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Conserved domains on  [gi|56090196|ref|NP_956514|]
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START domain containing 14 [Danio rerio]

Protein Classification

START domain-containing protein( domain architecture ID 10172287)

START (steroidogenic acute regulatory protein (StAR)-related lipid transfer) domain-containing protein may bind lipids; similar to STARD10 that may play metabolic roles in sperm maturation or fertilization

CATH:  3.30.530.20
Gene Ontology:  GO:0008289
PubMed:  10322415|31927098
SCOP:  4002052

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-234 8.39e-132

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: 371.97  E-value: 8.39e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196   3 RGSGILPDESMFAEFKRQCLSTENWVNKYDKNDMEVWVEQAPLSAsinnkgnyskVHKIRCQINIKDVSAATMYDVLHDG 82
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSS----------IKMIKVSAIFPDVPAETLYDVLHDP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  83 QYRKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMT 162
Cdd:cd08871  71 EYRKTWDSNMIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLT 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56090196 163 GYLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPAWKAANSPDHKPWLYPIQ 234
Cdd:cd08871 151 GYLIRPTGPKGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-234 8.39e-132

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: 371.97  E-value: 8.39e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196   3 RGSGILPDESMFAEFKRQCLSTENWVNKYDKNDMEVWVEQAPLSAsinnkgnyskVHKIRCQINIKDVSAATMYDVLHDG 82
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSS----------IKMIKVSAIFPDVPAETLYDVLHDP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  83 QYRKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMT 162
Cdd:cd08871  71 EYRKTWDSNMIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLT 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56090196 163 GYLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPAWKAANSPDHKPWLYPIQ 234
Cdd:cd08871 151 GYLIRPTGPKGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START pfam01852
START domain;
7-217 8.24e-31

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 114.04  E-value: 8.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     7 ILPDESMFAEFKRQCLSTENWVNKYDKndmevwvEQAPLSASINNKGNYskvHKIRCQINIKDVSAATMYDVLHDGQYRK 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSN-------ENGDVVLQIVEPDHG---EASRASGVVPMVAALLVAELLKDMEYRA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196    87 TWDPTMLESFDIARLAHNADVGYYS--WICPKPLKNRDVVTLRSW-QASENEYVIINFSVKHPKYPPRKDLVRAVSLMTG 163
Cdd:pfam01852  71 QWDKDVRSAETLEVISSGGDLQYYVaaLVAPSPLSPRDFVFLRYWrRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56090196   164 YLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPA 217
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 11-217 6.38e-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: 100.97  E-value: 6.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     11 ESMFAEFKRQCLSTENWVNKYDKndmevwvEQAPLSASINNKGNYSkVHKIRCQINIKDVSAATMYDVLHDGQYRKTWDP 90
Cdd:smart00234   4 EAAAELLKMAAASEEGWVLSSEN-------ENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADLVEELMDDLEYRPEWDK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     91 TMLESFDIARLAHNADVGYY---SWIcpKPLKNRDVVTLRSWQASENE-YVIINFSVKHPKYPPRKDLVRAVSLMTGYLI 166
Cdd:smart00234  76 NVAKAETLEVIDNGTVIYHYvskFAA--GPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLI 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 56090196    167 KPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPA 217
Cdd:smart00234 154 EPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 3-234 8.39e-132

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: 371.97  E-value: 8.39e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196   3 RGSGILPDESMFAEFKRQCLSTENWVNKYDKNDMEVWVEQAPLSAsinnkgnyskVHKIRCQINIKDVSAATMYDVLHDG 82
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSS----------IKMIKVSAIFPDVPAETLYDVLHDP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  83 QYRKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMT 162
Cdd:cd08871  71 EYRKTWDSNMIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLT 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56090196 163 GYLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPAWKAANSPDHKPWLYPIQ 234
Cdd:cd08871 151 GYLIRPTGPKGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 11-213 5.71e-46

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: 152.88  E-value: 5.71e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  11 ESMFAEFKRQCLSTENWVNKYDKNDMEVWVEQaplsasinNKGNYSKVHKIRCQINikdVSAATMYDVLHDGQYRKTWDP 90
Cdd:cd00177   1 EEAIEELLELLEEPEGWKLVKEKDGVKIYTKP--------YEDSGLKLLKAEGVIP---ASPEQVFELLMDIDLRKKWDK 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  91 TMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSW-QASENEYVIINFSVKHPKYPPRKDLVRAVSLMTGYLIKPT 169
Cdd:cd00177  70 NFEEFEVIEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRrKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 56090196 170 GPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQ 213
Cdd:cd00177 150 DPGKTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START pfam01852
START domain;
7-217 8.24e-31

