OSTF1_BOVIN
ID OSTF1_BOVIN Reviewed; 214 AA.
AC Q8MJ50;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Osteoclast-stimulating factor 1;
GN Name=OSTF1;
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 [MRNA].
RC TISSUE=Brain;
RA Guo J.H.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; AF523267; AAM82160.1; -; mRNA.
DR EMBL; BC112669; AAI12670.1; -; mRNA.
DR RefSeq; NP_776834.1; NM_174409.2.
DR AlphaFoldDB; Q8MJ50; -.
DR SMR; Q8MJ50; -.
DR STRING; 9913.ENSBTAP00000003560; -.
DR PaxDb; Q8MJ50; -.
DR PeptideAtlas; Q8MJ50; -.
DR PRIDE; Q8MJ50; -.
DR Ensembl; ENSBTAT00000003560; ENSBTAP00000003560; ENSBTAG00000002746.
DR GeneID; 281961; -.
DR KEGG; bta:281961; -.
DR CTD; 26578; -.
DR VEuPathDB; HostDB:ENSBTAG00000002746; -.
DR VGNC; VGNC:32479; OSTF1.
DR eggNOG; ENOG502QTZB; Eukaryota.
DR GeneTree; ENSGT00920000149159; -.
DR HOGENOM; CLU_092255_0_0_1; -.
DR InParanoid; Q8MJ50; -.
DR OMA; NMSWLRE; -.
DR OrthoDB; 1453481at2759; -.
DR TreeFam; TF314534; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000002746; Expressed in monocyte and 105 other tissues.
DR ExpressionAtlas; Q8MJ50; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
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 2: Evidence at transcript 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_0000238954"
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 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92882"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92882"
SQ SEQUENCE 214 AA; 23842 MW; 20E051518D032A3C CRC64;
MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTNWW KGTCKGRTGL
IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHRD
IVEMLFTQPN IELNQQNKLG DTALHAAAWK GYADIVQLLL EKGARTDLRN NEKKLALDMA
TNAACASLLK KKQGTDAVRS LSNAEDYLDD EDSD