ONCM_RAT
ID ONCM_RAT Reviewed; 239 AA.
AC Q65Z15;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Oncostatin-M;
DE Short=OSM;
DE Flags: Precursor;
GN Name=Osm;
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: Growth regulator. Inhibits the proliferation of a number of
CC tumor cell lines. It regulates cytokine production, including IL-6, G-
CC CSF and GM-CSF from endothelial cells (By similarity). Uses only type
CC II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in
CC the maturation of fetal hepatocytes, thereby promoting liver
CC development and regeneration. {ECO:0000250,
CC ECO:0000269|PubMed:15743783}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher levels in
CC liver, skin and spleen. {ECO:0000269|PubMed:15743783}.
CC -!- PTM: Propeptide processing is not important for receptor binding
CC activity but may be important growth-inhibitory activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LIF/OSM family. {ECO:0000305}.
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DR EMBL; AB167521; BAD44757.1; -; mRNA.
DR RefSeq; NP_001006962.1; NM_001006961.1.
DR AlphaFoldDB; Q65Z15; -.
DR SMR; Q65Z15; -.
DR STRING; 10116.ENSRNOP00000032548; -.
DR PaxDb; Q65Z15; -.
DR PRIDE; Q65Z15; -.
DR Ensembl; ENSRNOT00000035591; ENSRNOP00000032548; ENSRNOG00000024390.
DR GeneID; 289747; -.
DR KEGG; rno:289747; -.
DR UCSC; RGD:1585012; rat.
DR CTD; 5008; -.
DR RGD; 1585012; Osm.
DR eggNOG; ENOG502RVJA; Eukaryota.
DR GeneTree; ENSGT00390000004850; -.
DR HOGENOM; CLU_102028_0_0_1; -.
DR InParanoid; Q65Z15; -.
DR OMA; FMHSVGQ; -.
DR OrthoDB; 1469672at2759; -.
DR PhylomeDB; Q65Z15; -.
DR TreeFam; TF338204; -.
DR Reactome; R-RNO-6788467; IL-6-type cytokine receptor ligand interactions.
DR PRO; PR:Q65Z15; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000024390; Expressed in thymus and 5 other tissues.
DR Genevisible; Q65Z15; RN.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR GO; GO:0005147; F:oncostatin-M receptor binding; ISO:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0046888; P:negative regulation of hormone secretion; ISO:RGD.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; ISO:RGD.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISO:RGD.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR001581; Leukemia_IF/oncostatin.
DR InterPro; IPR019827; Leukemia_IF/oncostatin_CS.
DR InterPro; IPR039578; OSM.
DR PANTHER; PTHR14261; PTHR14261; 1.
DR Pfam; PF01291; LIF_OSM; 1.
DR SMART; SM00080; LIF_OSM; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00590; LIF_OSM; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Cytokine; Disulfide bond;
KW Growth regulation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..208
FT /note="Oncostatin-M"
FT /evidence="ECO:0000250|UniProtKB:P13725"
FT /id="PRO_0000408765"
FT PROPEP 209..239
FT /evidence="ECO:0000250|UniProtKB:P13725"
FT /id="PRO_0000408766"
FT DISULFID 29..140
FT /evidence="ECO:0000250"
FT DISULFID 72..179
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 27106 MW; 78BC63B25A148B16 CRC64;
MRAQPPPRTL LSLALALLFL SMSWAKRGCS SSSPKLLSQL KSQANITGNT ASLLEPYILH
QNLNTLTLRA ACTEHPVAFP SEDMLRQLSK PDFLSTVHAT LGRVWHQLGA FRQQFPKIQD
FPELERARQN IQGIRNNVYC MARLLHPPLE IPEPTQADSG TSRPTTTAPG IFQIKIDSCR
FLWGYHRFMG SVGRVFEEWG DGSRRSRRHS PLWAWLKGDH RIRPSRSSQS AMLRSLVPR
