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Conserved domains on  [gi|292618146|ref|XP_692994|]
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stAR-related lipid transfer protein 7, mitochondrial [Danio rerio]

Protein Classification

StAR-related lipid transfer protein 7( domain architecture ID 10172361)

mitochondrial StAR-related lipid transfer protein 7 (STARD7) may play a protective role in mucosal tissues by preventing exaggerated allergic responses

CATH:  3.30.530.20
Gene Symbol:  STARD7
Gene Ontology:  GO:0008289
PubMed:  31927098|18922149|10322415|11276083
SCOP:  4002052

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 175-362 7.17e-121

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: 348.90  E-value: 7.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRDVNTGTEVVHWAT 254
Cdd:cd08911   20 PDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPETGSEIIYWEM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 255 HFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPHRSFDENGFDYLLTYSDDPQTV 334
Cdd:cd08911  100 QWPKPFANRDYVYVRRYIIDEENKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPHKSFDEPGFEFVLTYFDNPGVN 179

                        170       180
                 ....*....|....*....|....*...
gi 292618146 335 FPRYCVSWMVSSGMPDFLEKLHTAALRA 362
Cdd:cd08911  180 IPSYITSWVAMSGMPDFLERLRNAALKY 207
 
Name Accession Description Interval E-value
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 175-362 7.17e-121

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: 348.90  E-value: 7.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRDVNTGTEVVHWAT 254
Cdd:cd08911   20 PDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPETGSEIIYWEM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 255 HFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPHRSFDENGFDYLLTYSDDPQTV 334
Cdd:cd08911  100 QWPKPFANRDYVYVRRYIIDEENKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPHKSFDEPGFEFVLTYFDNPGVN 179

                        170       180
                 ....*....|....*....|....*...
gi 292618146 335 FPRYCVSWMVSSGMPDFLEKLHTAALRA 362
Cdd:cd08911  180 IPSYITSWVAMSGMPDFLERLRNAALKY 207
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 177-362 2.40e-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: 90.95  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146   177 GWEVVMEKKNFRVWRR--PVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHWAT 254
Cdd:smart00234  19 GWVLSSENENGDEVRSifSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAETLEV-IDNGTVIYHYVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146   255 HFPY-PMYSRDYVYVRRYQVDlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPhrsfDENG---FDYLltYSDD 330
Cdd:smart00234  98 KFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEP----LGNGpskVTWV--SHAD 170

                          170       180       190
                   ....*....|....*....|....*....|..
gi 292618146   331 PQTVFPRYCVSWMVSSGMPDFLeKLHTAALRA 362
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFA-KTLVATLQK 201
START pfam01852
START domain;
177-361 2.98e-19

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 85.15  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146  177 GWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHW--AT 254
Cdd:pfam01852  20 GWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEV-ISSGGDLQYYvaAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146  255 HFPYPMYSRDYVYVRRYQVDlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPhrsfDENG---FDYLltYSDDP 331
Cdd:pfam01852  99 VAPSPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP----CGNGpskVTWV--SHADL 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 292618146  332 QTVFPRYCVSWMVSSGMPDFLeKLHTAALR 361
Cdd:pfam01852 172 KGWLPSWLLRSLYKSGMPEGA-KTWVATLQ 200
 
Name Accession Description Interval E-value
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 175-362 7.17e-121

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: 348.90  E-value: 7.17e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRDVNTGTEVVHWAT 254
Cdd:cd08911   20 PDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPETGSEIIYWEM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 255 HFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPHRSFDENGFDYLLTYSDDPQTV 334
Cdd:cd08911  100 QWPKPFANRDYVYVRRYIIDEENKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPHKSFDEPGFEFVLTYFDNPGVN 179

                        170       180
                 ....*....|....*....|....*...
gi 292618146 335 FPRYCVSWMVSSGMPDFLEKLHTAALRA 362
Cdd:cd08911  180 IPSYITSWVAMSGMPDFLERLRNAALKY 207
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 175-362 3.69e-71

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: 222.25  E-value: 3.69e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKN----FRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRDVNTGTEVV 250
Cdd:cd08870   21 GQAWQQVMDKSTpdmsYQAWRRKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDETVIEHETLEEDEKSGTEIV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 251 HWATHFPYPMYSRDYVYVRRYQvDLENNLMILVSRAVKHPCVPEtQEFVRVHSYQSKMVIRPHRsFDENGFDYLLTYSDD 330
Cdd:cd08870  101 RWVKKFPFPLSDREYVIARRLW-ESDDRSYVCVTKGVPYPSVPR-SGRKRVDDYESSLVIRAVK-GDGQGSACEVTYFHN 177

