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Conserved domains on  [gi|149057427|gb|EDM08750|]
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similar to StAR-related protein 1-4E (predicted), isoform CRA_b [Rattus norvegicus]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

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
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 6-169 1.06e-109

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 cd08903:

Pssm-ID: 472699  Cd Length: 208  Bit Score: 311.39  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVAGGLREKWDDNVNS 85
Cdd:cd08903    3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  86 FEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903   83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162


                 ....
gi 149057427 166 NSGK 169
Cdd:cd08903  163 EPDK 166
 
Name Accession Description Interval E-value
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 6-169 1.06e-109

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: 311.39  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVAGGLREKWDDNVNS 85
Cdd:cd08903    3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  86 FEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903   83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162


                 ....
gi 149057427 166 NSGK 169
Cdd:cd08903  163 EPDK 166
START pfam01852
START domain;
11-166 4.86e-16

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 72.44  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   11 EAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTP----EEVWDcvkpvAGGLREKWDDNVNSF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAallvAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   87 EIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGN 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-166 4.08e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 64.37  E-value: 4.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427     8 QESEAVAEKVLRYRRDASGWKKCREGN--GVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVaGGLREKWDDNVNS 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDD-LEYRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427    86 FEIVQSI-TDTLCVSRTStpSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLP 164
Cdd:smart00234  80 AETLEVIdNGTVIYHYVS--KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLG 157


                   ..
gi 149057427   165 GN 166
Cdd:smart00234 158 NG 159
 
Name Accession Description Interval E-value
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 6-169 1.06e-109

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: 311.39  E-value: 1.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVAGGLREKWDDNVNS 85
Cdd:cd08903    3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  86 FEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903   83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162


                 ....
gi 149057427 166 NSGK 169
Cdd:cd08903  163 EPDK 166
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 6-169 7.95e-89

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: 258.55  E-value: 7.95e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVAGGLREKWDDNVNS 85
Cdd:cd08867    3 FKVIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPPCGGLRLKWDKSLKH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  86 FEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08867   83 YEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKG 162


                 ....
gi 149057427 166 NSGK 169
Cdd:cd08867  163 SPDK 166
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 10-168 1.85e-47

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: 153.52  E-value: 1.85e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  10 SEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVkpVAGGLREKWDDNVNSFEIV 89
Cdd:cd08904    7 AQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFM--YQPEHRIKWDKSLQVYKML 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149057427  90 QSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGNSG 168
Cdd:cd08904   85 QRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPA 163
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 15-167 3.62e-37

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: 126.68  E-value: 3.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  15 EKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVagGLREKWDDNVNSFEIVQSITD 94
Cdd:cd00177    5 EELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDI--DLRKKWDKNFEEFEVIEEIDE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149057427  95 TLCVSRTSTPSaaMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGNS 167
Cdd:cd00177   83 HTDIIYYKTKP--PWPVSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGK 153
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 27-166 3.56e-30

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: 109.27  E-value: 3.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  27 WKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPvaGGLREKWDDNVNSFEIVQSITDTLCVSRTSTPSA 106
Cdd:cd08902   25 WRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRP--GPYRLDWDSLMTSMDIIEEFEENCCVMRYTTAGQ 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427 107 AMKLISPRDFVDLVLVKKYEDGTISSNAThVEHPlcPPKPGFVRGFNHPCGCFCEPLPGN 166
Cdd:cd08902  103 LLNIISPREFVDFSYTTQYEDGLLSCGVS-IEYE--EARPNFVRGFNHPCGWFCVPLKDN 159
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 25-169 3.58e-19

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: 80.48  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  25 SGWKK-CREGNGVSISWRpSEEFPGNLYRGEGILCGTPEEVWDCVKPVAGGLREkWDDNVNSFEIVQSITDTLCVSRTST 103
Cdd:cd08868   24 PGWKLeKNTTWGDVVYSR-NVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPS-WNPTVLECKIIQVIDDNTDISYQVA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149057427 104 PSAAMKLISPRDFVDLVLVKKYEDGTISSnATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGNSGK 169
Cdd:cd08868  102 AEAGGGLVSPRDFVSLRHWGIRENCYLSS-GVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNK 166
START pfam01852
START domain;
11-166 4.86e-16

