ID A0A0J7AXD6_COCIT Unreviewed; 967 AA.
AC A0A0J7AXD6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Oxysterol-binding protein 1 {ECO:0000313|EMBL:KMP02042.1};
GN ORFNames=CIRG_02181 {ECO:0000313|EMBL:KMP02042.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP02042.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
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DR EMBL; DS028093; KMP02042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7AXD6; -.
DR STRING; 404692.A0A0J7AXD6; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd13289; PH_Osh3p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF216; OXYSTEROL-BINDING PROTEIN HOMOLOG 3; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..145
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT DOMAIN 215..309
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 107624 MW; 4CA01C6BD179EB0E CRC64;
MAGMEEIEIH SKSYLVRWIN VSGEHTISWS IQPHKKSLNF GIFKHPGTTG TLTATSASIH
SSSDFGDGRE NGRPGNASSS VVTEKLKGIG LKPIRWVGKC EADKISQGTY DVGSGEGGNY
ALVFDNTFSK QISKTATFVL LTYPTHCPPR SGHQIHHSQA GLGYAAVTSA LTRSNPNIAS
GASDSTESLR NSRGLANSQS KTGSRGSDSP FPFHAQLHTG ILQKRRRKRH QGFARRFFSL
DFNTSTLSYY HDRNSSALRG AIPLTLAAIA TNSDTREISI DSGAEIWHLR ALNEQDFNVW
KRALEKASKI SEDVVQPEPK GKVRTHSIPT RRQSMITQDT KSWTEVGWLA EKVAMARDTV
RQLAKDTDPK YLPYSSDRPH VNTRQMPQQT DGTNEMADRE KRSFWKLKYR NDNQSAQRAV
SHGEPFGSYK PPMEMPNRGR DPVHDRLMAL LQELDSVVSD FSSLLEKKRP RPSRPPSIRT
RPSIESDVSE EFFDANDGHC SPLLTMHRDS EDEDEKSVAA ETAVGDESSL SGSDIEERDD
FLKFRHDNSS SLFPTKPKSL IPLPVENVVR RKTVLAPTVM PPSLIGFLRK NVGKDLSTIS
MPVSANEPIS LLQRAAEQFE YSRLLDKAAS ATDALERLIY VTAFAISPFS NMRVKERSIR
KPFNPMLGET YELVRGDLGF RFIAEKVSHR PVQLAYQADS KDWSYAQSPK PTQKFWGKSA
EIITEGKVRL TLHSSGEHFS WSPGTSFLRN IIAGEKYVEP VGEMCIVNET TGQKTVVTFK
AGGMFSGRSE EVTVKAFDTH GDELPLGLQG SWTTSLQLTE HGRETNHTIW AAGSLVDKAP
KHYGFTVFAA SLNEITAVEK AKLPPTDSRL RPDQRALENG DVDQAENLKA LLEEKQRHRR
KEMEAVGEVW RSRWFTKVGG TVDGANGTGT GDDDDDGVMW KLNTGKDGYW EERARGQWPG
TVPVFKL
//