                        170       180       190
                 ....*....|....*....|....*....|..
gi 292618146 331 PQTVFPRYCVSWMVSSGMPDFLEKLHTAALRA 362
Cdd:cd08870  178 PDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 178-361 1.38e-32

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: 121.83  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 178 WEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLdvVDRDVNtGTEVVHWATHFP 257
Cdd:cd08910   27 WELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKEL--YEKECD-GETVIYWEVKYP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 258 YPMYSRDYVYVR-RYQVDLE-NNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIrphRSFDENGFDYLLTYSDDPQTVF 335
Cdd:cd08910  104 FPLSNRDYVYIRqRRDLDVEgRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAI---ESDGKKGSKVFMYYFDNPGGMI 180

                        170       180
                 ....*....|....*....|....*.
gi 292618146 336 PRYCVSWMVSSGMPDFLEKLHTAALR 361
Cdd:cd08910  181 PSWLINWAAKNGVPNFLKDMQKACQN 206
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 175-361 2.22e-25

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: 102.72  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVI-RLDVVDRDVNtgTEVVHWA 253
Cdd:cd08871   22 TDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNMIeSFDICQLNPN--NDIGYYS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 254 THFPYPMYSRDYVYVRRYQVdlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPhrsFDENGfdYLLTY--SDDP 331
Cdd:cd08871  100 AKCPKPLKNRDFVNLRSWLE--FGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRP---TGPKG--CTLTYvtQNDP 172

                        170       180       190
                 ....*....|....*....|....*....|
gi 292618146 332 QTVFPRYCVSWMVSSGMPDFLEKLHTAALR 361
Cdd:cd08871  173 KGSLPKWVVNKATTKLAPKVMKKLHKAALK 202
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 175-313 8.60e-23

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: 94.71  E-value: 8.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSyTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDrDVNTGTEVVHWAT 254
Cdd:cd00177   14 PEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGV-IPASPEQVFELLMDIDLRKKWDKNFEEFEVIE-EIDEHTDIIYYKT 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 292618146 255 HFPYPMYSRDYVYVRrYQVDLENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPH 313
Cdd:cd00177   92 KPPWPVSPRDFVYLR-RRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPL 149
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 177-362 2.40e-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: 90.95  E-value: 2.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146   177 GWEVVMEKKNFRVWRR--PVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHWAT 254
Cdd:smart00234  19 GWVLSSENENGDEVRSifSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAETLEV-IDNGTVIYHYVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146   255 HFPY-PMYSRDYVYVRRYQVDlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPhrsfDENG---FDYLltYSDD 330
Cdd:smart00234  98 KFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEP----LGNGpskVTWV--SHAD 170

                          170       180       190
                   ....*....|....*....|....*....|..
gi 292618146   331 PQTVFPRYCVSWMVSSGMPDFLeKLHTAALRA 362
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFA-KTLVATLQK 201
START pfam01852
START domain;
177-361 2.98e-19

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 85.15  E-value: 2.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146  177 GWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHW--AT 254
Cdd:pfam01852  20 GWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEV-ISSGGDLQYYvaAL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146  255 HFPYPMYSRDYVYVRRYQVDlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPhrsfDENG---FDYLltYSDDP 331
Cdd:pfam01852  99 VAPSPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP----CGNGpskVTWV--SHADL 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 292618146  332 QTVFPRYCVSWMVSSGMPDFLeKLHTAALR 361
Cdd:pfam01852 172 KGWLPSWLLRSLYKSGMPEGA-KTWVATLQ 200
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 175-305 2.55e-16

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: 76.54  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGsYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRDVNTGTeVVHWAT 254
Cdd:cd08876   16 DGDWQLVKDKDGIKVYTRDVEGSPLKEFKAVA-EVDASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNER-SVYTVI 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 292618146 255 HFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPCvPETQEFVRVHSYQ 305
Cdd:cd08876   94 DLPWPVKDRDMVLRSTTEQDADDGSVTITLEAAPEAL-PEQKGYVRIKTVE 143
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 177-304 2.88e-09

