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Conserved domains on  [gi|2217316154|ref|XP_047293256|]
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stAR-related lipid transfer protein 6 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-215 2.18e-147

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: 408.91  E-value: 2.18e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTG 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  81 DRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904    70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217316154 161 PCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904   150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-215 2.18e-147

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: 408.91  E-value: 2.18e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTG 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  81 DRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904    70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217316154 161 PCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904   150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START pfam01852
START domain;
36-196 3.03e-25

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 98.24  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  36 FLFPFEKKITVSSKASRKFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAV 114
Cdd:pfam01852  22 VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALVAP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154 115 GSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKLVMFVQTEMRGKLSPSI 194
Cdd:pfam01852 102 SPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPSWL 179


                  ..
gi 2217316154 195 IE 196
Cdd:pfam01852 180 LR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 52-206 5.32e-25

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 97.50  E-value: 5.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   52 RKFHGNLYRVEGIIPESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITQSFAVGSISPRDFIDLVYIKR 130
Cdd:smart00234  39 GRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVSKFAAGPVSPRDFVFVRYWRE 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316154  131 YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKLSPSIIEKTMPSNLVNF 206
Cdd:smart00234 118 DEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEF 191
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-215 2.18e-147

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: 408.91  E-value: 2.18e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTG 80
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTS-----------KKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  81 DRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNH 160
Cdd:cd08904    70 HRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNH 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217316154 161 PCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08904   150 PCGYVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-215 1.55e-118

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: 335.97  E-value: 1.55e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQ-- 78
Cdd:cd08867     1 MDFKVIAEKLANEALQYINDTDGWKVLKTV-----------KNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpc 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  79 TGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGY 158
Cdd:cd08867    70 GGLRLKWDKSLKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGY 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217316154 159 NHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08867   150 NHPCGYFCSPLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 1-216 2.20e-55

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: 175.80  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFL--YQ 78
Cdd:cd08903     1 MDYAELAESVADKMLLYRRDESGWKTCRRT-----------NEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLkpAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  79 TGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGY 158
Cdd:cd08903    70 GGLRVKWDQNVKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGF 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316154 159 NHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKA 216
Cdd:cd08903   150 NHPCGCFCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 12-207 2.70e-36

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: 126.30  E-value: 2.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  12 QEVLGYNRDTSGWKVVKTsliicgflfpfEKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQV 91
Cdd:cd00177     5 EELLELLEEPEGWKLVKE-----------KDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  92 YNMVHRIDSDTFICHTITQSFAVgsISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 171
Cdd:cd00177    74 FEVIEEIDEHTDIIYYKTKPPWP--VSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDP 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217316154 172 NpaYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 207
Cdd:cd00177   152 G--KTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFL 185
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 24-215 2.68e-33

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: 118.90  E-value: 2.68e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  24 WKVVKTSliicgflfpfeKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTF 103
Cdd:cd08902    25 WRVAKKS-----------KDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFEENCC 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154 104 ICHTITQSFAVGSISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPssNYIRGYNHPCGFVCSPMEENPAYSKLVMFVQ 183
Cdd:cd08902    94 VMRYTTAGQLLNIISPREFVDFSYTTQYEDGL-LSCGVSIEYEEARP--NFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQ 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2217316154 184 TEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 215
Cdd:cd08902   171 TDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 1-217 1.29e-29

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: 109.75  E-value: 1.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   1 MDFKAIAQQTAQEVLGYNRDtSGWKVVKTSliicgflfpfEKKITVSSKaSRKFHGNLYRVEGIIPESPAKLSDFLYQTG 80
Cdd:cd08868     4 LEYLKQGAEALARAWSILTD-PGWKLEKNT----------TWGDVVYSR-NVPGVGKVFRLTGVLDCPAEFLYNELVLNV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  81 DRIT-WDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEgNMNIISSKSVDFPEYPPSSNYIRGYN 159
Cdd:cd08868    72 ESLPsWNPTVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE-NCYLSSGVSVEHPAMPPTKNYVRGEN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217316154 160 HPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKAH 217
Cdd:cd08868   151 GPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START pfam01852
START domain;
36-196 3.03e-25

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 98.24  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  36 FLFPFEKKITVSSKASRKFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAV 114
Cdd:pfam01852  22 VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALVAP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154 115 GSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKLVMFVQTEMRGKLSPSI 194
Cdd:pfam01852 102 SPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPSWL 179


                  ..
gi 2217316154 195 IE 196
Cdd:pfam01852 180 LR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 52-206 5.32e-25

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 97.50  E-value: 5.32e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   52 RKFHGNLYRVEGIIPESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITQSFAVGSISPRDFIDLVYIKR 130
Cdd:smart00234  39 GRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVSKFAAGPVSPRDFVFVRYWRE 117

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316154  131 YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKLSPSIIEKTMPSNLVNF 206
Cdd:smart00234 118 DEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEF 191
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 53-215 5.64e-23

