OSB11_MOUSE
ID OSB11_MOUSE Reviewed; 751 AA.
AC Q8CI95;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Oxysterol-binding protein-related protein 11;
DE Short=ORP-11;
DE Short=OSBP-related protein 11;
GN Name=Osbpl11;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-186 AND SER-194, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179; SER-182;
RP SER-186 AND SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Plays a role in regulating ADIPOQ and FABP4 levels in
CC differentiating adipocytes and is also involved in regulation of
CC adipocyte triglyceride storage. Weakly binds 25-hydroxycholesterol.
CC {ECO:0000250|UniProtKB:Q9BXB4}.
CC -!- SUBUNIT: Heterodimer with OSBPL9. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}. Note=Localizes
CC at the Golgi-late endosome interface. {ECO:0000250}.
CC -!- DOMAIN: The PH domain binds phosphoinositides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35278.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC035278; AAH35278.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8CI95; -.
DR BMRB; Q8CI95; -.
DR SMR; Q8CI95; -.
DR IntAct; Q8CI95; 1.
DR MINT; Q8CI95; -.
DR STRING; 10090.ENSMUSP00000039632; -.
DR iPTMnet; Q8CI95; -.
DR PhosphoSitePlus; Q8CI95; -.
DR EPD; Q8CI95; -.
DR jPOST; Q8CI95; -.
DR MaxQB; Q8CI95; -.
DR PaxDb; Q8CI95; -.
DR PeptideAtlas; Q8CI95; -.
DR PRIDE; Q8CI95; -.
DR ProteomicsDB; 294349; -.
DR MGI; MGI:2146553; Osbpl11.
DR eggNOG; KOG2210; Eukaryota.
DR InParanoid; Q8CI95; -.
DR PhylomeDB; Q8CI95; -.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR ChiTaRS; Osbpl11; mouse.
DR PRO; PR:Q8CI95; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CI95; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; 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:0045444; P:fat cell differentiation; ISO:MGI.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; ISO: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 Acetylation; Endosome; Golgi apparatus; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..751
FT /note="Oxysterol-binding protein-related protein 11"
FT /id="PRO_0000100382"
FT DOMAIN 63..160
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB4"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB4"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXB4"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 751 AA; 83629 MW; 70E5817835DC5B87 CRC64;
MQGGEPASVM KVSESEGKLE GLATAVTPNK NSGNSSCGGA ISSSSSNSSR GGSAKGWQYS
DHMESVNGYL MKYTNLVTGW QYRFFVLNNE AGLLEYFVNE QSRNQKPRGT LQLAGAVISP
SDEDSHTFTV NAASGEQYKL RATDAKERQH WVSRLQICTQ HHTEAIGKNN PPLKSRSFSL
ASSGNSPISQ RRPSQNAMSF FNVGHSKLQS VNKRAHLHPD HLVEVREMMS HAEGQQRDLI
RRIECLPASG LLSSLDQDLL MLKATSMATM NCLNDCFHIL QLQHASHQKG ALPSGTTIEW
LEPKIPLSNH YKNGAEQPFA TEPNKPMGAP EAQCVAESGV LAREPEDISA DDEVEDTCDN
KEDDLGAVEE QRSVILHLLS QLKLGMDLTR VVLPTFILEK RSLLEMYADF MSHPDLFIGI
TNGATPEDRM IRFVEYYLTS FHEGRKGAIA KKPYNPIIGE TFHCSWRMPK SEVASGVSSS
SSTPAITDHA PLPEEAPTQS VSDCYTVRFV AEQVSHHPPV SGFYAECAER KMCVNAHVWT
KSKFLGMSIG VTMVGEGVLC LLEHGEEYTF SLPCAYARSI LTVPWVELGG KVSVNCAKTG
YSASITFHTK PFYGGKLHRV TAEVKYNLTN TVVCRVQGEW NSVLEFTYSN GETKFVDLAK
LAVTKKRVRP LEKQDPFESR RLWKNVTDSL RESEIDKATE HKRSLEERQR TEERLRTETG
TPWKTKYFIK EGDGWVYHKP LWKGIPSQPA E
