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ONCM_MOUSE
ID   ONCM_MOUSE              Reviewed;         263 AA.
AC   P53347; Q3U1Y5; Q5SPX6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Oncostatin-M;
DE            Short=OSM;
DE   Flags: Precursor;
GN   Name=Osm;
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].
RX   PubMed=8605875; DOI=10.1002/j.1460-2075.1996.tb00443.x;
RA   Yoshimura A., Ichihara M., Kinjyo I., Moriyama M., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Hara T., Miyajima A.;
RT   "Mouse oncostatin M: an immediate early gene induced by multiple cytokines
RT   through the JAK-STAT5 pathway.";
RL   EMBO J. 15:1055-1063(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   INTERACTION WITH OSMR AND IL6ST.
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).
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 (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; D31942; BAA06712.1; -; mRNA.
DR   EMBL; AK155637; BAE33358.1; -; mRNA.
DR   EMBL; AL807825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC099866; AAH99866.1; -; mRNA.
DR   CCDS; CCDS24382.1; -.
DR   PIR; S64719; S64719.
DR   RefSeq; NP_001013383.1; NM_001013365.2.
DR   AlphaFoldDB; P53347; -.
DR   SMR; P53347; -.
DR   DIP; DIP-5786N; -.
DR   STRING; 10090.ENSMUSP00000074708; -.
DR   GlyGen; P53347; 3 sites.
DR   PhosphoSitePlus; P53347; -.
DR   PaxDb; P53347; -.
DR   PRIDE; P53347; -.
DR   Antibodypedia; 10652; 612 antibodies from 35 providers.
DR   DNASU; 18413; -.
DR   Ensembl; ENSMUST00000075221; ENSMUSP00000074708; ENSMUSG00000058755.
DR   GeneID; 18413; -.
DR   KEGG; mmu:18413; -.
DR   UCSC; uc007hus.2; mouse.
DR   CTD; 5008; -.
DR   MGI; MGI:104749; Osm.
DR   VEuPathDB; HostDB:ENSMUSG00000058755; -.
DR   eggNOG; ENOG502RVJA; Eukaryota.
DR   GeneTree; ENSGT00390000004850; -.
DR   HOGENOM; CLU_102028_0_0_1; -.
DR   InParanoid; P53347; -.
DR   OMA; FMHSVGQ; -.
DR   OrthoDB; 1416192at2759; -.
DR   PhylomeDB; P53347; -.
DR   TreeFam; TF338204; -.
DR   Reactome; R-MMU-6788467; IL-6-type cytokine receptor ligand interactions.
DR   BioGRID-ORCS; 18413; 3 hits in 73 CRISPR screens.
DR   PRO; PR:P53347; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P53347; protein.
DR   Bgee; ENSMUSG00000058755; Expressed in granulocyte and 20 other tissues.
DR   Genevisible; P53347; MM.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR   GO; GO:0005147; F:oncostatin-M receptor binding; ISO:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0140013; P:meiotic nuclear division; IDA:MGI.
DR   GO; GO:0046888; P:negative regulation of hormone secretion; ISO:MGI.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:MGI.
DR   GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR   GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0009408; P:response to heat; IMP:MGI.
DR   GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:MGI.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth regulation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..206
FT                   /note="Oncostatin-M"
FT                   /evidence="ECO:0000250|UniProtKB:P13725"
FT                   /id="PRO_0000017722"
FT   PROPEP          207..263
FT                   /evidence="ECO:0000250|UniProtKB:P13725"
FT                   /id="PRO_0000408764"
FT   REGION          241..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..177
FT                   /evidence="ECO:0000250"
FT   CONFLICT        217
FT                   /note="T -> S (in Ref. 2; BAE33358)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  30114 MW;  18326DB214797BCC CRC64;
     MQTRLLRTLL SLTLSLLILS MALANRGCSN SSSQLLSQLQ NQANLTGNTE SLLEPYIRLQ
     NLNTPDLRAA CTQHSVAFPS EDTLRQLSKP HFLSTVYTTL DRVLYQLDAL RQKFLKTPAF
     PKLDSARHNI LGIRNNVFCM ARLLNHSLEI PEPTQTDSGA SRSTTTPDVF NTKIGSCGFL
     WGYHRFMGSV GRVFREWDDG STRSRRQSPL RARRKGTRRI RVRHKGTRRI RVRRKGTRRI
     WVRRKGSRKI RPSRSTQSPT TRA
 
 
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