OS9_MOUSE
ID OS9_MOUSE Reviewed; 672 AA.
AC Q8K2C7;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein OS-9;
DE Flags: Precursor;
GN Name=Os9;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP INTERACTION WITH CPNE6.
RX PubMed=10403379; DOI=10.1016/s0014-5793(99)00700-0;
RA Nakayama T., Yaoi T., Kuwajima G., Yoshie O., Sakata T.;
RT "Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain
RT protein family, with OS-9, the product of a gene frequently amplified in
RT osteosarcoma.";
RL FEBS Lett. 453:77-80(1999).
RN [4]
RP GLYCOSYLATION.
RX PubMed=19084021; DOI=10.1016/j.jmb.2008.11.045;
RA Alcock F., Swanton E.;
RT "Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress
RT and facilitates ubiquitination of misfolded glycoproteins.";
RL J. Mol. Biol. 385:1032-1042(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, 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: Lectin which functions in endoplasmic reticulum (ER) quality
CC control and ER-associated degradation (ERAD). May bind terminally
CC misfolded non-glycosylated proteins as well as improperly folded
CC glycoproteins, retain them in the ER, and possibly transfer them to the
CC ubiquitination machinery and promote their degradation. Possible
CC targets include TRPV4 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CPNE6 (via second C2 domain);
CC this interaction occurs in a calcium-dependent manner in vitro
CC (PubMed:10403379). Component of the HRD1 complex, which comprises at
CC least SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1.
CC FAM8A1 is stabilized by interaction with SYNV1, which prevents its
CC proteasomal degradation. OS9 and UBE2J1 recruitment to the complex may
CC be mediated by SEL1L (By similarity). Through this complex, may
CC interact with ERLEC1 and HSPA5 (By similarity). Interacts with HSP90B1
CC (By similarity). Interacts with CREB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q13438, ECO:0000269|PubMed:10403379}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2C7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2C7-2; Sequence=VSP_038220;
CC -!- PTM: Intramolecular disulfide bonds. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19084021}.
CC -!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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DR EMBL; AC131760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031768; AAH31768.1; -; mRNA.
DR CCDS; CCDS24229.1; -. [Q8K2C7-2]
DR CCDS; CCDS48713.1; -. [Q8K2C7-1]
DR RefSeq; NP_001164497.1; NM_001171026.1. [Q8K2C7-1]
DR RefSeq; NP_808282.2; NM_177614.3. [Q8K2C7-2]
DR AlphaFoldDB; Q8K2C7; -.
DR SMR; Q8K2C7; -.
DR BioGRID; 229745; 15.
DR STRING; 10090.ENSMUSP00000128914; -.
DR GlyConnect; 2640; 5 N-Linked glycans (1 site).
DR GlyGen; Q8K2C7; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q8K2C7; -.
DR PhosphoSitePlus; Q8K2C7; -.
DR EPD; Q8K2C7; -.
DR jPOST; Q8K2C7; -.
DR MaxQB; Q8K2C7; -.
DR PaxDb; Q8K2C7; -.
DR PeptideAtlas; Q8K2C7; -.
DR PRIDE; Q8K2C7; -.
DR ProteomicsDB; 294110; -. [Q8K2C7-1]
DR ProteomicsDB; 294111; -. [Q8K2C7-2]
DR Antibodypedia; 2459; 289 antibodies from 29 providers.
DR DNASU; 216440; -.
DR Ensembl; ENSMUST00000080975; ENSMUSP00000079770; ENSMUSG00000040462. [Q8K2C7-2]
DR Ensembl; ENSMUST00000164259; ENSMUSP00000128914; ENSMUSG00000040462. [Q8K2C7-1]
DR GeneID; 216440; -.
DR KEGG; mmu:216440; -.
DR UCSC; uc007hhz.2; mouse. [Q8K2C7-2]
DR UCSC; uc007hia.2; mouse. [Q8K2C7-1]
DR CTD; 10956; -.
DR MGI; MGI:1924301; Os9.
DR VEuPathDB; HostDB:ENSMUSG00000040462; -.
DR eggNOG; KOG3394; Eukaryota.
DR GeneTree; ENSGT00530000063603; -.
DR HOGENOM; CLU_026715_0_0_1; -.
DR InParanoid; Q8K2C7; -.
DR OMA; WLKRLYV; -.
DR OrthoDB; 1475416at2759; -.
DR PhylomeDB; Q8K2C7; -.
DR TreeFam; TF314309; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR BioGRID-ORCS; 216440; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Os9; mouse.
DR PRO; PR:Q8K2C7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K2C7; protein.
DR Bgee; ENSMUSG00000040462; Expressed in lacrimal gland and 274 other tissues.
DR ExpressionAtlas; Q8K2C7; baseline and differential.
DR Genevisible; Q8K2C7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0006621; P:protein retention in ER lumen; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR045149; OS-9-like.
DR InterPro; IPR012913; OS9-like_dom.
DR PANTHER; PTHR15414; PTHR15414; 1.
DR Pfam; PF07915; PRKCSH; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Lectin; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..672
FT /note="Protein OS-9"
FT /id="PRO_0000386449"
FT DOMAIN 108..230
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 261..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..439
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 118
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 130
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 182
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 188
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 212
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT BINDING 218
FT /ligand="a mannooligosaccharide derivative"
FT /ligand_id="ChEBI:CHEBI:71274"
FT /evidence="ECO:0000250|UniProtKB:Q13438"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 181..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 196..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 539..593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038220"
FT CONFLICT 407
FT /note="D -> G (in Ref. 2; AAH31768)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="N -> D (in Ref. 2; AAH31768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 76108 MW; 7320981E721A9686 CRC64;
MAAEVLLSSL LGLLFLGLLL PARLTGGVGS LNLEELSEMR YGIQILPLPV MGGQSQASDV
VVVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY
EFCYGRHIQQ YHMEDSEIKG DVLYLGHYQS SFNWDDETAK ASKQHRLKRY HSQTYGNGSK
CDLNGKPREA EVRFLCDEGA GISGDYIDRV DEPVSCSYVL TIRTSRLCPH PLLRPPASAA
PQAILCHPAL QPDEYMAYLQ RQAESKQHEE KTTEEVQDTD RQVWSGSKAA GAPPKKEDVS
PAKEEKESEL WKLQGPEEQA AAREEAQAGE QDLNHEAAAD PAPSPPNDFQ NNVQVKLIRS
PADLIRLIEE LKAAEKGKPS VRREQPGDDT TEAPQREAEG TKAKGKDGEP PGLMEEEDGD
DEEEEEEEEE DEEEQQLLGE FEKELEGMLL PSNRERLRSE VKAGMERELE NIIQETEKEL
DPEGLRKESE REQAILALTS TLDKLIKRLQ ENQSPELVQK YKKRRVVPQK PPPSPHPTEE
EPEHRVRVRV TKLRPGGPNR DLTVLEMNRE NPQLKQIEGL VTEVLEREGL TAEGKIEIKI
VRPGAEGKEE DTRWLTDEDT RNLKEIFFNI LVQGAEEANK ERQRQSELES NYRRVWGSPG
GEDTGDLDEF DF
