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Conserved domains on  [gi|2217309462|ref|XP_047291115|]
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stAR-related lipid transfer protein 3 isoform X1 [Homo sapiens]

Protein Classification

MENTAL and SRPBCC domain-containing protein( domain architecture ID 10564580)

MENTAL and SRPBCC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 233-411 7.97e-118

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


The actual alignment was detected with superfamily member cd08906:

Pssm-ID: 472699  Cd Length: 209  Bit Score: 344.92  E-value: 7.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 233 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 312
Cdd:cd08906     1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 313 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLK 392
Cdd:cd08906    81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                         170
                  ....*....|....*....
gi 2217309462 393 SASNPRVCTFVWILNTDLK 411
Cdd:cd08906   161 SASNPSVCTFIWILNTDLK 179
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 47-213 1.44e-92

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: 279.17  E-value: 1.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  47 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIA 125
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 126 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QVAVARGPLLFSGA- 201
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 2217309462 202 -----LSEGQFYSPPES 213
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 ...
 233-411 7.97e-118

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: 344.92  E-value: 7.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 233 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 312
Cdd:cd08906     1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 313 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLK 392
Cdd:cd08906    81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                         170
                  ....*....|....*....
gi 2217309462 393 SASNPRVCTFVWILNTDLK 411
Cdd:cd08906   161 SASNPSVCTFIWILNTDLK 179
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 47-213 1.44e-92

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: 279.17  E-value: 1.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  47 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIA 125
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 126 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QVAVARGPLLFSGA- 201
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 2217309462 202 -----LSEGQFYSPPES 213
Cdd:pfam10457 161 grsnnQSDGNFYSPPES 177
START pfam01852
START domain;
239-411 2.95e-47

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 162.57  E-value: 2.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 239 IRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 318
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 319 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNP 397
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170
                  ....*....|....
gi 2217309462 398 rvCTFVWILNTDLK 411
Cdd:pfam01852 161 --SKVTWVSHADLK 172
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 240-411 2.65e-40

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 144.11  E-value: 2.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  240 RQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 317
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  318 QILQRVEDNTLISYDVSAGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASN 396
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170
                   ....*....|....*
gi 2217309462  397 PrvCTFVWILNTDLK 411
Cdd:smart00234 160 P--SKVTWVSHADLK 172
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 233-411 7.97e-118

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: 344.92  E-value: 7.97e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 233 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 312
Cdd:cd08906     1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 313 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLK 392
Cdd:cd08906    81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                         170
                  ....*....|....*....
gi 2217309462 393 SASNPRVCTFVWILNTDLK 411
Cdd:cd08906   161 SASNPSVCTFIWILNTDLK 179
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 47-213 1.44e-92

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: 279.17  E-value: 1.44e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  47 SDVRRTFCLFVTFDLLFISLLWIIELNTN-TGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIA 125
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINgENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 126 VTTLVSSAFLIVKVILSELL--SKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAA-QVAVARGPLLFSGA- 201
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLssSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAiTSADERAPLLQPGPe 160

                         170
                  ....*....|....*..
gi 2217309462 202 -----LSEGQFYSPPES 213
Cdd:pfam10457 161 grsnnQSDGNFYSPPES 177
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 233-411 2.25e-87

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: 266.91  E-value: 2.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 233 AQEREYIRQGKEATAVVDQILAQEeNWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNK 312
Cdd:cd08868     1 SQELEYLKQGAEALARAWSILTDP-GWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 313 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLK 392
Cdd:cd08868    80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159

                         170
                  ....*....|....*....
gi 2217309462 393 SASNPRVCTFVWILNTDLK 411
Cdd:cd08868   160 LPNNPNKCNFTWLLNTDLK 178
START pfam01852
START domain;
239-411 2.95e-47

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 162.57  E-value: 2.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 239 IRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQ 318
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 319 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNP 397
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170
                  ....*....|....
gi 2217309462 398 rvCTFVWILNTDLK 411
Cdd:pfam01852 161 --SKVTWVSHADLK 172
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 240-411 2.65e-40

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 144.11  E-value: 2.65e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  240 RQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTAC 317
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462  318 QILQRVEDNTLISYDVSAGAAgGVVSPRDFVNVRRIERRRD-RYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASN 396
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWREDEDgSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170
                   ....*....|....*
gi 2217309462  397 PrvCTFVWILNTDLK 411
Cdd:smart00234 160 P--SKVTWVSHADLK 172
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 234-411 5.79e-40

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: 143.44  E-value: 5.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 234 QEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKT 313
Cdd:cd08905     2 AEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 314 VTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKS 393
Cdd:cd08905    82 VKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPL 161

