ID   SPP24_BOVIN             Reviewed;         203 AA.
AC   Q27967; Q3ZBZ5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Secreted phosphoprotein 24;
DE            Short=Spp-24;
DE   AltName: Full=Secreted phosphoprotein 2;
DE   Flags: Precursor;
GN   Name=SPP2; Synonyms=SPP24;
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], AND PROTEIN SEQUENCE OF 24-45; 143-160 AND
RP   179-198.
RC   TISSUE=Bone, and Liver;
RX   PubMed=7814406; DOI=10.1074/jbc.270.19.11619;
RA   Hu B., Coulson L., Moyer B., Price P.A.;
RT   "Isolation and molecular cloning of a novel bone phosphoprotein related in
RT   sequence to the cystatin family of thiol protease inhibitors.";
RL   J. Biol. Chem. 270:431-436(1995).
RN   [2]
RP   ERRATUM OF PUBMED:7814406.
RA   Hu B., Coulson L., Moyer B., Price P.A.;
RL   J. Biol. Chem. 270:10359-10359(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Rumen reticulum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could coordinate an aspect of bone turnover.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: In liver and bone but not in heart, lung, kidney,
CC       or spleen.
CC   -!- PTM: Multiply phosphorylated at serine residues in Ser-X-Glu/Ser(P)
CC       sequences, a recognition motif for phosphorylation by secretory pathway
CC       protein kinase.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPP2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U03872; AAA63582.1; -; mRNA.
DR   EMBL; BC103007; AAI03008.1; -; mRNA.
DR   PIR; I46051; I46051.
DR   RefSeq; NP_776613.2; NM_174188.3.
DR   AlphaFoldDB; Q27967; -.
DR   SMR; Q27967; -.
DR   STRING; 9913.ENSBTAP00000002631; -.
DR   PaxDb; Q27967; -.
DR   PRIDE; Q27967; -.
DR   Ensembl; ENSBTAT00000002631; ENSBTAP00000002631; ENSBTAG00000002030.
DR   GeneID; 281500; -.
DR   KEGG; bta:281500; -.
DR   CTD; 6694; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002030; -.
DR   VGNC; VGNC:35233; SPP2.
DR   eggNOG; ENOG502S7TB; Eukaryota.
DR   GeneTree; ENSGT00390000009001; -.
DR   HOGENOM; CLU_115216_0_0_1; -.
DR   InParanoid; Q27967; -.
DR   OMA; NHQHRAR; -.
DR   OrthoDB; 1281655at2759; -.
DR   TreeFam; TF335972; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000002030; Expressed in liver and 56 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046849; P:bone remodeling; IEA:InterPro.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR010892; Spp-24.
DR   PANTHER; PTHR15444; PTHR15444; 1.
DR   Pfam; PF07448; Spp-24; 1.
DR   SUPFAM; SSF54403; SSF54403; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:7814406"
FT   CHAIN           24..203
FT                   /note="Secreted phosphoprotein 24"
FT                   /id="PRO_0000022402"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13103"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62740"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62740"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1I3"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62740"
FT   DISULFID        86..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        110..128
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   203 AA;  23134 MW;  DDE820EA1018CB41 CRC64;
     MEKMAMKMLV IFVLGMNHWT CTGFPVYDYD PASLKEALSA SVAKVNSQSL SPYLFRAFRS
     SVKRVNALDE DSLTMDLEFR IQETTCRRES EADPATCDFQ RGYHVPVAVC RSTVRMSAEQ
     VQNVWVRCHW SSSSGSSSSE EMFFGDILGS STSRNSYLLG LTPDRSRGEP LYEPSREMRR
     NFPLGNRRYS NPWPRARVNP GFE