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Conserved domains on  [gi|21040261|ref|NP_631910|]
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stAR-related lipid transfer protein 6 isoform 1 [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 ...
 1-204 4.21e-150

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: 415.46  E-value: 4.21e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQV 80
Cdd:cd08904   1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  81 YNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 160
Cdd:cd08904  81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21040261 161 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08904 161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-204 4.21e-150

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: 415.46  E-value: 4.21e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQV 80
Cdd:cd08904   1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  81 YNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 160
Cdd:cd08904  81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21040261 161 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08904 161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START pfam01852
START domain;
23-185 3.28e-27

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 102.87  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261    23 GWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSF 101
Cdd:pfam01852  20 GWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   102 AVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKLVMFVQTEMRGKLSP 181
Cdd:pfam01852 100 APSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPS 177


                  ....
gi 21040261   182 SIIE 185
Cdd:pfam01852 178 WLLR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 23-195 6.86e-26

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 99.43  E-value: 6.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261     23 GWKVVKTSKKITVSSK--ASRKFHGNLYRVEGIIPESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITQ 99
Cdd:smart00234  19 GWVLSSENENGDEVRSifSPGRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261    100 SFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKL 179
Cdd:smart00234  98 KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWL 175

                          170
                   ....*....|....*.
gi 21040261    180 SPSIIEKTMPSNLVNF 195
Cdd:smart00234 176 PHWLVRSLIKSGLAEF 191
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-204 4.21e-150

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: 415.46  E-value: 4.21e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQV 80
Cdd:cd08904   1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  81 YNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 160
Cdd:cd08904  81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21040261 161 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08904 161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-204 1.96e-121

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: 342.90  E-value: 1.96e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQ--TGDRITWDKSL 78
Cdd:cd08867   1 MDFKVIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpcGGLRLKWDKSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  79 QVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPM 158
Cdd:cd08867  81 KHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21040261 159 EENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08867 161 KGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 1-205 6.30e-59

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: 184.65  E-value: 6.30e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFL--YQTGDRITWDKSL 78
Cdd:cd08903   1 MDYAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLkpAAGGLRVKWDQNV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  79 QVYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPM 158
Cdd:cd08903  81 KDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPV 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21040261 159 EENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKA 205
Cdd:cd08903 161 PGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 12-196 3.48e-39

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: 133.62  E-value: 3.48e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  12 QEVLGYNRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDT 91
Cdd:cd00177   5 EELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHT 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  92 FICHTITQSFAVgsISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKLVMFV 171
Cdd:cd00177  85 DIIYYKTKPPWP--VSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPG--KTKVTYVL 160

                       170       180
                ....*....|....*....|....*
gi 21040261 172 QTEMRGKLSPSIIEKTMPSNLVNFI 196
Cdd:cd00177 161 QVDPKGSIPKSLVNSAAKKQLASFL 185
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 24-204 1.00e-36

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: 127.38  E-value: 1.00e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  24 WKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFAV 103
Cdd:cd08902  25 WRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMTSMDIIEEFEENCCVMRYTTAGQLL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261 104 GSISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPssNYIRGYNHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSI 183
Cdd:cd08902 105 NIISPREFVDFSYTTQYEDGL-LSCGVSIEYEEARP--NFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGMLPQSA 181

                       170       180
                ....*....|....*....|.
gi 21040261 184 IEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08902 182 VDTAMASTLVNFYSDLKKALK 202
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 1-206 1.31e-31

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: 114.37  E-value: 1.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   1 MDFKAIAQQTAQEVLGYNRDtSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRIT-WDKSLQ 79
Cdd:cd08868   4 LEYLKQGAEALARAWSILTD-PGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPsWNPTVL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  80 VYNMVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEgNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPME 159
Cdd:cd08868  83 ECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE-NCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21040261 160 ENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKAH 206
Cdd:cd08868 162 NNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START pfam01852
START domain;
23-185 3.28e-27

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 102.87  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261    23 GWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSF 101
Cdd:pfam01852  20 GWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLvAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVAALV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   102 AVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKLVMFVQTEMRGKLSP 181
Cdd:pfam01852 100 APSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKVTWVSHADLKGWLPS 177


                  ....
gi 21040261   182 SIIE 185
Cdd:pfam01852 178 WLLR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 23-195 6.86e-26