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 114.04  E-value: 8.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     7 ILPDESMFAEFKRQCLSTENWVNKYDKndmevwvEQAPLSASINNKGNYskvHKIRCQINIKDVSAATMYDVLHDGQYRK 86
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSN-------ENGDVVLQIVEPDHG---EASRASGVVPMVAALLVAELLKDMEYRA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196    87 TWDPTMLESFDIARLAHNADVGYYS--WICPKPLKNRDVVTLRSW-QASENEYVIINFSVKHPKYPPRKDLVRAVSLMTG 163
Cdd:pfam01852  71 QWDKDVRSAETLEVISSGGDLQYYVaaLVAPSPLSPRDFVFLRYWrRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSG 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56090196   164 YLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPA 217
Cdd:pfam01852 151 YLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 11-217 6.38e-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: 100.97  E-value: 6.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     11 ESMFAEFKRQCLSTENWVNKYDKndmevwvEQAPLSASINNKGNYSkVHKIRCQINIKDVSAATMYDVLHDGQYRKTWDP 90
Cdd:smart00234   4 EAAAELLKMAAASEEGWVLSSEN-------ENGDEVRSIFSPGRKP-GEAFRLVGVVPMVCADLVEELMDDLEYRPEWDK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196     91 TMLESFDIARLAHNADVGYY---SWIcpKPLKNRDVVTLRSWQASENE-YVIINFSVKHPKYPPRKDLVRAVSLMTGYLI 166
Cdd:smart00234  76 NVAKAETLEVIDNGTVIYHYvskFAA--GPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLI 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 56090196    167 KPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNYPA 217
Cdd:smart00234 154 EPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCA 204
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 22-200 2.47e-18

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: 80.86  E-value: 2.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  22 LSTENWvnKYDKNDmevwvEQAPLSASINNKGnYSKVHKIRCQInikDVSAATMYDVLHDGQYR-KTWDPTMLESFDIAR 100
Cdd:cd08868  21 LTDPGW--KLEKNT-----TWGDVVYSRNVPG-VGKVFRLTGVL---DCPAEFLYNELVLNVESlPSWNPTVLECKIIQV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 101 LAHNADVGYYswiCPKPLKN-----RDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMTGYLIKPTG--PQS 173
Cdd:cd08868  90 IDDNTDISYQ---VAAEAGGglvspRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPnnPNK 166

                       170       180
                ....*....|....*....|....*...
gi 56090196 174 CIFTYLSQADPKGSLPKWVVNKA-SQVL 200
Cdd:cd08868 167 CNFTWLLNTDLKGWLPQYLVDQAlASVL 194
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 62-206 1.40e-17

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: 78.50  E-value: 1.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  62 RCQINIKDVSAATMYDVLHDgqyRKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQASENEY--VII 139
Cdd:cd08869  47 RASTEVEAPPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGacVLV 123

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56090196 140 NFSVKHPK-YPPRkdLVRAVSLMTGYLIKPTGPQSCIFTYLSQADPKGSLPKWvVNKA-SQVLAPKVLR 206
Cdd:cd08869 124 ETSVEHTEpVPLG--GVRAVVLASRYLIEPCGSGKSRVTHICRVDLRGRSPEW-YNKVyGHLCARELLR 189
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 23-215 2.21e-17

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: 78.10  E-value: 2.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  23 STENWVNKYDKNDMEVWVEQAPlsasinNKGNYS-KVHKircqiNIKDVSAATMYDVLHDGQYRKTWDPTM--LESFDIA 99
Cdd:cd08911  19 EPDGWEPFIEKKDMLVWRREHP------GTGLYEyKVYG-----SFDDVTARDFLNVQLDLEYRKKWDATAveLEVVDED 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 100 RLAHnADVGYYSWICPKPLKNRDVVTLRSWQASENE--YVIINFSVKHPKYPPRKDLVRAV---SLMTgylIKPTGPQSC 174
Cdd:cd08911  88 PETG-SEIIYWEMQWPKPFANRDYVYVRRYIIDEENklIVIVSKAVQHPSYPESPKKVRVEdywSYMV---IRPHKSFDE 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 56090196 175 -----IFTYLSqaDPKGSLPK----WVVNKAsqvlAPKVLRSAHKAGQNY 215
Cdd:cd08911 164 pgfefVLTYFD--NPGVNIPSyitsWVAMSG----MPDFLERLRNAALKY 207
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 25-206 7.39e-13

