207  Bit Score: 70.40  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  22 EDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQETIGT-INPNNDVCYY 100
Cdd:cd08911    18 QEPDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEdPETGSEIIYW 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 101 SLNSVSPIRPRDFVMQRSWLETDKDRL--ICSHSVCHEDYPPAKGCIRATVLISGYLIKE----KEQGCEVIYISHSDPK 174
Cdd:cd08911    98 EMQWPKPFANRDYVYVRRYIIDEENKLivIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPhksfDEPGFEFVLTYFDNPG 177

                         170       180       190
                  ....*....|....*....|....*....|
gi 1831511535 175 GKLPTWLVNRVTKVVAPKVIKKLHKACLGY 204
Cdd:cd08911   178 VNIPSYITSWVAMSGMPDFLERLRNAALKY 207
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 75-180 1.86e-13

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: 67.33  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  75 RAKWDKYMIKQETIGTINPNNDVCYYSLNSVSPIRPRDFVMQRSWlETDKDRLIC---SHSVCHEDYPPAKGcIRATVLI 151
Cdd:cd08869    67 RHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTW-RTDLPKGACvlvETSVEHTEPVPLGG-VRAVVLA 144

                          90       100       110
                  ....*....|....*....|....*....|
gi 1831511535 152 SGYLIKEKEQG-CEVIYISHSDPKGKLPTW 180
Cdd:cd08869   145 SRYLIEPCGSGkSRVTHICRVDLRGRSPEW 174
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 10-185 6.16e-13

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup 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) 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. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 66.10  E-value: 6.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  10 EDSDYEKVKNLCEDSEGWVEVYKKKDITI-CTQNIEKSSYQMIKAIAQLPDVSATVVYDVLHDsayRAKWDKYMIKQETI 88
Cdd:cd08907    12 EDNVQCLLREASERFKGWHSAPGPDNTELaCKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRE---RHLWDEDLLHSQVI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  89 GTINPNNDVCYYSLNSVSPIRPRDFVMQRSWlETDKDRLIC---SHSVCHEDYPPAKGcIRATVLISGYLIKEKEQG-CE 164
Cdd:cd08907    89 EALENNTEVYHYVTDSMAPHPRRDFVVLRMW-RSDLPRGGCllvSQSVDHDNPQLEAG-VRAVLLTSQYLIEPCGMGrSR 166

                         170       180
                  ....*....|....*....|.
gi 1831511535 165 VIYISHSDPKGKLPTWLvNRV 185
Cdd:cd08907   167 LTHICRADLRGRSPDWY-NKV 186
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 22-180 2.03e-12

C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) 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. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176918  Cd Length: 205  Bit Score: 64.55  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  22 EDSEGWVEVYKKKDITICTQNI-EKSSYQMIKAIAQLPDVSATVVYDVLHDsayRAKWDKYMIKQETIGTINPNNDVCYY 100
Cdd:cd08909    24 EKFKGWISCSSSDNTELAYKKVgDGNPLRLWKVSVEVEAPPSVVLNRVLRE---RHLWDEDFLQWKVVETLDKQTEVYQY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 101 SLNSVSPIRPRDFVMQRSWlETDKDRLIC---SHSVCHEDYPPAkGCIRATVLISGYLIKEKEQG-CEVIYISHSDPKGK 176
Cdd:cd08909   101 VLNCMAPHPSRDFVVLRSW-RTDLPKGACslvSVSVEHEEAPLL-GGVRAVVLDSQYLIEPCGSGkSRLTHICRVDLKGH 178


                  ....
gi 1831511535 177 LPTW 180
Cdd:cd08909   179 SPEW 182
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 23-182 3.83e-11

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: 60.94  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  23 DSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVYDVL-HDSAYRAKWDKYMIKQETIGTINPNNDVCYYS 101
Cdd:cd08867    20 DTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIpPCGGLRLKWDKSLKHYEVLEKISEDLCVGRTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 102 LNS--VSPIRPRDFVmQRSWLETDKDR--LICSHSVCHEDYPPAKGCIRATVLISGYL---IKEKEQGCEVIYISHSDPK 174
Cdd:cd08867   100 TPSaaMGLISPRDFV-DLVYVKRYEDNqwSSSGKSVDIPERPPTPGFVRGYNHPCGYFcspLKGSPDKSFLVLYVQTDLR 178


                  ....*...
gi 1831511535 175 GKLPTWLV 182
Cdd:cd08867   179 GMIPQSLV 186
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 11-204 2.46e-10