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 99.43  E-value: 6.86e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261     23 GWKVVKTSKKITVSSK--ASRKFHGNLYRVEGIIPESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITQ 99
Cdd:smart00234  19 GWVLSSENENGDEVRSifSPGRKPGEAFRLVGVVPMVCADLVeELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYH-YVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261    100 SFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKL 179
Cdd:smart00234  98 KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKVTWVSHADLKGWL 175

                          170
                   ....*....|....*.
gi 21040261    180 SPSIIEKTMPSNLVNF 195
Cdd:smart00234 176 PHWLVRSLIKSGLAEF 191
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 24-204 2.00e-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: 93.00  E-value: 2.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  24 WKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKL-SDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQSFA 102
Cdd:cd08906  27 WKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVyQEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYDVAAGAA 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261 103 VGSISPRDFIDLVYIKRYeGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPS 182
Cdd:cd08906 107 GGVVSPRDFVNVRRIERR-RDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLKSASNPSVCTFIWILNTDLKGRLPRY 185

                       170       180
                ....*....|....*....|..
gi 21040261 183 IIEKTMPSNLVNFILNAKDGIK 204
Cdd:cd08906 186 LIHQSLAATMFEFASHLRQRIR 207
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 8-196 1.67e-19

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: 82.96  E-value: 1.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   8 QQTAQEVLGYNRDTSGWKV-VKTSKKITVSSKASRKFhGNLYRVEGIIPESP----AKLSDFLYQTGDritWDKSLQVYN 82
Cdd:cd08905  11 EEALQKSLSILQDQEGWKTeIVAENGDKVLSKVVPDI-GKVFRLEVVVDQPLdnlySELVDRMEQMGE---WNPNVKEVK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  83 MVHRIDSDTFICHTITQSFAVGSISPRDFIDLVYIKRyEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENP 162
Cdd:cd08905  87 ILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKR-RGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPLAGDP 165

                       170       180       190
                ....*....|....*....|....*....|....
gi 21040261 163 AYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 196
Cdd:cd08905 166 SKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFA 199
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 21-182 3.79e-12

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: 63.01  E-value: 3.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  21 TSGWKVVKTSKKITVSSKA-SRKFHGnlYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQ 99
Cdd:cd08874  21 TAGWSYQCLEKDVVIYYKVfNGTYHG--FLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDICLVYLVHE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261 100 SFAVGSISPRDFIdLVYIKRYEGNMNIISSKSVDFPEYP-PSSNYIRGYNHPCGFVCSPMEEN-PAYSKLVMFVQTEMRG 177
Cdd:cd08874  99 TPLCLLKQPRDFC-CLQVEAKEGELSVVACQSVYDKSMPePGRSLVRGEILPSAWILEPVTVEgNQYTRVIYIAQVALCG 177


                ....*
gi 21040261 178 KLSPS 182
Cdd:cd08874 178 PDVPA 182
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 22-198 3.01e-11

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: 60.69  E-value: 3.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  22 SGWKVVKTSKKITVsskASRKFHGNLYRVEGIIPESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHTITQS 100
Cdd:cd08873  55 SDWTVASSTTSVTL---YTLEQDGVLSFCVELKVQTCASDAfDLLSDPFKRPEWDPHGRSCEEVKRVGEDDGIYHTTMPS 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261 101 faVGSISPRDFIDLVYIKR--YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFV----CSPMEE----NPAYSKLVMF 170
Cdd:cd08873 132 --LTSEKPNDFVLLVSRRKpaTDGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVirqdCGTCTEvsyyNETNPKLLSY 209

                       170       180
                ....*....|....*....|....*...
gi 21040261 171 VQTEMRGkLSpSIIEKTMPSnLVNFILN 198
Cdd:cd08873 210 VTCNLAG-LS-ALYCRTFHC-CEQFLVT 234
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 20-196 1.35e-09

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: 56.11  E-value: 1.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  20 DTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPE-SPAKLSDFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtit 98
Cdd:cd08871  21 STDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVLHDPEYRKTWDSNMIESFDICQLNPNNDIGY--- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  99 qsFAVGS---ISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEM 175
Cdd:cd08871  98 --YSAKCpkpLKNRDFVNLRSWLEFGGEY-IIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKG--CTLTYVTQNDP 172