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. 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. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). 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.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 65.37  E-value: 7.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  25 ENWVNKYDKNDMEVWVEQAPlsasinnkgnYSKVHKIRCQINIkDVSAATMYDVLHDGQ-YRKtWDPTMLESFDIARLAH 103
Cdd:cd08876  17 GDWQLVKDKDGIKVYTRDVE----------GSPLKEFKAVAEV-DASIEAFLALLRDTEsYPQ-WMPNCKESRVLKRTDD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 104 NADVGYYSWICPKPLKNRDVVTL-RSWQASENEYVIINFSVKHPKYPPRKDLVRaVSLMTG-YLIKPTGPQSCIFTYLSQ 181
Cdd:cd08876  85 NERSVYTVIDLPWPVKDRDMVLRsTTEQDADDGSVTITLEAAPEALPEQKGYVR-IKTVEGqWTFTPLGNGKTRVTYQAY 163

                       170       180
                ....*....|....*....|....*
gi 56090196 182 ADPKGSLPKWVVNKASQVLAPKVLR 206
Cdd:cd08876 164 ADPGGSIPGWLANAFAKDAPYNTLE 188
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 67-215 2.02e-12

Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) 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. 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 have a mitochondrial function.


Pssm-ID: 176919  Cd Length: 207  Bit Score: 64.43  E-value: 2.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  67 IKDVSAATMYDVLHDGQYRKTWDPTMLESFDiaRLAHNADVGYYSWICPKPLKNRDVVTLRSWQASENEY----VIINFS 142
Cdd:cd08910  57 LEDCSPSLLADVYMDLEYRKQWDQYVKELYE--KECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGrkiwVILARS 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56090196 143 VKHPKYPPRKDLVRAVSLMTGYLIKPTGPQSC-IFTYLSQaDPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNY 215
Cdd:cd08910 135 TSLPQLPEKPGVIRVKQYKQSLAIESDGKKGSkVFMYYFD-NPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 85-206 1.35e-10

C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) 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. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176918  Cd Length: 205  Bit Score: 59.55  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  85 RKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQAS--ENEYVIINFSVKHPKYPPRKDlVRAVSLMT 162
Cdd:cd08909  75 RHLWDEDFLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWRTDlpKGACSLVSVSVEHEEAPLLGG-VRAVVLDS 153

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 56090196 163 GYLIKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLR 206
Cdd:cd08909 154 QYLIEPCGSGKSRLTHICRVDLKGHSPEWYNKGFGHLCAAEAAR 197
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 88-206 3.64e-10

C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) 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. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176917  Cd Length: 204  Bit Score: 58.10  E-value: 3.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  88 WDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQAS--ENEYVIINFSVKHPKYPPRKdlVRAVSLMTGYL 165
Cdd:cd08908  78 WDVDLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNlpKGACALLATSVDHDRAPVAG--VRVNVLLSRYL 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56090196 166 IKPTGPQSCIFTYLSQADPKGSLPKWVVNKASQVLAPKVLR 206
Cdd:cd08908 156 IEPCGSGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVK 196
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 85-191 2.06e-09

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup 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) 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. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 56.08  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  85 RKTWDPTMLESFDIARLAHNADVGYYSWICPKPLKNRDVVTLRSWQAS--ENEYVIINFSVKHPKYPPRKDlVRAVSLMT 162
Cdd:cd08907  75 RHLWDEDLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDlpRGGCLLVSQSVDHDNPQLEAG-VRAVLLTS 153

                        90       100
                ....*....|....*....|....*....
gi 56090196 163 GYLIKPTGPQSCIFTYLSQADPKGSLPKW 191
Cdd:cd08907 154 QYLIEPCGMGRSRLTHICRADLRGRSPDW 182
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 69-215 2.51e-08

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: 52.77  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  69 DVSAATMYDVLHDGQYRKTWDPTMLESFDIARLAHNA-DVGYysWIC--PKPLKNRDVVTLRS-WQASENEYVIINFSVK 144
Cdd:cd08870  60 DCTPELLRDFYWDDEYRKKWDETVIEHETLEEDEKSGtEIVR--WVKkfPFPLSDREYVIARRlWESDDRSYVCVTKGVP 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56090196 145 HPKYPPRKDL-VRAVSLMTGYLIKPTGPQ--SCIFTYLSQadPKGSLPKWVVNKASQVLAPKVLRSAHKAGQNY 215
Cdd:cd08870 138 YPSVPRSGRKrVDDYESSLVIRAVKGDGQgsACEVTYFHN--PDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 70-185 6.51e-08

