ID A0A0V0UNS7_9BILA Unreviewed; 604 AA.
AC A0A0V0UNS7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Oxysterol-binding protein {ECO:0000256|RuleBase:RU003845};
GN Name=osbpl9 {ECO:0000313|EMBL:KRX52998.1};
GN ORFNames=T09_13837 {ECO:0000313|EMBL:KRX52998.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52998.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52998.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52998.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the OSBP family.
CC {ECO:0000256|RuleBase:RU003844}.
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:KRX52998.1}.
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DR EMBL; JYDN01000217; KRX52998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0UNS7; -.
DR Proteomes; UP000054681; 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; cd13290; PH_ORP9; 1.
DR Gene3D; 1.10.287.2720; -; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10972:SF102; OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 9; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW ECO:0000256|RuleBase:RU003845};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003845}.
FT DOMAIN 1..96
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 209..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 68541 MW; 5CA29529A4D909AB CRC64;
MEGPLSKWTN VIEGWQFRLF VLDETAGTLS YYTSQDKMKK GQVRGCVRLK GAVVGIDDED
DCTFTITVDQ KMFHFQVAKD YEERDRWISA LEKTIQEHSD IYRYRFKHTN VGVARSSSSY
IQFEKRIAQV DTYLQMVIDR IQHLESFVAD LKPEEESGKI SRIIQIANEM LDSVKHSVVL
LQYAKNEIVP EESKALVEAN SAISGEQKLN AGPLSNLEPL QKSDIKPPLE EEKISDDDET
QRPTDSSLLS TVENIQFKDE PILSYSKSDE EDELYYDSVE QMAMLVDDMQ IESRESEMNN
GIVNQLNNSS TGEADDFPYV LHNEPQFTDP GVNFDTLYED DAEDELEDTR EHGSVIMHLL
SQLSVGMDLT KIVLPTYILE RRSLLEIIAD CELADDRMLA VVRWYLSTFY GGRRSGLAKK
PYNPILGEVF ACCWKSPSVK ASDEKVADGP VPTATVNQIT FVGEQVSHHP PVSAFYVEHP
SKKLQLNGHI WTKSKFLGLS IAVHNVGQTC LSVLERGEEY LFDFPNGYGR SILTTPWVEF
GGKCSIRCEK TSYHADIEFS TKTFYSGKAH CLKVEVYRPA EKSPYATIRG QWNGVMHIKT
NQTV
//
