OSMR_MOUSE
ID OSMR_MOUSE Reviewed; 971 AA.
AC O70458; O88821;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Oncostatin-M-specific receptor subunit beta;
DE AltName: Full=Interleukin-31 receptor subunit beta;
DE Short=IL-31 receptor subunit beta;
DE Short=IL-31R subunit beta;
DE Short=IL-31R-beta;
DE Short=IL-31RB;
DE Flags: Precursor;
GN Name=Osmr; Synonyms=Osmrb;
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 1), SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=9584176; DOI=10.1128/mcb.18.6.3357;
RA Lindberg R.A., Juan T.S.-C., Welcher A.A., Sun Y., Cupples R., Guthrie B.,
RA Fletcher F.A.;
RT "Cloning and characterization of a specific receptor for mouse oncostatin
RT M.";
RL Mol. Cell. Biol. 18:3357-3367(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=9920829;
RA Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A., Miyajima A.;
RT "Reconstitution of the functional mouse oncostatin M (OSM) receptor:
RT molecular cloning of the OSM receptor beta subunit.";
RL Blood 93:804-815(1999).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-577; ASN-689 AND ASN-722.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25381841; DOI=10.1111/exd.12587;
RA Arai I., Tsuji M., Miyagawa K., Takeda H., Akiyama N., Saito S.;
RT "Repeated administration of IL-31 upregulates IL-31 receptor A (IL-31RA) in
RT dorsal root ganglia and causes severe itch-associated scratching behaviour
RT in mice.";
RL Exp. Dermatol. 24:75-78(2015).
CC -!- FUNCTION: Associates with IL31RA to form the IL31 receptor
CC (PubMed:9920829). Binds IL31 to activate STAT3 and possibly STAT1 and
CC STAT5 (By similarity). Capable of transducing OSM-specific signaling
CC events (By similarity). {ECO:0000250|UniProtKB:Q99650,
CC ECO:0000269|PubMed:9920829}.
CC -!- SUBUNIT: Heterodimer composed of OSMR and IL6ST (type II OSM receptor).
CC Heterodimer with IL31RA to form the IL31 receptor.
CC {ECO:0000269|PubMed:9584176, ECO:0000269|PubMed:9920829}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O70458-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70458-2; Sequence=VSP_021530;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9584176). Expressed at
CC highest levels in the lung, heart, thymus and spleen (PubMed:9920829).
CC Expressed in dorsal root ganglia (PubMed:25381841).
CC {ECO:0000269|PubMed:25381841, ECO:0000269|PubMed:9584176,
CC ECO:0000269|PubMed:9920829}.
CC -!- INDUCTION: Up-regulated by IL31 in dorsal root ganglia.
CC {ECO:0000269|PubMed:25381841}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding. {ECO:0000250}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC subfamily. {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; AF058805; AAC40122.1; -; mRNA.
DR EMBL; AB015978; BAA33725.1; -; mRNA.
DR CCDS; CCDS27368.1; -. [O70458-1]
DR CCDS; CCDS79358.1; -. [O70458-2]
DR RefSeq; NP_001297398.1; NM_001310469.1.
DR RefSeq; NP_035149.2; NM_011019.3.
DR AlphaFoldDB; O70458; -.
DR SMR; O70458; -.
DR BioGRID; 201984; 2.
DR DIP; DIP-5787N; -.
DR IntAct; O70458; 38.
DR MINT; O70458; -.
DR STRING; 10090.ENSMUSP00000022746; -.
DR GlyGen; O70458; 14 sites.
DR iPTMnet; O70458; -.
DR PhosphoSitePlus; O70458; -.
DR SwissPalm; O70458; -.
DR MaxQB; O70458; -.
DR PaxDb; O70458; -.
DR PeptideAtlas; O70458; -.
DR PRIDE; O70458; -.
DR ProteomicsDB; 294122; -. [O70458-1]
DR ProteomicsDB; 294123; -. [O70458-2]
DR DNASU; 18414; -.
