OSBL1_MOUSE
ID OSBL1_MOUSE Reviewed; 950 AA.
AC Q91XL9; O88318; Q3TH97; Q673L8; Q6DFU6;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Oxysterol-binding protein-related protein 1;
DE Short=ORP-1;
DE Short=OSBP-related protein 1;
GN Name=Osbpl1a; Synonyms=Orp1, Orp1a, Orp1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12215260; DOI=10.1089/104454902320308942;
RA Anniss A.M., Apostolopoulos J., Dworkin S., Purton L.E., Sparrow R.L.;
RT "An oxysterol-binding protein family identified in the mouse.";
RL DNA Cell Biol. 21:571-580(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15871461; DOI=10.1093/dnares/11.6.381;
RA Okamura K., Yamada Y., Sakaki Y., Ito T.;
RT "An evolutionary scenario for genomic imprinting of Impact lying between
RT nonimprinted neighbors.";
RL DNA Res. 11:381-390(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Snider J., Sano H., Ohta M.;
RT "Mouse putative oxysterol-binding protein mRNA, complete cds.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 15-23, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH OAS1B.
RX PubMed=22623793; DOI=10.1128/jvi.00333-12;
RA Courtney S.C., Di H., Stockman B.M., Liu H., Scherbik S.V., Brinton M.A.;
RT "Identification of novel host cell binding partners of Oas1b, the protein
RT conferring resistance to flavivirus-induced disease in mice.";
RL J. Virol. 86:7953-7963(2012).
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 (By similarity). Interacts with the GTP-
CC bound form of RAB7A (By similarity). Interacts with OAS1B
CC (PubMed:22623793). Interacts (via FFAT motif) with MOSPD2 (via MSP
CC domain) (By similarity). {ECO:0000250|UniProtKB:Q8K4M9,
CC ECO:0000250|UniProtKB:Q9BXW6, ECO:0000269|PubMed:22623793}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Osbpl1b;
CC IsoId=Q91XL9-1; Sequence=Displayed;
CC Name=2; Synonyms=Osbpl1a;
CC IsoId=Q91XL9-2; Sequence=VSP_017724;
CC Name=3;
CC IsoId=Q91XL9-3; Sequence=VSP_017723;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12215260}.
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; AF394063; AAK71661.2; -; mRNA.
DR EMBL; AY536214; AAT06024.1; -; mRNA.
DR EMBL; AB017026; BAA33012.1; -; mRNA.
DR EMBL; AK168366; BAE40301.1; -; mRNA.
DR EMBL; BC076637; AAH76637.1; -; mRNA.
DR CCDS; CCDS29067.1; -. [Q91XL9-1]
DR CCDS; CCDS57114.1; -. [Q91XL9-2]
DR RefSeq; NP_001239418.1; NM_001252489.1.
DR RefSeq; NP_001239419.1; NM_001252490.1. [Q91XL9-2]
DR RefSeq; NP_001239420.1; NM_001252491.1. [Q91XL9-2]
DR RefSeq; NP_001239421.1; NM_001252492.1. [Q91XL9-2]
DR RefSeq; NP_001239422.1; NM_001252493.1. [Q91XL9-2]
DR RefSeq; NP_997413.2; NM_207530.3. [Q91XL9-1]
DR RefSeq; XP_006526204.1; XM_006526141.3. [Q91XL9-1]
DR RefSeq; XP_006526205.1; XM_006526142.3. [Q91XL9-1]
DR RefSeq; XP_006526210.1; XM_006526147.2. [Q91XL9-2]
DR RefSeq; XP_006526211.1; XM_006526148.2. [Q91XL9-2]
DR RefSeq; XP_017173451.1; XM_017317962.1. [Q91XL9-2]
DR RefSeq; XP_017173452.1; XM_017317963.1. [Q91XL9-2]
DR RefSeq; XP_017173453.1; XM_017317964.1. [Q91XL9-2]
DR RefSeq; XP_017173454.1; XM_017317965.1. [Q91XL9-2]
DR PDB; 5Z2M; X-ray; 2.14 A; B/D=1-136.
DR PDB; 5Z2N; X-ray; 2.14 A; A/B=1-136.
DR PDBsum; 5Z2M; -.
DR PDBsum; 5Z2N; -.
DR AlphaFoldDB; Q91XL9; -.
DR SMR; Q91XL9; -.
DR BioGRID; 211053; 2.
DR STRING; 10090.ENSMUSP00000073957; -.
DR iPTMnet; Q91XL9; -.
DR PhosphoSitePlus; Q91XL9; -.
DR EPD; Q91XL9; -.
DR jPOST; Q91XL9; -.
DR MaxQB; Q91XL9; -.
DR PaxDb; Q91XL9; -.
DR PeptideAtlas; Q91XL9; -.
DR PRIDE; Q91XL9; -.
DR ProteomicsDB; 294223; -. [Q91XL9-1]
DR ProteomicsDB; 294224; -. [Q91XL9-2]
DR ProteomicsDB; 294225; -. [Q91XL9-3]
DR Antibodypedia; 22086; 193 antibodies from 29 providers.
DR DNASU; 64291; -.
