OSMR_RAT
ID OSMR_RAT Reviewed; 962 AA.
AC Q65Z14;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15743783; DOI=10.1016/s0002-9440(10)62292-4;
RA Okaya A., Kitanaka J., Kitanaka N., Satake M., Kim Y., Terada K.,
RA Sugiyama T., Takemura M., Fujimoto J., Terada N., Miyajima A.,
RA Tsujimura T.;
RT "Oncostatin M inhibits proliferation of rat oval cells, OC15-5, inducing
RT differentiation into hepatocytes.";
RL Am. J. Pathol. 166:709-719(2005).
CC -!- FUNCTION: Associates with IL31RA to form the IL31 receptor. Binds IL31
CC and activates STAT1, STAT3 and STAT5. Capable of transducing OSM-
CC specific signaling events (By similarity). The OSM/OSM-R system is
CC pivotal in the differentiation of oval cells into hepatocytes, thereby
CC promoting liver regeneration. {ECO:0000250,
CC ECO:0000269|PubMed:15743783}.
CC -!- SUBUNIT: Heterodimer composed of OSMR and IL6ST (type II OSM receptor).
CC Heterodimer with IL31RA to form the IL31 receptor (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC liver, skin and spleen. In the liver it is expressed exclusively in the
CC oval cells. {ECO:0000269|PubMed:15743783}.
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}.
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DR EMBL; AB167522; BAD44758.1; -; mRNA.
DR RefSeq; NP_001005384.1; NM_001005384.1.
DR AlphaFoldDB; Q65Z14; -.
DR SMR; Q65Z14; -.
DR STRING; 10116.ENSRNOP00000039644; -.
DR GlyGen; Q65Z14; 5 sites.
DR PaxDb; Q65Z14; -.
DR GeneID; 310132; -.
DR KEGG; rno:310132; -.
DR UCSC; RGD:1302983; rat.
DR CTD; 9180; -.
DR RGD; 1302983; Osmr.
DR eggNOG; ENOG502QWRV; Eukaryota.
DR InParanoid; Q65Z14; -.
DR OrthoDB; 331447at2759; -.
DR PhylomeDB; Q65Z14; -.
DR Reactome; R-RNO-6788467; IL-6-type cytokine receptor ligand interactions.
DR PRO; PR:Q65Z14; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005900; C:oncostatin-M receptor complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; ISO:RGD.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0004924; F:oncostatin-M receptor activity; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR CDD; cd00063; FN3; 4.
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; 2.
DR Pfam; PF17971; LIFR_D2; 1.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..962
FT /note="Oncostatin-M-specific receptor subunit beta"
FT /id="PRO_0000259761"
FT TOPO_DOM 29..738
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 237..332
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 333..426
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 428..527
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 528..621
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 623..734
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 818..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 413..417
FT /note="WSXWS motif"
FT /evidence="ECO:0000250"
FT MOTIF 768..776
FT /note="Box 1 motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 243..253
FT /evidence="ECO:0000250"
SQ SEQUENCE 962 AA; 108625 MW; A7A15FED59A6E21A CRC64;
MAFSVVLHQV TFLLAVLSLR TSQSKVLGEP LQLTPEIHTV SLQSALQEAN LEWTVPTFSH
QELNIVFQIE ISRMRTSNTI WVGNYSTTVK HEETVHWKWT SDIPLECATH FIRIRAMVDD
AQYPPQSSWS NWSSWKEVNA QVSVPPDTLL IFPEDRLLEE GSNVTICLMI GQNLYNVSCK
LQEEPIRGEQ LDSHLSLIKL NNVVFLNNAG TNINCKAMNG TKNTFGTVLF VSKVLEEPKN
FSCETRDFKT LNCLWEPGID TTLSWHKQRS QHYTLYESFS GRREVSNHRN SHTWQITEDS
QETYNFTLTA ENNLRKRSVS ISFNLTHRVH PKAPHDVTLK TVGATKAHMT WKVPSRGDYT
LLCQVELQCE GEVIHEHNVS VHTSANYLFS DLEPDTEYKA CVRCASANHF WKWSDWMQKK
FRTPEAAPSE ALDVWRDVRT ENGRHVVTLF WKPLLKSQAN GKIISYNIVV ENEANPTESE
QYSVRAPALG TNLSLDLHPY KIHISANNSA GASPESLVVL SSHSGHEEVH EKTIKGIKNG
FNISWEPVSG DAIGYVVDWC AHSQTQRCDL QWKNVGPNIT STIITSDAFE PGVRYNFRIF
ERSVEENVRL VEKQRGYTQE LAPSVNPGVT IHNLTPNSFS LKWQDYASDF QSGFIKGYLV
YLKSKELQCN PNWERTVLSD KSVLCKYDVD DPETKTLTVE NLRPESLYEF LVTPYTSAGQ
GPNETYTKVT TPDVRSHMLL QIILPMTLGV FLSIIVCYWK SQWVKEKCYP DIPNPYKSSI
LSLIKSKKNP HLIMNVKDCI PDVLEVINKA EGSKTQCVGS GKLHTEDVPT KPPLVPTEKD
SSGPMPFVFL ENFTYDQSAF DSGSHGFIPG PLKNTPHQLG LLAPPNKLQN VLENDYMKSL
VESPTEETSL IYVSQLASPI CGDKDSLVTN PPMPVHGSEY KKQMALPGSL TSASLKENNL
TS
