ID   OSBL1_RAT               Reviewed;         950 AA.
AC   Q8K4M9;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Oxysterol-binding protein-related protein 1;
DE            Short=ORP-1;
DE            Short=OSBP-related protein 1;
GN   Name=Osbpl1a; Synonyms=Orp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=10965890; DOI=10.1210/endo.141.9.7685;
RA   Nishi N., Shoji H., Miyanaka H., Nakamura T.;
RT   "Androgen-regulated expression of a novel member of the aldo-keto reductase
RT   superfamily in regrowing rat prostate.";
RL   Endocrinology 141:3194-3199(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 472-481 IN COMPLEX WITH VAPA, AND
RP   INTERACTION WITH VAPA.
RX   PubMed=16004875; DOI=10.1016/j.str.2005.04.010;
RA   Kaiser S.E., Brickner J.H., Reilein A.R., Fenn T.D., Walter P.,
RA   Brunger A.T.;
RT   "Structural basis of FFAT motif-mediated ER targeting.";
RL   Structure 13:1035-1045(2005).
CC   -!- FUNCTION: Binds phospholipids; exhibits strong binding to phosphatidic
CC       acid and weak binding to phosphatidylinositol 3-phosphate. Stabilizes
CC       GTP-bound RAB7A on late endosomes/lysosomes and alters functional
CC       properties of late endocytic compartments via its interaction with
CC       RAB7A. Binds 25-hydroxycholesterol and cholesterol.
CC       {ECO:0000250|UniProtKB:Q9BXW6}.
CC   -!- SUBUNIT: Interacts with VAPA (PubMed:16004875). Interacts with the GTP-
CC       bound form of RAB7A (By similarity). Interacts with OAS1B (By
CC       similarity). Interacts (via FFAT motif) with MOSPD2 (via MSP domain)
CC       (By similarity). {ECO:0000250|UniProtKB:Q91XL9,
CC       ECO:0000250|UniProtKB:Q9BXW6, ECO:0000269|PubMed:16004875}.
CC   -!- INTERACTION:
CC       Q8K4M9; Q9Z270: Vapa; NbExp=6; IntAct=EBI-15554439, EBI-2909425;
CC   -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000250|UniProtKB:Q9BXW6}.
CC       Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.
CC       {ECO:0000250|UniProtKB:Q9BXW6}.
CC   -!- TISSUE SPECIFICITY: Detected in prostate and liver.
CC       {ECO:0000269|PubMed:10965890}.
CC   -!- DOMAIN: The FFAT motif is required for interaction with MOSPD2.
CC       {ECO:0000250|UniProtKB:Q9BXW6}.
CC   -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR   EMBL; AB089316; BAC07227.1; -; mRNA.
DR   RefSeq; NP_742020.1; NM_172023.1.
DR   PDB; 1Z9O; X-ray; 1.90 A; G/H/I/J/K/L=472-481.
DR   PDBsum; 1Z9O; -.
DR   AlphaFoldDB; Q8K4M9; -.
DR   SMR; Q8K4M9; -.
DR   DIP; DIP-48447N; -.
DR   ELM; Q8K4M9; -.
DR   IntAct; Q8K4M9; 1.
DR   STRING; 10116.ENSRNOP00000065976; -.
DR   PhosphoSitePlus; Q8K4M9; -.
DR   PaxDb; Q8K4M9; -.
DR   PRIDE; Q8K4M9; -.
DR   GeneID; 259221; -.
DR   KEGG; rno:259221; -.
DR   CTD; 114876; -.
DR   RGD; 628888; Osbpl1a.
DR   eggNOG; KOG2209; Eukaryota.
DR   InParanoid; Q8K4M9; -.
DR   OrthoDB; 863978at2759; -.
DR   PhylomeDB; Q8K4M9; -.
DR   Reactome; R-RNO-192105; Synthesis of bile acids and bile salts.
DR   Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR   EvolutionaryTrace; Q8K4M9; -.
DR   PRO; PR:Q8K4M9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; ISO:RGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0044232; C:organelle membrane contact site; ISO:RGD.
DR   GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR   GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR   GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PTHR10972; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13857; Ank_5; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF144000; SSF144000; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Coiled coil; Endosome; Lipid transport;
KW   Lipid-binding; Reference proteome; Repeat; Transport.
FT   CHAIN           1..950
FT                   /note="Oxysterol-binding protein-related protein 1"
FT                   /id="PRO_0000228846"
FT   REPEAT          47..76
FT                   /note="ANK 1"
FT   REPEAT          80..109
FT                   /note="ANK 2"
FT   REPEAT          175..204
FT                   /note="ANK 3"
FT   DOMAIN          235..334
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1..237
FT                   /note="Interaction with RAB7A"
FT                   /evidence="ECO:0000250"
FT   REGION          795..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..463
FT                   /evidence="ECO:0000255"
FT   COILED          877..913
FT                   /evidence="ECO:0000255"
FT   MOTIF           469..483
FT                   /note="FFAT"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BXW6"
FT   COMPBIAS        795..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   950 AA;  107765 MW;  CA312E8C7326B61F CRC64;
     MNTEAEQQLL HHARNGNAEE VRKLLEAMAR AEVVADIDCK GRSKSNLGWT PLHLACYFGH
     KQVVQDLLKA GAKVNMLNDM GDTPLHRAAF TGRKELVMLL LEYNADTTVV NGSGQTAKEA
     THDKEIRQML EAVERTQQRK LEELLLGAAR EGRTAEVSAL LSRPNPPDVN CSDQLGNTPL
     HCAAYRAHKQ CVLKLLRSGA DPSLKNKNDQ KPLDLAHGTE MKHILVGNKV VHKALKRFEG
     PLWKSSRFFG WKLFWVVLEH GVLSWYRKQP DAVHNSYRQG CKHLTQAVCT VKPTDGCLFS
     VRCFDDTVHG FRVPKNSLQQ SREKWLEAIE EHSAYSTHYC SQDQVTDDEE EDVASAMDLK
     ESLARAQTCQ QRLDREIYNF LKMIKECDVA KDMLPSFLQK ADVLSEASRE TCVALSDCLN
     LFTKQEGVRN FKLEQEQEKN KILSEALETL ATEHHELERS LVEGSPPVSI LSEDEFYDAL
     SGSESEGSLT CLEAVTARAF EENEVPANSG KHRMSEGKDC GGGDALSNGI KKHRTSLPSP
     MFSRNDFSIW SILRKCIGME LSKITMPVIF NEPLSFLQRL TEYMEHTYLI HKASSFSDPV
     ERMQCVAAFA VSAVASQWER TGKPFNPLLG ETYELVRDDL GFRLISEQVS HHPPISAFHA
     EGLNNDFIFH GSIYPKLKFW GKSVEAEPKG TITLELLEHN EAYTWTNPTC CVHNIIVGKL
     WIEQYGNVEI INHKTGDKCV LNFKPCGLFG KELHKVEGYI QDKSKKKLCA LYGKWTECLY
     SVDPATFDAY KKNDKKNTEE KKTSKQASTS EESDEMPVPD SESVFVIPGS ALLWRIAPRP
     PNSAQMYNFT SFAMVLNEVD KEMETVIPKT DCRLRPDIRA MENGEIDQAS EEKKRLEEKQ
     RAARKNRSKS EEDWKTRWFH QGPNPYSGAQ DWIYSGSYWD RNYFNLPDIY