                         170
                  ....*....|....*...
gi 2217309462 394 ASNPRVCTFVWILNTDLK 411
Cdd:cd08905   162 AGDPSKTKLTWLLSIDLK 179
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 243-411 2.33e-24

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: 100.11  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 243 KEATAVVDQILAQEENWKFEKNNEyGDTVYTIEVPFHGKTFI-LKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQ 321
Cdd:cd00177     1 EEAIEELLELLEEPEGWKLVKEKD-GVKIYTKPYEDSGLKLLkAEGVIPASPEQVF-ELLMDIDLRKKWDKNFEEFEVIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 322 RVEDNTLISYdvSAGAAGGVVSPRDFVNVRRIERRRD-RYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKsaSNPRVC 400
Cdd:cd00177    79 EIDEHTDIIY--YKTKPPWPVSPRDFVYLRRRRKLDDgTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEP--LDPGKT 154

                         170
                  ....*....|.
gi 2217309462 401 TFVWILNTDLK 411
Cdd:cd00177   155 KVTYVLQVDPK 165
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 256-410 7.09e-16

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: 76.35  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 256 EENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYqEVILQP---ERmVLWNKTVTACQILQRVEDNTLISYD 332
Cdd:cd08867    21 TDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVI-DVIIPPcggLR-LKWDKSLKHYEVLEKISEDLCVGRT 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217309462 333 VSAGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNPRVCTFVWILNTDL 410
Cdd:cd08867    99 ITPSAAMGLISPRDFVDlVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDL 177
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 243-411 2.50e-13

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: 68.78  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 243 KEATAVVDQILAQEEN---WKFEKNNEYGDTVYTIEVPFHGKTFILKTFLP-CPAELVyqEVILQPERMVLWNKTVTACQ 318
Cdd:cd08904     5 KIAQETSQEVLGYSRDtsgWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPeSPAKLI--QFMYQPEHRIKWDKSLQVYK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 319 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNP 397
Cdd:cd08904    83 MLQRIDSDTFICHTITQSFAMGSISPRDFVDlVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENP 162

                         170
                  ....*....|....
gi 2217309462 398 RVCTFVWILNTDLK 411
Cdd:cd08904   163 AYSKLVMFVQPELR 176
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 302-410 9.96e-09

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: 55.61  E-value: 9.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 302 LQPER---MVLWNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGiAT--SHSAKPPTH 376
Cdd:cd08903    65 LKPAAgglRVKWDQNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSN-ATnvEHPLCPPQA 143

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2217309462 377 KYVRGENGPGGFIVLKSASNPRVCTFVWILNTDL 410
Cdd:cd08903   144 GFVRGFNHPCGCFCEPVPGEPDKTQLVSFFQTDL 177
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 310-411 6.17e-06

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: 47.26  E-value: 6.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 310 WNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPthKYVRGENGPGGFI 389
Cdd:cd08902    75 WDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARP--NFVRGFNHPCGWF 152

                          90       100
                  ....*....|....*....|..
gi 2217309462 390 VLKSASNPRVCTFVWILNTDLK 411
Cdd:cd08902   153 CVPLKDNPSHSLLTGYIQTDLR 174
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 251-403 6.34e-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: 38.31  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 251 QILAQEENWKF--EKNNEygdTVYTIEVPfHGKTFILKTFLPCPAELVYQ---EVILQPErmvlWNKTVTACQILQRV-E 324
Cdd:cd08913    53 KMLVAKDNWVLssEKNQV---RLYTLEED-KFLSFKVEMVVHVDAAQAFLllsDLRRRPE----WDKHYRSCELVQQVdE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 325 DNTLisYDVSAGAAGGVVSPRDFVNVRRIER---RRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNPRVCT 401
Cdd:cd08913   125 DDAI--YHVTSPSLSGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVS 202


                  ..
gi 2217309462 402 FV 403
Cdd:cd08913   203 YY 204
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 253-407 8.55e-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: 37.96  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217309462 253 LAQEENWKFEKNNEyGDTVYTIEVpfHG-KTFILKTFLPCPAELVYqEVILQPERMVLWNKTVTACQILQRVEDNTLIsY 331
Cdd:cd08873    51 LAAKSDWTVASSTT-SVTLYTLEQ--DGvLSFCVELKVQTCASDAF-DLLSDPFKRPEWDPHGRSCEEVKRVGEDDGI-Y 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217309462 332 DVSAGAAGGVVsPRDFVNVRRIERRRD---RYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNprvCTFVWILN 407
Cdd:cd08873   126 HTTMPSLTSEK-PNDFVLLVSRRKPATdgdPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVIRQDCGT---CTEVSYYN 200
 
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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