DR Ensembl; ENSMUST00000074352; ENSMUSP00000073957; ENSMUSG00000044252. [Q91XL9-1]
DR Ensembl; ENSMUST00000117361; ENSMUSP00000112681; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000118313; ENSMUSP00000113735; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000119043; ENSMUSP00000113357; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000121774; ENSMUSP00000113268; ENSMUSG00000044252. [Q91XL9-3]
DR Ensembl; ENSMUST00000121808; ENSMUSP00000113841; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000121888; ENSMUSP00000112895; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000234194; ENSMUSP00000157017; ENSMUSG00000044252. [Q91XL9-2]
DR Ensembl; ENSMUST00000234871; ENSMUSP00000157342; ENSMUSG00000044252. [Q91XL9-2]
DR GeneID; 64291; -.
DR KEGG; mmu:64291; -.
DR UCSC; uc008ecp.2; mouse. [Q91XL9-2]
DR UCSC; uc008ecu.2; mouse. [Q91XL9-1]
DR UCSC; uc012azm.2; mouse. [Q91XL9-3]
DR CTD; 114876; -.
DR MGI; MGI:1927551; Osbpl1a.
DR VEuPathDB; HostDB:ENSMUSG00000044252; -.
DR eggNOG; KOG2209; Eukaryota.
DR GeneTree; ENSGT00940000155295; -.
DR HOGENOM; CLU_007105_5_1_1; -.
DR InParanoid; Q91XL9; -.
DR OMA; AQTCQQK; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q91XL9; -.
DR TreeFam; TF320922; -.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 64291; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Osbpl1a; mouse.
DR PRO; PR:Q91XL9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91XL9; protein.
DR Bgee; ENSMUSG00000044252; Expressed in retrosplenial region and 252 other tissues.
DR ExpressionAtlas; Q91XL9; baseline and differential.
DR Genevisible; Q91XL9; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
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:MGI.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
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; Alternative splicing; ANK repeat; Coiled coil;
KW Direct protein sequencing; Endosome; Lipid transport; Lipid-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..950
FT /note="Oxysterol-binding protein-related protein 1"
FT /id="PRO_0000100368"
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 502..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..463
FT /evidence="ECO:0000255"
FT COILED 879..913
FT /evidence="ECO:0000255"
FT MOTIF 469..483
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW6"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXW6"
FT VAR_SEQ 1..540
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_017723"
FT VAR_SEQ 1..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12215260,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_017724"
FT CONFLICT 572
FT /note="E -> D (in Ref. 5; AAH76637)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="P -> L (in Ref. 3; BAA33012)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="E -> K (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT CONFLICT 697..698
FT /note="LD -> FV (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="H -> Q (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="N -> T (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="K -> N (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="Y -> S (in Ref. 1; AAK71661)"
FT /evidence="ECO:0000305"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:5Z2N"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5Z2N"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:5Z2N"
SQ SEQUENCE 950 AA; 107795 MW; AA4F5678999B0EB5 CRC64;
MNTEAEQQLL HHARNGNAEE VRKLLAAMAR MEVVADIDCK GRSKSNLGWT PLHLACYFGH
KQVVEDLLKA GAKVNMLNDM GDTPLHRAAF TGRKELVLLL LEYDADSTVV NGSGQTAKEA
THDKEIRNML EAVERTQQRK LEELLLGAAR EGRTAEVSAL LSRPNPPDVN CSDQLGNTPL
HCAAYRAHKQ CVLKLLRSGA DPSLKNKNDQ KPLDLAQGAE MKHILVGNKV VHKALKRYEG
PLWKSSRFFG WKLFWVVLEH GVLSWYRKQP DAVHNSYRQG CKHLTQAVCT VKPTDSCLFS
IRCFDDTVHC FRVPKNSVQQ SREKWLEAIE EHSAYSTHYC SQDQVTDDEE EDVVSAMDLK
ESLARAQTCQ QRLDREIYNF LKMIKECDVA KDMLPSFLQK ADIVSEASRE TCVALNDCLN
LFTKQEGVRN FKLEQEQEKN KILSEALETL ATEHHELERS LVEGSPPVSI LSEEEFYDAL
SGSESEGSLT CLEAVTAHSF EENEVPGSSG KHRMSEGKDC GGGDALSNGI KKHRTSLPSP
MFSRNDFSIW SILRKCIGME LSKITMPVIF NEPLSFLQRL TEYMEHTYLI HKASSLSDPV
ERMQCVAAFA VSAVASQWER TGKPFNPLLG ETYELVRDDL GFRLISEQVS HHPPISAFHA
EGLNNDFIFH GSIYPKLKFW GKSVEAEPKG TITLELLDHN EAYTWTNPTC CVHNIIVGKL
WIEQYGNVEI INHKTGDKCV LNFKPCGLFG KELHKVEGYI QDKSKKKLCA LYGKWTECLY
SVDPATFDAY KKNDKKNTEE KKNSKQTSSS EESDEMPVPD SESVFIIPGS VLLWRIAPRP
PNSAQMYNFT SFAMVLNEVD KEMESVIPKT DCRLRPDIRA MENGEIDLAS EEKKRLEEKQ
RAARKNRSKS EEDWKTRWFH QGPNPYSGAQ DWIYSGSYWD RNYFNLPDIY
