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Conserved domains on  [gi|10946984|ref|NP_067522|]
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stAR-related lipid transfer protein 3 isoform 1 [Mus musculus]

Protein Classification

stAR-related lipid transfer protein 3( domain architecture ID 10564579)

stAR-related lipid transfer protein 3 (STARD3) is a sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes

CATH:  3.30.530.20
Gene Symbol:  STARD3
Gene Ontology:  GO:0015485|GO:0120020|GO:0030301
PubMed:  28377464|31927098|10322415|11276083|15718238
SCOP:  4002052

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 234-442 5.54e-141

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: 401.93  E-value: 5.54e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 234 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 313
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 314 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 393
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 10946984 394 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 442
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-214 3.40e-89

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


:

Pssm-ID: 463097  Cd Length: 177  Bit Score: 268.77  E-value: 3.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    48 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEVIHYSFQSSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIA 126
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   127 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QAAVARGPLLFSGA- 202
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 10946984   203 -----LSEGQFYSPPES 214
Cdd:pfam10457 161 grsnnQSDGNFYSPPES 177
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 234-442 5.54e-141

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: 401.93  E-value: 5.54e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 234 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 313
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 314 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 393
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 10946984 394 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 442
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-214 3.40e-89

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 268.77  E-value: 3.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    48 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEVIHYSFQSSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIA 126
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   127 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QAAVARGPLLFSGA- 202
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 10946984   203 -----LSEGQFYSPPES 214
Cdd:pfam10457 161 grsnnQSDGNFYSPPES 177
START pfam01852
START domain;
240-445 1.30e-64

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 206.48  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   240 IRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 319
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   320 ILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNP 398
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 10946984   399 rvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 445
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 241-445 3.76e-56

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 184.56  E-value: 3.76e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    241 RQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 318
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    319 QILQRVEDNTLVSYDVSSGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANN 397
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 10946984    398 PrvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 445
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 234-442 5.54e-141

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: 401.93  E-value: 5.54e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 234 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 313
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 314 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 393
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 10946984 394 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 442
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 234-442 2.82e-101

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: 300.81  E-value: 2.82e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 234 AQEREYIRQGKEATAVVDQILAQEeNWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 313
Cdd:cd08868   1 SQELEYLKQGAEALARAWSILTDP-GWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 314 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 393
Cdd:cd08868  80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 10946984 394 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 442
Cdd:cd08868 160 LPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-214 3.40e-89

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 268.77  E-value: 3.40e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    48 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEVIHYSFQSSFFDIFVLAFFRFSGLLLGYAVLRLQHWWVIA 126
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   127 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QAAVARGPLLFSGA- 202
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 10946984   203 -----LSEGQFYSPPES 214
Cdd:pfam10457 161 grsnnQSDGNFYSPPES 177
START pfam01852
START domain;
240-445 1.30e-64

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 206.48  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   240 IRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 319
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984   320 ILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNP 398
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 10946984   399 rvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 445
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 241-445 3.76e-56

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 184.56  E-value: 3.76e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    241 RQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 318
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984    319 QILQRVEDNTLVSYDVSSGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANN 397
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 10946984    398 PrvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 445
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 235-439 9.82e-50

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


Pssm-ID: 176914  Cd Length: 209  Bit Score: 168.09  E-value: 9.82e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 235 QEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKT 314
Cdd:cd08905   2 AEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 315 VTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKS 394
Cdd:cd08905  82 VKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPL 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 10946984 395 ANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRV 439
Cdd:cd08905 162 AGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRM 206
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 244-437 1.38e-28

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: 111.28  E-value: 1.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 244 KEATAVVDQILAQEENWKFERSNEyGDTVYTIEVPFHGKTFI-LKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQ 322
Cdd:cd00177   1 EEAIEELLELLEEPEGWKLVKEKD-GVKIYTKPYEDSGLKLLkAEGVIPASPEQVF-ELLMDIDLRKKWDKNFEEFEVIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 323 RVEDNTLVSYDVSSgaAGGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNprVC 401
Cdd:cd00177  79 EIDEHTDIIYYKTK--PPWPVSPRDFVYLRRRRKLDDgTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPG--KT 154

