ID   OSTF1_RAT               Reviewed;         214 AA.
AC   Q6P686; Q8K3X7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Osteoclast-stimulating factor 1;
GN   Name=Ostf1;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RA   Guo J.H.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 SRC and SMN1. Interacts with FASLG (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The SH3 domain mediates interaction with SMN1. {ECO:0000250}.
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DR   EMBL; AF523266; AAM82159.1; -; mRNA.
DR   EMBL; BC062400; AAH62400.1; -; mRNA.
DR   RefSeq; NP_683690.2; NM_148892.3.
DR   RefSeq; XP_008758509.1; XM_008760287.2.
DR   AlphaFoldDB; Q6P686; -.
DR   SMR; Q6P686; -.
DR   IntAct; Q6P686; 1.
DR   STRING; 10116.ENSRNOP00000016871; -.
DR   iPTMnet; Q6P686; -.
DR   PhosphoSitePlus; Q6P686; -.
DR   jPOST; Q6P686; -.
DR   PaxDb; Q6P686; -.
DR   PRIDE; Q6P686; -.
DR   GeneID; 259275; -.
DR   KEGG; rno:259275; -.
DR   UCSC; RGD:628849; rat.
DR   CTD; 26578; -.
DR   RGD; 628849; Ostf1.
DR   VEuPathDB; HostDB:ENSRNOG00000012156; -.
DR   eggNOG; ENOG502QTZB; Eukaryota.
DR   HOGENOM; CLU_092255_0_0_1; -.
DR   InParanoid; Q6P686; -.
DR   OMA; NMSWLRE; -.
DR   OrthoDB; 1453481at2759; -.
DR   PhylomeDB; Q6P686; -.
DR   TreeFam; TF314534; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q6P686; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000012156; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q6P686; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
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..214
FT                   /note="Osteoclast-stimulating factor 1"
FT                   /id="PRO_0000238956"
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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92882"
FT   MOD_RES         200
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92882"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92882"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        124
FT                   /note="V -> D (in Ref. 1; AAM82159)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   214 AA;  23669 MW;  2F849A11D40C692F CRC64;
     MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTSWW KGTCKGRTGL
     IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
     IVEVLFTQPN VELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN NEKKLALDMA
     TNAACASLLK KKQATDGART LSNAEDYLDD EDSD