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. 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. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176882  Cd Length: 235  Bit Score: 59.15  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  11 DSDYEKVKNLCEDSeGWVEVYKKKDITICTQNIEKS-SYQMIKAiaqlPDVSATVVYDVLHDSAYRAKWDKYMIKQETIG 89
Cdd:cd08873    42 YGNVTALKRLAAKS-DWTVASSTTSVTLYTLEQDGVlSFCVELK----VQTCASDAFDLLSDPFKRPEWDPHGRSCEEVK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  90 TINPNNDVCYYSLNSVSPIRPRDFVM---QRSWLETDKDRLICSHSVCHEDYPPAKGCIRATVLISGYLI-KEKEQGCEV 165
Cdd:cd08873   117 RVGEDDGIYHTTMPSLTSEKPNDFVLlvsRRKPATDGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVIrQDCGTCTEV 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1831511535 166 IYISHSDPKgklptwLVNRVTKVVA--PKVIKKLHKACLGY 204
Cdd:cd08873   197 SYYNETNPK------LLSYVTCNLAglSALYCRTFHCCEQF 231
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 18-195 3.74e-10

C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) 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. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176917  Cd Length: 204  Bit Score: 58.10  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  18 KNLCEDSEGWVEVYKKKDITICTQNI-EKSSYQMIKAIAQLPDVSATVVYDVLHDSAYrakWDKYMIKQETIGTINPNND 96
Cdd:cd08908    20 KEVKEKFKGWVSYSTSEQAELSYKKVsEGPPLRLWRTTIEVPAAPEEILKRLLKEQHL---WDVDLLDSKVIEILDSQTE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  97 VCYYSLNSVSPIRPRDFVMQRSWlETDKDRLICS---HSVCHeDYPPAKGcIRATVLISGYLIKEKEQG-CEVIYISHSD 172
Cdd:cd08908    97 IYQYVQNSMAPHPARDYVVLRTW-RTNLPKGACAllaTSVDH-DRAPVAG-VRVNVLLSRYLIEPCGSGkSKLTYMCRID 173

                         170       180
                  ....*....|....*....|...
gi 1831511535 173 PKGKLPTWLVNRVTKVVAPKVIK 195
Cdd:cd08908   174 LRGHMPEWYTKSFGHLCAAEVVK 196
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 22-204 6.50e-10

Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of PtdCho to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers. It showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176879  Cd Length: 209  Bit Score: 57.39  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  22 EDSEGWVEVYKKKDITICTQ----NIEKSSYQMIKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQETIgTINPNN-- 95
Cdd:cd08870    19 AEGQAWQQVMDKSTPDMSYQawrrKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDETVIEHETL-EEDEKSgt 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  96 DVCYYSLNSVSPIRPRDFVMQRSWLETDKDRLICSHSVCheDYP--PAKGCIRATVLISGYLIKEKEQG-----CEVIYI 168
Cdd:cd08870    98 EIVRWVKKFPFPLSDREYVIARRLWESDDRSYVCVTKGV--PYPsvPRSGRKRVDDYESSLVIRAVKGDgqgsaCEVTYF 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1831511535 169 SHsdPKGKLPTWLVNRVTKVVAPKVIKKLHKACLGY 204
Cdd:cd08870   176 HN--PDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 59-201 1.17e-09

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: 56.59  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  59 DVSATVVYDVLHDSAYRAK-WDKYMIKQETIGTINPNNDVCYY----SLNSVspIRPRDFVMQRSWLETDKDRLICSHSV 133
Cdd:cd08868    57 DCPAEFLYNELVLNVESLPsWNPTVLECKIIQVIDDNTDISYQvaaeAGGGL--VSPRDFVSLRHWGIRENCYLSSGVSV 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831511535 134 CHEDYPPAKGCIRATVLISGYLIKEK---EQGCEVIYISHSDPKGKLPTWLVNRVTKVVAPKVIKKLHKAC 201
Cdd:cd08868   135 EHPAMPPTKNYVRGENGPGCWILRPLpnnPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRI 205
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 11-178 4.48e-08

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) 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. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 52.59  E-value: 4.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  11 DSDYEKVKNLCEDSeGWVEVYKKKDITICTqnIEKSSYQMIKAIAQLpDVSATVVYDVLHDSAYRAKWDKYMIKQETIGT 90
Cdd:cd08914    43 DSNVEALKKLAAKS-GWEVTSTVEKIKIYT--LEEHDVLSVWVEKHV-KRPAHLAYRLLSDFTKRPLWDPHFLSCEVIDW 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  91 INPNNDVCYYSLNSVSPIRPRDFVMQRSWLETDKD---RLICSHSVCHEDYPPAKGCIRATVLISGYLIKEKEQG-CEVI 166
Cdd:cd08914   119 VSEDDQIYHITCPIVNNDKPKDLVVLVSRRKPLKDgntYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNsCTVS 198

                         170
                  ....*....|..
gi 1831511535 167 YISHSDPkGKLP 178
Cdd:cd08914   199 YFNQISA-SILP 209
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 15-178 2.18e-07