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 10946984 402 TFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQ 437
Cdd:cd00177 155 KVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRK 190
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 257-439 4.39e-21

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: 90.98  E-value: 4.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 257 EENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYqEVILQP---ERmVLWNKTVTACQILQRVEDNTLVSYD 333
Cdd:cd08867  21 TDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVI-DVIIPPcggLR-LKWDKSLKHYEVLEKISEDLCVGRT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 334 VSSGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLK 412
Cdd:cd08867  99 ITPSAAMGLISPRDFVDlVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLR 178

                       170       180
                ....*....|....*....|....*..
gi 10946984 413 GRLPRYLIHQSLGATMFEFAFHLRQRV 439
Cdd:cd08867 179 GMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 279-431 7.84e-17

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: 78.80  E-value: 7.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 279 FHGKTFILKTFLP-CPAELVyqEVILQPERMVLWNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVN-VRRIER 356
Cdd:cd08904  43 YHGNLYRVEGIIPeSPAKLI--QFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDlVHIKRY 120

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10946984 357 RRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEF 431
Cdd:cd08904 121 EGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNL 195
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 246-442 8.99e-14

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


Pssm-ID: 176912  Cd Length: 208  Bit Score: 69.87  E-value: 8.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 246 ATAVVDQILA---QEENWKF-ERSNEYgdTVY-TIEVPFHGKTFILKTFLPCPAELVYQevILQPER---MVLWNKTVTA 317
Cdd:cd08903   7 AESVADKMLLyrrDESGWKTcRRTNEV--AVSwRPSAEFAGNLYKGEGIVYATLEQVWD--CLKPAAgglRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 318 CQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGiAT--THCSKPPTHKYVRGENGPGGFIVLKSA 395
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSN-ATnvEHPLCPPQAGFVRGFNHPCGCFCEPVP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 10946984 396 NNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 442
Cdd:cd08903 162 GEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 311-437 1.17e-09

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: 58.04  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 311 WNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPthKYVRGENGPGGFI 390
Cdd:cd08902  75 WDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARP--NFVRGFNHPCGWF 152

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 10946984 391 VLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQ 437
Cdd:cd08902 153 CVPLKDNPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKK 199
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 252-416 1.26e-03

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup 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) 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. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes 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. In addition to having a START domain, most proteins in this subgroup 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.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 40.24  E-value: 1.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 252 QILAQEENWKFERSNEyGDTVYTIEVPfHGKTFILKTFLPCPAELVYQ---EVILQPErmvlWNKTVTACQILQRV-EDN 327
Cdd:cd08913  53 KMLVAKDNWVLSSEKN-QVRLYTLEED-KFLSFKVEMVVHVDAAQAFLllsDLRRRPE----WDKHYRSCELVQQVdEDD 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 328 TLvsYDVSSGAAGGVVSPRDFVNVRRIER---RRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFV 404
Cdd:cd08913 127 AI--YHVTSPSLSGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYY 204

                       170
                ....*....|..
gi 10946984 405 wilNTDLKGRLP 416
Cdd:cd08913 205 ---NQATPGVLP 213
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 254-416 1.65e-03

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: 39.89  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 254 LAQEENWKFERSNEyGDTVYTIEVpfHG-KTFILKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQRVEDNTLVsY 332
Cdd:cd08873  51 LAAKSDWTVASSTT-SVTLYTLEQ--DGvLSFCVELKVQTCASDAF-DLLSDPFKRPEWDPHGRSCEEVKRVGEDDGI-Y 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10946984 333 DVSSGAAGGVVsPRDFVNVRRIERRRD---RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNprvCTFVWILNT 409
Cdd:cd08873 126 HTTMPSLTSEK-PNDFVLLVSRRKPATdgdPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGT---CTEVSYYNE 201


                ....*..
gi 10946984 410 DLKGRLP 416
Cdd:cd08873 202 TNPKLLS 208
 
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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