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Conserved domains on  [gi|568975151|ref|XP_006533958|]
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stAR-related lipid transfer protein 3 isoform X1 [Mus musculus]

Protein Classification

SRPBCC family protein( domain architecture ID 10300696)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 255-463 7.96e-142

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: 404.63  E-value: 7.96e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 255 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 334
Cdd:cd08906    1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 335 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 414
Cdd:cd08906   81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568975151 415 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 463
Cdd:cd08906  161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
MENTAL super family cl11103
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-235 2.89e-53

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.


The actual alignment was detected with superfamily member pfam10457:

Pssm-ID: 463097  Cd Length: 177  Bit Score: 176.71  E-value: 2.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   48 SDVRRTFCLFVTFDLLFISLLWIIELN----GLLRHWKKDILHSRlpsepFLSSSADqhwhpeelgaggdplqlpeLVLR 123
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVingeNIKKAFEKEVLHYN-----IKTSLFD-------------------IVLL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  124 HLCSgFLPLLWAApGLCCAP--SPALVTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQE 199
Cdd:pfam10457  57 AAFR-FLVLLLFY-ALLRLNhwWIIAITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568975151  200 AEEERWYLAA-QAAVARGPLLFSGA------LSEGQFYSPPES 235
Cdd:pfam10457 135 AEAERRYLAAiTSADERAPLLQPGPegrsnnQSDGNFYSPPES 177
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 255-463 7.96e-142

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: 404.63  E-value: 7.96e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 255 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 334
Cdd:cd08906    1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 335 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 414
Cdd:cd08906   81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568975151 415 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 463
Cdd:cd08906  161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
START pfam01852
START domain;
261-466 6.52e-64

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 205.33  E-value: 6.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  261 IRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 340
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  341 ILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNP 419
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568975151  420 rvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 466
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 262-466 6.36e-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: 6.36e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   262 RQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 339
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   340 QILQRVEDNTLVSYDVSSGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANN 418
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568975151   419 PrvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 466
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-235 2.89e-53

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: 176.71  E-value: 2.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   48 SDVRRTFCLFVTFDLLFISLLWIIELN----GLLRHWKKDILHSRlpsepFLSSSADqhwhpeelgaggdplqlpeLVLR 123
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVingeNIKKAFEKEVLHYN-----IKTSLFD-------------------IVLL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  124 HLCSgFLPLLWAApGLCCAP--SPALVTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQE 199
Cdd:pfam10457  57 AAFR-FLVLLLFY-ALLRLNhwWIIAITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568975151  200 AEEERWYLAA-QAAVARGPLLFSGA------LSEGQFYSPPES 235
Cdd:pfam10457 135 AEAERRYLAAiTSADERAPLLQPGPegrsnnQSDGNFYSPPES 177
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 255-463 7.96e-142

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: 404.63  E-value: 7.96e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 255 AQEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 334
Cdd:cd08906    1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 335 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 414
Cdd:cd08906   81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568975151 415 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 463
Cdd:cd08906  161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 255-463 5.86e-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: 5.86e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 255 AQEREYIRQGKEATAVVDQILAQEeNWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 334
Cdd:cd08868    1 SQELEYLKQGAEALARAWSILTDP-GWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 335 TVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLK 414
Cdd:cd08868   80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568975151 415 SANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 463
Cdd:cd08868  160 LPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START pfam01852
START domain;
261-466 6.52e-64

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 205.33  E-value: 6.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  261 IRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 340
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  341 ILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNP 419
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568975151  420 rvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 466
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 262-466 6.36e-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: 6.36e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   262 RQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 339
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   340 QILQRVEDNTLVSYDVSSGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANN 418
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568975151   419 PrvCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGELGAR 466
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 48-235 2.89e-53

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: 176.71  E-value: 2.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151   48 SDVRRTFCLFVTFDLLFISLLWIIELN----GLLRHWKKDILHSRlpsepFLSSSADqhwhpeelgaggdplqlpeLVLR 123
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVingeNIKKAFEKEVLHYN-----IKTSLFD-------------------IVLL 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151  124 HLCSgFLPLLWAApGLCCAP--SPALVTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQE 199
Cdd:pfam10457  57 AAFR-FLVLLLFY-ALLRLNhwWIIAITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568975151  200 AEEERWYLAA-QAAVARGPLLFSGA------LSEGQFYSPPES 235
Cdd:pfam10457 135 AEAERRYLAAiTSADERAPLLQPGPegrsnnQSDGNFYSPPES 177
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 256-460 1.50e-49

