ID A0A3A2ZZ85_9EURO Unreviewed; 935 AA.
AC A0A3A2ZZ85;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE SubName: Full=Oxysterol binding protein {ECO:0000313|EMBL:RJE26687.1};
GN ORFNames=PHISCL_01011 {ECO:0000313|EMBL:RJE26687.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE26687.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|ARBA:ARBA00008842}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJE26687.1}.
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DR EMBL; MVGC01000017; RJE26687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZZ85; -.
DR STRING; 2070753.A0A3A2ZZ85; -.
DR OrthoDB; 1854502at2759; -.
DR Proteomes; UP000266188; Unassembled WGS sequence.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005319; F:lipid transporter activity; IEA:UniProtKB-ARBA.
DR GO; GO:0032934; F:sterol binding; IEA:TreeGrafter.
DR GO; GO:0006897; P:endocytosis; IEA:TreeGrafter.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IEA:TreeGrafter.
DR GO; GO:0006887; P:exocytosis; IEA:TreeGrafter.
DR GO; GO:0030011; P:maintenance of cell polarity; IEA:TreeGrafter.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:TreeGrafter.
DR CDD; cd13289; PH_Osh3p_yeast; 1.
DR FunFam; 2.30.29.30:FF:000369; Oxysterol binding protein; 1.
DR FunFam; 2.40.160.120:FF:000013; Oxysterol binding protein; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 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:SF203; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..149
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT DOMAIN 176..270
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 51..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 854..884
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..82
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..542
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 102981 MW; 5301632604D67F8A CRC64;
MAGLEVLEVH SKSYLVRWIN VKPDHTISWS IQPHKKSLNF GIFKHPGHSA VLNSSNGPTS
DSHSTDSNEN LPSTVSSSRQ SSSTSVIDKL TGIGLKSIKW IGKCEADKIA QGTYDVPSNE
GGNYALVIDN TFSKQISKTV TLVLFTYPTG ESSEPSARGG ANNIAGKPAH SGSSSPAGHT
GLLQKRRRKR HQGWARRYFS LDFTTSTLSY YHDRNTSTLR GSIPLSLAAV ATNEKSREIS
VDSGAEIWHL RASNEQDFIS WKRALEKASS KASAEDDSQP DQLLHVPSPR APSAAEDRDW
DKVRVLVGQL SGSRDTVRQL AKDTDPKYFG AAERPRGRSS SPNPRNAEAN GEDYFTSRER
RPFWRRKSSA NSQPGGKRST PVTSSPQLVV PGSADTASLT GDRKPGSVAS QTDQDDVHDR
LMALLHDLDR IALEFSSLVA ERKRRRYPVP SQSRRSMESD MSQEFFDAID GGDASPLLTI
QDSDDDEDVD NVDAARQTEE EEAVEDNAPS DSEDELHETS TISGHRDQST FFPTKPKSLT
PLPLGRVERR TNITAPTVLP PSLIGFLRKN VGKDLSQISM PVSANEPLSL LQKAAEVMEY
SNLLDKAAST TGSVERLMYV TAFALSSLAC NRVKERAIRK PFNPMLGETY ELVREDRGFR
FIAEKVSHRP VQLAYLADSK DWSLAQSPMP SQKFWGKSAE IITEGKFRLT LHATGEHFSW
PAATSFLRNI IAGEKYVEPV GELPVLNEST GQKSVSTFKV GGMFSGRSEE VSTKAIDSSG
KELPLGLTGT WTSSLQLTKN GSTTGGPIWS AGALVPNAPK HYGFTAFAAT LNEITLIEQD
KLPPTDCRLR PDQKALEDND LDKAEEVKVK LEEAQRSRRR EMESKGESWS PRWFTRVEDD
SADGEVAWRL KTGKDGYWEE RAKGTWSGVV PVLKI
//