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: 92.23  E-value: 5.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  53 KFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRY 131
Cdd:cd08906    45 PFHGKTFILKAFMQCPAELVyQEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154 132 eGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAK 211
Cdd:cd08906   125 -RDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLR 203


                  ....
gi 2217316154 212 DGIK 215
Cdd:cd08906   204 QRIR 207
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 8-207 1.52e-17

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: 77.95  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154   8 QQTAQEVLGYNRDTSGWKvvKTSLIICGflfpfEKkitVSSKASRKFhGNLYRVEGIIPESP----AKLSDFLYQTGDri 83
Cdd:cd08905    11 EEALQKSLSILQDQEGWK--TEIVAENG-----DK---VLSKVVPDI-GKVFRLEVVVDQPLdnlySELVDRMEQMGE-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  84 tWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRyEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCG 163
Cdd:cd08905    78 -WNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKR-RGSTCVLAGMATHFGLMPEQKGFIRAENGPTC 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217316154 164 FVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 207
Cdd:cd08905   156 IVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFA 199
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 41-193 4.22e-10

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: 57.23  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  41 EKKITVSSKA-SRKFHGnlYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSISP 119
Cdd:cd08874    30 EKDVVIYYKVfNGTYHG--FLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDICLVYLVHETPLCLLKQP 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217316154 120 RDFIdLVYIKRYEGNMNIISSKSVDFPEYP-PSSNYIRGYNHPCGFVCSPMEEN-PAYSKLVMFVQTEMRGKLSPS 193
Cdd:cd08874   108 RDFC-CLQVEAKEGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPVTVEgNQYTRVIYIAQVALCGPDVPA 182
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 66-209 2.40e-09

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: 55.68  E-value: 2.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  66 PESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSfaVGSISPRDFIDLVYIKR--YEGNMNIISSKS 142
Cdd:cd08873    85 VQTCASDAfDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPS--LTSEKPNDFVLLVSRRKpaTDGDPYKVAFRS 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217316154 143 VDFPEYPPSSNYIRGYNHPCGFV----CSPMEE----NPAYSKLVMFVQTEMRGkLSpSIIEKTMPSnLVNFILN 209
Cdd:cd08873   163 VTLPRVPQTPGYSRTEVACAGFVirqdCGTCTEvsyyNETNPKLLSYVTCNLAG-LS-ALYCRTFHC-CEQFLVT 234
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 42-207 2.51e-07

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: 49.56  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  42 KKITVSSKASRKFHGNLYRVEGIIPE-SPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtitqsFAVGS---I 117
Cdd:cd08871    32 NNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNNDIGY-----YSAKCpkpL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154 118 SPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKLspsiiek 197
Cdd:cd08871   107 KNRDFVNLRSWLEFGGEY-IIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKG--CTLTYVTQNDPKGSL------- 176

                         170
                  ....*....|
gi 2217316154 198 tmPSNLVNFI 207
Cdd:cd08871   177 --PKWVVNKA 184
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 59-183 1.21e-06

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: 47.94  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  59 YRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAVGSiSPRDFIDLVYIKR--YEGNMN 136
Cdd:cd08913    83 FKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQVDEDDAIYHVTSPSLSGHG-KPQDFVILASRRKpcDNGDPY 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2217316154 137 IISSKSVDFPEYPPSSNYIRGYNHPCGFVCspMEENPAYSKLVMFVQ 183
Cdd:cd08913   162 VIALRSVTLPTHPPTPEYTRGETLCSGFCI--WEESDQLTKVSYYNQ 206
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 67-172 2.06e-04

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) 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. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 41.42  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  67 ESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITqSFAVGSISPRDFIDLVYiKRY---EGNMNIISSKS 142
Cdd:cd08914    87 KRPAHLAyRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYH-IT-CPIVNNDKPKDLVVLVS-RRKplkDGNTYVVAVKS 163

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217316154 143 VDFPEYPPSSNYIRGYNHPCGFVCSPMEEN 172
Cdd:cd08914   164 VILPSVPPSPQYIRSEIICAGFLIHAIDSN 193
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 18-156 3.43e-03

Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176920  Cd Length: 207  Bit Score: 37.27  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217316154  18 NRDTSGWKVVktsliicgflfpFEKKitvSSKASRKFH--GNL--YRVEGIIPESPAKlsDFLYQTGD---RITWDKSLQ 90
Cdd:cd08911    17 NQEPDGWEPF------------IEKK---DMLVWRREHpgTGLyeYKVYGSFDDVTAR--DFLNVQLDleyRKKWDATAV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217316154  91 VYNMVHR-IDSDTFICHTITQ---SFAvgsisPRDFidlVYIKRY----EGNMNIISSKSVDFPEYPPSSNYIR 156
Cdd:cd08911    80 ELEVVDEdPETGSEIIYWEMQwpkPFA-----NRDY---VYVRRYiideENKLIVIVSKAVQHPSYPESPKKVR 145
 
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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