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: 56.70  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 177 GWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSyTDVTPRQFFNV--QLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHWAT 254
Cdd:cd08867   23 GWKVLKTVKNITVSWKPSTEFTGHLYRAEGI-VDALPEKVIDViiPPCGGLRLKWDKSLKHYEVLEK-ISEDLCVGRTIT 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 292618146 255 H-FPYPMYS-RDYV---YVRRYqvdlENNLMILVSRAVKHPCVPETQEFVRVHSY 304
Cdd:cd08867  101 PsAAMGLISpRDFVdlvYVKRY----EDNQWSSSGKSVDIPERPPTPGFVRGYNH 151
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 262-355 1.12e-06

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: 48.89  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 262 SRDYVYVRRYQVdlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRPHRSF-DENGFDYLLtySDDPQTVFPRYCV 340
Cdd:cd08868  111 PRDFVSLRHWGI--RENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNpNKCNFTWLL--NTDLKGWLPQYLV 186

                         90
                 ....*....|....*
gi 292618146 341 SWMVSSGMPDFLEKL 355
Cdd:cd08868  187 DQALASVLLDFMKHL 201
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 177-312 1.64e-06

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: 48.37  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 177 GWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDvTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHWATHf 256
Cdd:cd08904   23 GWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPE-SPAKLIQFMYQPEHRIKWDKSLQVYKMLQR-IDSDTFICHTITQ- 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 292618146 257 PYPMYS---RDY---VYVRRYqvdlENNLMILVSRAVKHPCVPETQEFVRVHSYQSKMVIRP 312
Cdd:cd08904  100 SFAMGSispRDFvdlVHIKRY----EGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSP 157
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 226-312 8.13e-05

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: 43.45  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 226 RKKWDALVIRLDVVDRdVNTGTEVVHWATHFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPC-VPETQefVRVHSY 304
Cdd:cd08869   67 RHLWDDDLLQWKVVET-LDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGACVLVETSVEHTEpVPLGG--VRAVVL 143


                 ....*...
gi 292618146 305 QSKMVIRP 312
Cdd:cd08869  144 ASRYLIEP 151
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 226-312 1.05e-04

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: 42.99  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 226 RKKWDALVIRLDVVDRdVNTGTEVVHWATHFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPcVPETQEFVRVHSYQ 305
Cdd:cd08907   75 RHLWDEDLLHSQVIEA-LENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHD-NPQLEAGVRAVLLT 152


                 ....*..
gi 292618146 306 SKMVIRP 312
Cdd:cd08907  153 SQYLIEP 159
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 175-240 1.29e-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: 39.94  E-value: 1.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVEGSHLFEYRVFGSYTDVTPRQFFNVQlDTEYRKKWDALVIRLDVVD 240
Cdd:cd08902   22 EEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIR-PGPYRLDWDSLMTSMDIIE 86
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 175-301 1.33e-03

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: 40.02  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 175 DQGWEVVMEKKNFRVWRRPVE--GSHLFEYRVFGSYTDVTPRQFFNVQLDTEYRKKWDALVIRLDVVDRdVNTGTEVVHW 252
Cdd:cd08872   25 ADGWQLFAEEGEMKVYRREVEedGVVLDPLKATHAVKGVTGHEVCHYFFDPDVRMDWETTLENFHVVET-LSQDTLIFHQ 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 292618146 253 ATHFPYPMYSRDYVYVR--RYQVDLEN----NLMILVSRAVKHPCVPETQEFVRV 301
Cdd:cd08872  104 THKRVWPAAQRDALFVShiRKIPALEEpnahDTWIVCNFSVDHDSAPLNNKCVRA 158
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 166-312 2.97e-03

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: 38.84  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292618146 166 VSPKVATHVDQGWEVVMEKKNFRVWRRPVEgshlfeyrvfgsyTDVTPRQFFNVQLDTEYRkkWDALVIRLDVVDrDVNT 245
Cdd:cd08908   30 VSYSTSEQAELSYKKVSEGPPLRLWRTTIE-------------VPAAPEEILKRLLKEQHL--WDVDLLDSKVIE-ILDS 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 292618146 246 GTEVVHWATHFPYPMYSRDYVYVRRYQVDLENNLMILVSRAVKHPCVPETQefVRVHSYQSKMVIRP 312
Cdd:cd08908   94 QTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRAPVAG--VRVNVLLSRYLIEP 158
 
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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