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: 1.50e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 256 QEREYIRQGKEATAVVDQILAQEENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKT 335
Cdd:cd08905    2 AEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 336 VTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKS 415
Cdd:cd08905   82 VKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 568975151 416 ANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRV 460
Cdd:cd08905  162 AGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRM 206
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 265-458 2.13e-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: 110.89  E-value: 2.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 265 KEATAVVDQILAQEENWKFERSNEyGDTVYTIEVPFHGKTFI-LKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQ 343
Cdd:cd00177    1 EEAIEELLELLEEPEGWKLVKEKD-GVKIYTKPYEDSGLKLLkAEGVIPASPEQVF-ELLMDIDLRKKWDKNFEEFEVIE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 344 RVEDNTLVSYDVSSgaAGGVVSPRDFVNVRRIERRRD-RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNprVC 422
Cdd:cd00177   79 EIDEHTDIIYYKTK--PPWPVSPRDFVYLRRRRKLDDgTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPG--KT 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568975151 423 TFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQ 458
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 ...
 278-460 5.59e-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: 90.60  E-value: 5.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 278 EENWKFERSNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYqEVILQP---ERmVLWNKTVTACQILQRVEDNTLVSYD 354
Cdd:cd08867   21 TDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVI-DVIIPPcggLR-LKWDKSLKHYEVLEKISEDLCVGRT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 355 VSSGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLK 433
Cdd:cd08867   99 ITPSAAMGLISPRDFVDlVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLR 178

                        170       180
                 ....*....|....*....|....*..
gi 568975151 434 GRLPRYLIHQSLGATMFEFAFHLRQRV 460
Cdd:cd08867  179 GMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 300-452 9.81e-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: 78.41  E-value: 9.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 300 FHGKTFILKTFLP-CPAELVyqEVILQPERMVLWNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVN-VRRIER 377
Cdd:cd08904   43 YHGNLYRVEGIIPeSPAKLI--QFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDlVHIKRY 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975151 378 RRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEF 452
Cdd:cd08904  121 EGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNL 195
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 267-463 1.76e-13

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: 69.09  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 267 ATAVVDQILA---QEENWKF-ERSNEYgdTVY-TIEVPFHGKTFILKTFLPCPAELVYQevILQPER---MVLWNKTVTA 338
Cdd:cd08903    7 AESVADKMLLyrrDESGWKTcRRTNEV--AVSwRPSAEFAGNLYKGEGIVYATLEQVWD--CLKPAAgglRVKWDQNVKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 339 CQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGiAT--THCSKPPTHKYVRGENGPGGFIVLKSA 416
Cdd:cd08903   83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSN-ATnvEHPLCPPQAGFVRGFNHPCGCFCEPVP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568975151 417 NNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQRVGEL 463
Cdd:cd08903  162 GEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 332-458 1.31e-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: 57.66  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 332 WNKTVTACQILQRVEDNTLVSYDVSSGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATTHCSKPPthKYVRGENGPGGFI 411
Cdd:cd08902   75 WDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARP--NFVRGFNHPCGWF 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568975151 412 VLKSANNPRVCTFVWILNTDLKGRLPRYLIHQSLGATMFEFAFHLRQ 458
Cdd:cd08902  153 CVPLKDNPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKK 199
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 273-437 1.19e-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: 40.62  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 273 QILAQEENWKFERSNEyGDTVYTIEVPfHGKTFILKTFLPCPAELVYQ---EVILQPErmvlWNKTVTACQILQRV-EDN 348
Cdd:cd08913   53 KMLVAKDNWVLSSEKN-QVRLYTLEED-KFLSFKVEMVVHVDAAQAFLllsDLRRRPE----WDKHYRSCELVQQVdEDD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 349 TLvsYDVSSGAAGGVVSPRDFVNVRRIER---RRDRYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNPRVCTFV 425
Cdd:cd08913  127 AI--YHVTSPSLSGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYY 204

                        170
                 ....*....|..
gi 568975151 426 wilNTDLKGRLP 437
Cdd:cd08913  205 ---NQATPGVLP 213
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 275-437 1.59e-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: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 275 LAQEENWKFERSNEyGDTVYTIEVpfHG-KTFILKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQRVEDNTLVsY 353
Cdd:cd08873   51 LAAKSDWTVASSTT-SVTLYTLEQ--DGvLSFCVELKVQTCASDAF-DLLSDPFKRPEWDPHGRSCEEVKRVGEDDGI-Y 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975151 354 DVSSGAAGGVVsPRDFVNVRRIERRRD---RYLSSGIATTHCSKPPTHKYVRGENGPGGFIVLKSANNprvCTFVWILNT 430
Cdd:cd08873  126 HTTMPSLTSEK-PNDFVLLVSRRKPATdgdPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGT---CTEVSYYNE 201


                 ....*..
gi 568975151 431 DLKGRLP 437
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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