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: 52.21  E-value: 6.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  70 VSAATMYDVLHDGQYRKTWDPTMLESFDIARLAHnaDVGYYSWICP-----KPlknRDVVTLRSWQ---ASENEYVIINF 141
Cdd:cd08873  87 TCASDAFDLLSDPFKRPEWDPHGRSCEEVKRVGE--DDGIYHTTMPsltseKP---NDFVLLVSRRkpaTDGDPYKVAFR 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 56090196 142 SVKHPKYPPRKDLVRAVSLMTGYLIKPTGPQSCIFTYLSQADPK 185
Cdd:cd08873 162 SVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPK 205
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 70-189 7.45e-08

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: 51.82  E-value: 7.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  70 VSAATMYDVLHDGQYRKTWDPTMLESFDIARLAHNADVGYYSwiCP--KPLKNRDVVTL---RSWQASENEYVIINFSVK 144
Cdd:cd08914  88 RPAHLAYRLLSDFTKRPLWDPHFLSCEVIDWVSEDDQIYHIT--CPivNNDKPKDLVVLvsrRKPLKDGNTYVVAVKSVI 165

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 56090196 145 HPKYPPRKDLVRAVSLMTGYLIKPTGPQSCIFTYLSQADPkGSLP 189
Cdd:cd08914 166 LPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISA-SILP 209
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 121-196 8.38e-07

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: 48.70  E-value: 8.38e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56090196 121 RDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMTGYLI--KPTGPQSCIFTYLSQADPKGSLPKWVVNKA 196
Cdd:cd08906 113 RDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVlkSASNPSVCTFIWILNTDLKGRLPRYLIHQS 190
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 67-206 1.69e-06

Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD11 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. STARD11 can mediate transfer of the natural ceramide isomers, dihydroceramide and phytoceramide, as well as ceramides having C14, C16, C18, and C20 chains. They can also transfer diacylglycerol, but with a lower efficiency. STARD11 is synthesized from two major transcripts: a larger one encoding Goodpasture antigen-binding protein (GPBP)/ceramide transporter long form (CERTL); and a smaller one encoding GPBPdelta26/CERT, which is deleted for 26 amino acids. Both splicing variants mediate ceramide transfer from the ER to the Golgi, in a non-vesicular manner. It is likely that these two carry out different functions in specific sub-cellular locations. These proteins have roles in brain homeostasis and disease processes. GPBP/CERTL exists in multiple isoforms originating from alternative translation initiation sites and post-translational modifications. Goodpasture syndrome is a human disorder caused by antibodies directed against the a3-chain of collagen type IV. GPBP/CERTL binds and phosphorylates this antigen. The human gene encoding STARD11 is referred to as COL4A3BP referring to its collagen binding function. It is unknown whether the ceramide-transfer function of GPBP/CERTL is related to this collagen interaction. The expression of GPBP/CERTL is elevated in these and other spontaneous autoimmune disorders including cutaneous lupus erythematosus, pemphigoid, and lichen planus. GPBL/CERTL contains an N-terminal pleckstrin homology domain (PH), which targets the protein to the Golgi, a middle region containing two serine-rich domains (SR1, SR2), a FFAT (two phenylalanine amino acids in an acidic tract) motif which is involved in endoplasmic reticulum targeting, and this C-terminal SMART domain. The shorter splicing variant, CERT, lacks the SR2 domain.


Pssm-ID: 176881  Cd Length: 235  Bit Score: 47.72  E-value: 1.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  67 IKDVSAATMYDVLHDGQYRKTWDPTmLESFD-IARLAHNADVGYYS----WicpkPLKNRDVV---TLRSWQASENE--- 135
Cdd:cd08872  60 VKGVTGHEVCHYFFDPDVRMDWETT-LENFHvVETLSQDTLIFHQThkrvW----PAAQRDALfvsHIRKIPALEEPnah 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 136 --YVIINFSVKHPKYPPRKDLVRA---VSLMTGYLIKPT---GPQS-----CIFTYLSQADPKGSLPKWVVNKASQVLAP 202
Cdd:cd08872 135 dtWIVCNFSVDHDSAPLNNKCVRAkltVAMICQTFVSPPdgnQEITrdnilCKITYVANVNPGGWAPASVLRAVYKREYP 214


                ....
gi 56090196 203 KVLR 206
Cdd:cd08872 215 KFLK 218
DUF3074 pfam11274
Protein of unknown function (DUF3074); This eukaryotic family of proteins has no known ...
 115-206 3.56e-06

Protein of unknown function (DUF3074); This eukaryotic family of proteins has no known function but appears to be part of the START superfamily.


