OSTF1_MOUSE
ID OSTF1_MOUSE Reviewed; 215 AA.
AC Q62422; Q3UF05;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Osteoclast-stimulating factor 1;
DE AltName: Full=SH3 domain protein 3;
GN Name=Ostf1; Synonyms=Sh3d3, Sh3p2;
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=9238627; DOI=10.1007/bf01718694;
RA Hoffman N.G., Sparks A.B., Carter J.M., Kay B.K.;
RT "Binding properties of SH3 peptide ligands identified from phage-displayed
RT random peptide libraries.";
RL Mol. Divers. 2:5-12(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Kidney, Placenta, Small intestine,
RC Sympathetic ganglion, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Induces bone resorption, acting probably through a signaling
CC cascade which results in the secretion of factor(s) enhancing
CC osteoclast formation and activity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with C-SRC and SMN1. Interacts with FASLG (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The SH3 domain mediates interaction with SMN1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U58888; AAC52641.1; ALT_INIT; mRNA.
DR EMBL; AK002899; BAB22442.1; -; mRNA.
DR EMBL; AK005525; BAB24098.1; -; mRNA.
DR EMBL; AK008123; BAB25477.1; -; mRNA.
DR EMBL; AK008467; BAB25685.1; -; mRNA.
DR EMBL; AK010074; BAB26683.1; -; mRNA.
DR EMBL; AK145949; BAE26777.1; -; mRNA.
DR EMBL; AK149175; BAE28756.1; -; mRNA.
DR EMBL; AK150145; BAE29340.1; -; mRNA.
DR EMBL; AK155028; BAE33000.1; -; mRNA.
DR EMBL; BC060986; AAH60986.1; -; mRNA.
DR CCDS; CCDS37930.1; -.
DR RefSeq; NP_059071.1; NM_017375.3.
DR AlphaFoldDB; Q62422; -.
DR SMR; Q62422; -.
DR BioGRID; 203211; 2.
DR IntAct; Q62422; 1.
DR MINT; Q62422; -.
DR STRING; 10090.ENSMUSP00000025631; -.
DR iPTMnet; Q62422; -.
DR PhosphoSitePlus; Q62422; -.
DR SwissPalm; Q62422; -.
DR UCD-2DPAGE; Q62422; -.
DR EPD; Q62422; -.
DR jPOST; Q62422; -.
DR MaxQB; Q62422; -.
DR PaxDb; Q62422; -.
DR PeptideAtlas; Q62422; -.
DR PRIDE; Q62422; -.
DR ProteomicsDB; 294397; -.
DR Antibodypedia; 27176; 223 antibodies from 27 providers.
DR DNASU; 20409; -.
DR Ensembl; ENSMUST00000025631; ENSMUSP00000025631; ENSMUSG00000024725.
DR GeneID; 20409; -.
DR KEGG; mmu:20409; -.
DR UCSC; uc008gxs.2; mouse.
DR CTD; 26578; -.
DR MGI; MGI:700012; Ostf1.
DR VEuPathDB; HostDB:ENSMUSG00000024725; -.
DR eggNOG; ENOG502QTZB; Eukaryota.
DR GeneTree; ENSGT00920000149159; -.
DR HOGENOM; CLU_092255_0_0_1; -.
DR InParanoid; Q62422; -.
DR OMA; NMSWLRE; -.
DR OrthoDB; 1453481at2759; -.
DR PhylomeDB; Q62422; -.
DR TreeFam; TF314534; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 20409; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ostf1; mouse.
DR PRO; PR:Q62422; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q62422; protein.
DR Bgee; ENSMUSG00000024725; Expressed in granulocyte and 246 other tissues.
DR ExpressionAtlas; Q62422; baseline and differential.
DR Genevisible; Q62422; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92882"
FT CHAIN 2..215
FT /note="Osteoclast-stimulating factor 1"
FT /id="PRO_0000067036"
FT DOMAIN 12..71
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 72..101
FT /note="ANK 1"
FT REPEAT 105..135
FT /note="ANK 2"
FT REPEAT 139..168
FT /note="ANK 3"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q92882"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92882"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 215 AA; 23783 MW; DAB682C371929B8A CRC64;
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTSWW KGTCKGRTGL
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
IVEVLFTQPN VELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN NEKKLALDMA
TNAACASLLK KKQQGTDGAR TLSNAEDYLD DEDSD