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: 50.29  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  15 EKVKNLCEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVyDVLHDSAYRAKWDKYMIKQETIGTINPN 94
Cdd:cd08904    12 QEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLI-QFMYQPEHRIKWDKSLQVYKMLQRIDSD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  95 NDVCYYSLNS--VSPIRPRDFV--MQRSWLETDKDrLICSHSVCHEDYPPAKGCIRATVLISGYL---IKEKEQGCEVIY 167
Cdd:cd08904    91 TFICHTITQSfaMGSISPRDFVdlVHIKRYEGNMN-IVSSVSVEYPQCPPSSNYIRGYNHPCGYVcspLPENPAYSKLVM 169

                         170
                  ....*....|.
gi 1831511535 168 ISHSDPKGKLP 178
Cdd:cd08904   170 FVQPELRGNLS 180
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 51-197 2.80e-07

Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD11 and related domains. 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. STARD11 can mediate transfer of the natural ceramide isomers, dihydroceramide and phytoceramide, as well as ceramides having C14, C16, C18, and C20 chains. They can also transfer diacylglycerol, but with a lower efficiency. STARD11 is synthesized from two major transcripts: a larger one encoding Goodpasture antigen-binding protein (GPBP)/ceramide transporter long form (CERTL); and a smaller one encoding GPBPdelta26/CERT, which is deleted for 26 amino acids. Both splicing variants mediate ceramide transfer from the ER to the Golgi, in a non-vesicular manner. It is likely that these two carry out different functions in specific sub-cellular locations. These proteins have roles in brain homeostasis and disease processes. GPBP/CERTL exists in multiple isoforms originating from alternative translation initiation sites and post-translational modifications. Goodpasture syndrome is a human disorder caused by antibodies directed against the a3-chain of collagen type IV. GPBP/CERTL binds and phosphorylates this antigen. The human gene encoding STARD11 is referred to as COL4A3BP referring to its collagen binding function. It is unknown whether the ceramide-transfer function of GPBP/CERTL is related to this collagen interaction. The expression of GPBP/CERTL is elevated in these and other spontaneous autoimmune disorders including cutaneous lupus erythematosus, pemphigoid, and lichen planus. GPBL/CERTL contains an N-terminal pleckstrin homology domain (PH), which targets the protein to the Golgi, a middle region containing two serine-rich domains (SR1, SR2), a FFAT (two phenylalanine amino acids in an acidic tract) motif which is involved in endoplasmic reticulum targeting, and this C-terminal SMART domain. The shorter splicing variant, CERT, lacks the SR2 domain.


Pssm-ID: 176881  Cd Length: 235  Bit Score: 50.03  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  51 IKAIAQLPDVSATVVYDVLHDSAYRAKWDKYMIKQETIGTINPNNDVCYYSLNSVSPIRPRD--FV--MQRSWLETDKDR 126
Cdd:cd08872    54 LKATHAVKGVTGHEVCHYFFDPDVRMDWETTLENFHVVETLSQDTLIFHQTHKRVWPAAQRDalFVshIRKIPALEEPNA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535 127 ----LICSHSVCHEDYPPAKGCIRATVLIS------------GYLIKEKEQGCEVIYISHSDPKGKLPTWLVNRVTKVVA 190
Cdd:cd08872   134 hdtwIVCNFSVDHDSAPLNNKCVRAKLTVAmicqtfvsppdgNQEITRDNILCKITYVANVNPGGWAPASVLRAVYKREY 213


                  ....*..
gi 1831511535 191 PKVIKKL 197
Cdd:cd08872   214 PKFLKRF 220
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 50-184 2.20e-04

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: 41.39  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  50 MIKAIAQLPdvsATVVY-DVLHDSAYRAKWDKYMIKQETIGTINPNNDVCY--YSLNSVSPIRPRDFVMQRSwLETDKDR 126
Cdd:cd08906    52 ILKAFMQCP---AELVYqEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYdvAAGAAGGVVSPRDFVNVRR-IERRRDR 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831511535 127 LICSH-SVCHEDYPPAKGCIRATVLISGYLIKEKEQG---CEVIYISHSDPKGKLPTWLVNR 184
Cdd:cd08906   128 YVSAGiSTTHSHKPPLSKYVRGENGPGGFVVLKSASNpsvCTFIWILNTDLKGRLPRYLIHQ 189
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 21-146 1.21e-03

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: 39.17  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511535  21 CEDSEGWVEVYKKKDITICTQNIEKSSYQMIKAIAQLPDVSATVVyDVLHDSAYRAKWDKYMIKQETIGTINPNNDVCYY 100
Cdd:cd08902    19 SILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIV-DHIRPGPYRLDWDSLMTSMDIIEEFEENCCVMRY 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511535 101 S-----LNSVSpirPRDFVMQRSWLETDKDRLICSHSVCHEDYPPakGCIR 146
Cdd:cd08902    98 TtagqlLNIIS---PREFVDFSYTTQYEDGLLSCGVSIEYEEARP--NFVR 143
 
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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