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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
 
 
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