OSBP2_MOUSE
ID OSBP2_MOUSE Reviewed; 908 AA.
AC Q5QNQ6; Q8CF21;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Oxysterol-binding protein 2;
GN Name=Osbp2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-908.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: Binds 7-ketocholesterol. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; AL691413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK007088; BAC25163.1; -; mRNA.
DR CCDS; CCDS24367.1; -.
DR RefSeq; NP_690031.2; NM_152818.2.
DR AlphaFoldDB; Q5QNQ6; -.
DR SMR; Q5QNQ6; -.
DR STRING; 10090.ENSMUSP00000068652; -.
DR iPTMnet; Q5QNQ6; -.
DR PhosphoSitePlus; Q5QNQ6; -.
DR MaxQB; Q5QNQ6; -.
DR PaxDb; Q5QNQ6; -.
DR PeptideAtlas; Q5QNQ6; -.
DR PRIDE; Q5QNQ6; -.
DR ProteomicsDB; 294120; -.
DR Antibodypedia; 5683; 113 antibodies from 22 providers.
DR DNASU; 74309; -.
DR Ensembl; ENSMUST00000070552; ENSMUSP00000068652; ENSMUSG00000020435.
DR GeneID; 74309; -.
DR KEGG; mmu:74309; -.
DR UCSC; uc007hto.2; mouse.
DR CTD; 23762; -.
DR MGI; MGI:1921559; Osbp2.
DR VEuPathDB; HostDB:ENSMUSG00000020435; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000157987; -.
DR HOGENOM; CLU_007105_5_1_1; -.
DR InParanoid; Q5QNQ6; -.
DR OMA; AQGHKWS; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; Q5QNQ6; -.
DR TreeFam; TF320922; -.
DR BioGRID-ORCS; 74309; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Osbp2; mouse.
DR PRO; PR:Q5QNQ6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5QNQ6; protein.
DR Bgee; ENSMUSG00000020435; Expressed in spermatid and 142 other tissues.
DR ExpressionAtlas; Q5QNQ6; baseline and differential.
DR Genevisible; Q5QNQ6; MM.
DR GO; GO:0097440; C:apical dendrite; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 GO; GO:0007286; P:spermatid development; IMP:MGI.
DR Gene3D; 2.30.29.30; -; 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; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..908
FT /note="Oxysterol-binding protein 2"
FT /id="PRO_0000223481"
FT DOMAIN 179..271
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 42..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 908 AA; 101353 MW; 7CF33E2F411906D5 CRC64;
MGKAAALSRG GGCAGRSRGL SSLFTVVPCL SCHTAAPGMN SSAFGSGPAS KPQLQPVQAP
ERELLSKQVC QPISEPASRS EPGSQTTSVP RPSGVGQESE LQGLWPGSEN GTRSVSIIKA
SPELAMPSPL QSTVGSLPVT KPESKLVPKT QSFLRQGQAK ISVGTPVSGI GVQMVSPPLD
SYKGWLLKWT NYLKGYQRRW FVLGNGLLSY YRNQGEMAHT CRATINLAST HFETEDSCGI
LLCNGARTYH LKASSEVDRQ HWITALELAK AKAIRVMKTQ SDDSGDDDEE PAAPADNSEL
HHTLKTLSLK LNDLSTCNDL IAKHGAALQR SLNELDSLKI PSECGEKLKV VNERATLFRI
TSNAMINACR DFLELAETHS RKWQRALNYE QEQRVHLEET IEQLAKQHNS LERAFCNTPG
GPASSSKSFS EGSFLTSKGE NSEEDEDTEY FDAMEDSTSF ITVVTEAKED RKPESGPGTT
TVDWTSADNV LDGASFMPKN SCKVKRRVRI PDKPNYSLNL WSIMKNCIGR ELSRIPMPVN
FNEPLSMLQR LTEDLEYHHL LDKAVNCTSS VEQMCLVAAF SVSSYSTTVH RIAKPFNPML
GETFELDRME DMGLRSLCEQ VSHHPPSAAH HVFSKHGWSL WQEITIASKF RGKYISIMPL
GAIHLEFQAS GNHYVWRKST STVHNIIVGK LWIDQSGDIE IVNHKTKDRC QLKFVPYSYF
SKEAARKVTG VVSDSQGKAH YVLSGSWDDQ MECSKIVHSS PSSDGRQKTV YQTLPAKLLW
RKYPLPENAE NMYYFSELAL TLNEQEDGVA PTDSRLRPDQ RLMERGRWDE ANTEKQRLEE
KQRLSRRRRL ESCTAGCGGE EEKESDGYVP LWFEKRLDPL TGEMACMYKG GYWEAKEKKD
WHMCPNIF