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 72.44  E-value: 4.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   11 EAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTP----EEVWDcvkpvAGGLREKWDDNVNSF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAallvAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   87 EIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGN 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-166 4.08e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 64.37  E-value: 4.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427     8 QESEAVAEKVLRYRRDASGWKKCREGN--GVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCVKPVaGGLREKWDDNVNS 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDD-LEYRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427    86 FEIVQSI-TDTLCVSRTStpSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLP 164
Cdd:smart00234  80 AETLEVIdNGTVIYHYVS--KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLG 157


                   ..
gi 149057427   165 GN 166
Cdd:smart00234 158 NG 159
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 15-173 1.24e-11

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 60.73  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  15 EKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCG-TPEEVWDCVkpVAGGLREKWDDNV-NSFEIVQsi 92
Cdd:cd08871   13 EEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVL--HDPEYRKTWDSNMiESFDICQ-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  93 tdtLCVSRT-STPSAAM-KLISPRDFVDLVLVKKYEDGTISSNaTHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGNsgkG 170
Cdd:cd08871   89 ---LNPNNDiGYYSAKCpKPLKNRDFVNLRSWLEFGGEYIIFN-HSVKHKKYPPRKGFVRAISLLTGYLIRPTGPK---G 161


                 ...
gi 149057427 171 CEL 173
Cdd:cd08871  162 CTL 164
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 1-169 5.95e-11

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: 58.69  E-value: 5.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427   1 MDLSWATQESEAVaEKVLRYRRDASGWKKcrEGNGVSISWRPSEEFP--GNLYRGEGILCGTPEEVWdcvkpvaGGLREK 78
Cdd:cd08905    2 AEMSYIKQGEEAL-QKSLSILQDQEGWKT--EIVAENGDKVLSKVVPdiGKVFRLEVVVDQPLDNLY-------SELVDR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  79 ------WDDNVNSFEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDlVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGF 152
Cdd:cd08905   72 meqmgeWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVS-VRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAE 150

                        170
                 ....*....|....*..
gi 149057427 153 NHPCGCFCEPLPGNSGK 169
Cdd:cd08905  151 NGPTCIVLRPLAGDPSK 167
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 79-166 7.30e-11

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: 58.33  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  79 WDDNVNSFEIVQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNAThVEHPLCPPKPGFVRGFNHPCGC 158
Cdd:cd08906   78 WNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGIS-TTHSHKPPLSKYVRGENGPGGF 156


                 ....*...
gi 149057427 159 FCEPLPGN 166
Cdd:cd08906  157 VVLKSASN 164
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 24-166 4.24e-06

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), 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. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 45.29  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  24 ASGWKKCREGNGVSISWRPseeFPGNLYR--GEGILCGTPEEVWDCVK-PvagGLREKWDDNVNSFEIVQSITDTLCVSR 100
Cdd:cd08874   21 TAGWSYQCLEKDVVIYYKV---FNGTYHGflGAGVIKAPLATVWKAVKdP---RTRFLYDTMIKTARIHKTFTEDICLVY 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149057427 101 TSTPSAAMKLISPRDFVDLVLVKKYEDGTISSnATHVEHPLCP-PKPGFVRGFNHPCGCFCEPLPGN 166
Cdd:cd08874   95 LVHETPLCLLKQPRDFCCLQVEAKEGELSVVA-CQSVYDKSMPePGRSLVRGEILPSAWILEPVTVE 160
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 76-160 4.06e-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: 36.81  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149057427  76 REKWDDNVNSFEIVQSITDTLCVSRTSTPSAAMKliSPRDFVDLVLVKK-YEDGTISSNATH-VEHPLCPPKPGFVRGfN 153
Cdd:cd08873  102 RPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSE--KPNDFVLLVSRRKpATDGDPYKVAFRsVTLPRVPQTPGYSRT-E 178


                 ....*..
gi 149057427 154 HPCGCFC 160
Cdd:cd08873  179 VACAGFV 185
 
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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