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Database: UniProt
Entry: ONCM_BOVIN
LinkDB: ONCM_BOVIN
Original site: ONCM_BOVIN 
ID   ONCM_BOVIN              Reviewed;         245 AA.
AC   P53346;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Oncostatin-M;
DE            Short=OSM;
DE   Flags: Precursor;
GN   Name=OSM;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7739518; DOI=10.1128/mcb.15.5.2349;
RA   Malik N., Haugen H.S., Modrell B., Shoyab M., Clegg C.H.;
RT   "Developmental abnormalities in mice transgenic for bovine oncostatin M.";
RL   Mol. Cell. Biol. 15:2349-2358(1995).
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. Uses both type I OSM receptor
CC       (heterodimers composed of LIFR and IL6ST) and type II OSM receptor
CC       (heterodimers composed of OSMR and IL6ST) (By similarity). Involved in
CC       the maturation of fetal hepatocytes, thereby promoting liver
CC       development and regeneration (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; S78435; AAB34208.1; -; Genomic_DNA.
DR   EMBL; S78434; AAB34208.1; JOINED; Genomic_DNA.
DR   EMBL; S78487; AAB34208.1; JOINED; Genomic_DNA.
DR   PIR; A57417; A57417.
DR   AlphaFoldDB; P53346; -.
DR   SMR; P53346; -.
DR   STRING; 9913.ENSBTAP00000021515; -.
DR   GlyCosmos; P53346; 1 site, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000021515; -.
DR   eggNOG; ENOG502RVJA; Eukaryota.
DR   InParanoid; P53346; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0005147; F:oncostatin-M receptor binding; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0010646; P:regulation of cell communication; IEA:UniProt.
DR   GO; GO:0023051; P:regulation of signaling; IEA:UniProt.
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; ONCOSTATIN M; 1.
DR   PANTHER; PTHR14261:SF0; ONCOSTATIN-M; 1.
DR   Pfam; PF01291; LIF_OSM; 1.
DR   SMART; SM00080; LIF_OSM; 1.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   PROSITE; PS00590; LIF_OSM; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth regulation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..206
FT                   /note="Oncostatin-M"
FT                   /evidence="ECO:0000250|UniProtKB:P13725"
FT                   /id="PRO_0000017719"
FT   PROPEP          207..245
FT                   /evidence="ECO:0000250|UniProtKB:P13725"
FT                   /id="PRO_0000408763"
FT   REGION          143..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..177
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  27554 MW;  3372D6E660776C0E CRC64;
     MGAQRMQRTL LSLVLRLLLL CTVATGKCSG KYHELLLQLQ RQADLMQDPS TLLDPYIHLQ
     GLHSPVLQEH CRERPGDFPS EDALWRLSRQ DFLQTLNTTL GLILRMLSAL QQDLPEAAHQ
     QAEMNVRGFG NNIHCMAQLL RGSSDPKAAE PTQPGPGPTP LPPTPPSSTF QRKLRNCGFL
     RGYHRFMRTA GQVLRGWGER QGRSRRHSPC RALKRGARRT QPFPEIRRLA PRGQPPGSLW
     GAPAR
//
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