Pssm-ID: 431775  Cd Length: 181  Bit Score: 46.09  E-value: 3.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196   115 PKPLKNRDVVTL---------RSWQASENEYVIINFSVK-HPKYPPRKDLVRA--VSLMTGYLIkPTGPQSCIFTY---- 178
Cdd:pfam11274  67 PGPLTPRDFVVLlltadlppeESPGSEHAEFMVVSIPVDdHPDAPPRKGFVRGqyESVERIREI-PVDDEYDEETGpvew 145

                          90       100       110
                  ....*....|....*....|....*....|....
gi 56090196   179 --LSQADPKGSLPKWVVNKA--SQVL--APKVLR 206
Cdd:pfam11274 146 imATASDAGGSIPRWLQEKGtpGAIAkdVGKFLD 179
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 121-207 1.37e-04

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: 42.13  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 121 RDVVTLRSWQASENEYVIINFSVKHPKYPPRKDLVRAVSLMTGYLIKPTG--PQSCIFTYLSQADPKGSLPKWVVNKA-- 196
Cdd:cd08905 113 RDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPLAgdPSKTKLTWLLSIDLKGWLPKSIINQVls 192

                        90
                ....*....|..
gi 56090196 197 -SQVLAPKVLRS 207
Cdd:cd08905 193 qTQVDFANHLRQ 204
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 71-196 8.85e-04

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: 39.51  E-value: 8.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  71 SAATMYDVLHDGQYRKTWDptmlESFDIARLAHNADVGyySWICPK--------PLKNRDVVTLRSWQASENEYVIIN-F 141
Cdd:cd08904  57 SPAKLIQFMYQPEHRIKWD----KSLQVYKMLQRIDSD--TFICHTitqsfamgSISPRDFVDLVHIKRYEGNMNIVSsV 130

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 56090196 142 SVKHPKYPPRKDLVRAVSLMTGYLIKP--TGPQSCIFTYLSQADPKGSLPKWVVNKA 196
Cdd:cd08904 131 SVEYPQCPPSSNYIRGYNHPCGYVCSPlpENPAYSKLVMFVQPELRGNLSRSVIEKT 187
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 70-189 2.55e-03

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 38.31  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  70 VSAATMYDVLHDGQYRKTWDPTMLESFDIARLahNADVGYYSWICP---KPLKNRDVVTLRSWQA---SENEYVIINFSV 143
Cdd:cd08913  91 VDAAQAFLLLSDLRRRPEWDKHYRSCELVQQV--DEDDAIYHVTSPslsGHGKPQDFVILASRRKpcdNGDPYVIALRSV 168

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 56090196 144 KHPKYPPRKDLVRAVSLMTGYLIKPTGPQSCIFTYLSQADPkGSLP 189
Cdd:cd08913 169 TLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATP-GVLP 213
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 24-196 4.33e-03

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: 37.44  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196  24 TENWVNKYDKNDMEVWVEqaplsASINNKGNyskVHKIRCQInikDVSAATMYDVL--HDGQYRKTWDPTMLESFDIARL 101
Cdd:cd08867  21 TDGWKVLKTVKNITVSWK-----PSTEFTGH---LYRAEGIV---DALPEKVIDVIipPCGGLRLKWDKSLKHYEVLEKI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090196 102 AHNADVGYYswICPKPLKN----RDVVTLRSWQASENEYVIIN-FSVKHPKYPPRKDLVRAVSLMTGYLIKPT--GPQSC 174
Cdd:cd08867  90 SEDLCVGRT--ITPSAAMGlispRDFVDLVYVKRYEDNQWSSSgKSVDIPERPPTPGFVRGYNHPCGYFCSPLkgSPDKS 167

                       170       180
                ....*....|....*....|..
gi 56090196 175 IFTYLSQADPKGSLPKWVVNKA 196
Cdd:cd08867 168 FLVLYVQTDLRGMIPQSLVESA 189
 
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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