                       170       180
                ....*....|....*....|.
gi 21040261 176 RGKLspsiiektmPSNLVNFI 196
Cdd:cd08871 173 KGSL---------PKWVVNKA 184
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 9-153 1.12e-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: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   9 QTAQEVLGYNrDTSGWKV-------VKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKLSDFLYQTGDRITWDKSLQVY 81
Cdd:cd08913  38 PSNQVYLSYN-NVSALKMlvakdnwVLSSEKNQVRLYTLEEDKFLSFKVEMVVHVDAAQAFLLLSDLRRRPEWDKHYRSC 116

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21040261  82 NMVHRIDSDTFICHTITQSFAVGSiSPRDFIDLVYIKR--YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGF 153
Cdd:cd08913 117 ELVQQVDEDDAIYHVTSPSLSGHG-KPQDFVILASRRKpcDNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGF 189
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 22-161 2.91e-05

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: 43.73  E-value: 2.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  22 SGWKVVKTSKKITVSSKASRKFHGnlYRVEGIIpESPAKLS-DFLYQTGDRITWDKSLQVYNMVHRIDSDTFICHtITqS 100
Cdd:cd08914  56 SGWEVTSTVEKIKIYTLEEHDVLS--VWVEKHV-KRPAHLAyRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYH-IT-C 130

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21040261 101 FAVGSISPRDFIDLVYiKRY---EGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEEN 161
Cdd:cd08914 131 PIVNNDKPKDLVVLVS-RRKplkDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSN 193
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 18-145 1.03e-04

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: 41.89  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  18 NRDTSGWKVVKTSKKITVSSKASRKFHGNLYRVEGIIPESPAKlsDFLYQTGD---RITWDKSLQVYNMVHR-IDSDTFI 93
Cdd:cd08911  17 NQEPDGWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTAR--DFLNVQLDleyRKKWDATAVELEVVDEdPETGSEI 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21040261  94 CHTITQ---SFAvgsisPRDFidlVYIKRY----EGNMNIISSKSVDFPEYPPSSNYIR 145
Cdd:cd08911  95 IYWEMQwpkPFA-----NRDY---VYVRRYiideENKLIVIVSKAVQHPSYPESPKKVR 145
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 8-136 4.22e-04

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). 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. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 39.98  E-value: 4.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261   8 QQTAQEVLGYNRDTS-GWKVVKTSKKITVSSKASRKFHG-NLYRVEGIIPESPAKLSDFLYQtgDRITWDKSLQVYNMVH 85
Cdd:cd08869   4 ERCVQDLLREARDKSkGWVSVSSSDHVELAFKKVDDGHPlRLWRASTEVEAPPEEVLQRILR--ERHLWDDDLLQWKVVE 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21040261  86 RIDSDTFICHTITQSFAvgSISPRDFidlVYIKRYEGNMN----IISSKSVDFPE 136
Cdd:cd08869  82 TLDEDTEVYQYVTNSMA--PHPTRDY---VVLRTWRTDLPkgacVLVETSVEHTE 131
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 23-189 1.76e-03

Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). 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. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of 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: 176879  Cd Length: 209  Bit Score: 38.13  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  23 GWKVVKTSKKITVSSKASRKFHGNL----YRVEGIIPE-SPAKLSDFLYQTGDRITWDKSLQVYNMVHR-IDSDTFICHT 96
Cdd:cd08870  23 AWQQVMDKSTPDMSYQAWRRKPKGTglyeYLVRGVFEDcTPELLRDFYWDDEYRKKWDETVIEHETLEEdEKSGTEIVRW 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040261  97 ITQsFAVgSISPRDFIdlVYIKRYE--GNMNIISSKSVDFPEYPPS-SNYIRGY-------NHPCGFVCSPME----ENP 162
Cdd:cd08870 103 VKK-FPF-PLSDREYV--IARRLWEsdDRSYVCVTKGVPYPSVPRSgRKRVDDYesslvirAVKGDGQGSACEvtyfHNP 178

                       170       180
                ....*....|....*....|....*..
gi 21040261 163 AYSKLVMFVQTEMRgKLSPSIIEKTMP 189
Cdd:cd08870 179 DGGIPRELAKLAVK-RGMPGFLKKLEN 204
 
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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