DR GeneID; 18414; -.
DR KEGG; mmu:18414; -.
DR UCSC; uc011zrc.1; mouse. [O70458-2]
DR CTD; 9180; -.
DR MGI; MGI:1330819; Osmr.
DR eggNOG; ENOG502QWRV; Eukaryota.
DR InParanoid; O70458; -.
DR OrthoDB; 331447at2759; -.
DR PhylomeDB; O70458; -.
DR Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR BioGRID-ORCS; 18414; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Osmr; mouse.
DR PRO; PR:O70458; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70458; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005900; C:oncostatin-M receptor complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IPI:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0004924; F:oncostatin-M receptor activity; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003529; Hematopoietin_rcpt_Gp130_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040817; LIFR_D2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF17971; LIFR_D2; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..971
FT /note="Oncostatin-M-specific receptor subunit beta"
FT /id="PRO_0000259760"
FT TOPO_DOM 24..737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 332..425
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 427..523
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 524..620
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..733
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 949..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 412..416
FT /note="WSXWS motif"
FT /evidence="ECO:0000250"
FT MOTIF 767..775
FT /note="Box 1 motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 952..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 242..252
FT /evidence="ECO:0000250"
FT VAR_SEQ 527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9920829"
FT /id="VSP_021530"
FT CONFLICT 505
FT /note="T -> A (in Ref. 2; BAA33725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 110229 MW; BECAA85BBD47C1E7 CRC64;
MAFSVVLHPA FLLAVLSLRA SRSEVLEEPL PLTPEIHKVS FQLKLQEVNL EWTVPALTHE
ELNMIFQIEI SRLNISNTIW VENYSTTVKR EEAVRWNWTS DIPLECVKHF IRIRALVDDT
KSLPQSSWGN WSSWKEVNAK VSVEPDKSLI FPKDKVLEEG SNVTICLMYG QNVYNVSCKL
QDEPIHGEQL DSHVSLLKLN NVVFLSDTGT NINCQATKGP KRIFGTVLFV SKVLEEPKNV
SCETRDFKTL DCSWEPGVDT TLTWRKQRFQ NYTLCESFSK RCEVSNYRNS YTWQITEGSQ
EMYNFTLTAE NQLRKRSVNI NFNLTHRVHP KAPQDVTLKI IGATKANMTW KVHSHGNNYT
LLCQVKLQYG EVIHEHNVSV HMSANYLFSD LDPDTKYKAF VRCASANHFW KWSDWTQKEF
STPETAPSQA LDVWRQVWSE NGRRIVTLFW KPLLKSQANG KIISYNIVVE NEAKPTESEH
YCVWAPALST NLSLDLQPYK IRITTNNSMG ASPESLMVLS NDSGHEEVKE KTIKGIKDAF
NISWEPVSGD TMGYVVDWCA HSQDQRCDLQ WKNLGPNTTS TTITSDDFKP GVRYNFRIFE
RSVEHKARLV EKQRGYTQEL APLVNPKVEI PYSTPNSFVL RWPDYDSDFQ AGFIKGYLVY
VKSKEMQCNQ PWERTLLPDN SVLCKYDING SETKTLTVEN LQPESLYEFF VTPYTSAGPG
PNETFTKVTT PDARSHMLLQ IILPMTLCVL LSIIVCYWKS QWVKEKCYPD IPNPYKSSIL
SLIKSKKNPH LIMNVKDCIP DVLEVINKAE GSKTQCVGSG KLHIEDVPTK PPIVPTEKDS
SGPVPCIFFE NFTYDQSAFD SGSHGLIPGP LKDTAHQLGL LAPPNKFQNV LKNDYMKPLV
ESPTEETSLI YVSQLASPMC GDKDTLATEP PVPVHGSEYK RQMVVPGSLA SPSLKEDNSL
TSTVLLGQGE Q
