ID   SPP24_RAT               Reviewed;         203 AA.
AC   Q62740; Q5M874;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   25-MAY-2022, entry version 116.
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   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 [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-203.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Hu B., Price P.A.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-138 AND SER-174, AND
RP   IDENTIFICATION BY 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: Could coordinate an aspect of bone turnover. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Multiply phosphorylated at serine residues. {ECO:0000250}.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPP2 family. {ECO:0000305}.
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DR   EMBL; BC088193; AAH88193.1; -; mRNA.
DR   EMBL; U19485; AAA87903.1; -; mRNA.
DR   RefSeq; NP_446029.1; NM_053577.1.
DR   AlphaFoldDB; Q62740; -.
DR   SMR; Q62740; -.
DR   STRING; 10116.ENSRNOP00000026108; -.
DR   iPTMnet; Q62740; -.
DR   PhosphoSitePlus; Q62740; -.
DR   PaxDb; Q62740; -.
DR   PRIDE; Q62740; -.
DR   GeneID; 94168; -.
DR   KEGG; rno:94168; -.
DR   UCSC; RGD:708488; rat.
DR   CTD; 6694; -.
DR   RGD; 708488; Spp2.
DR   eggNOG; ENOG502S7TB; Eukaryota.
DR   InParanoid; Q62740; -.
DR   OrthoDB; 1281655at2759; -.
DR   PhylomeDB; Q62740; -.
DR   TreeFam; TF335972; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q62740; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0046849; P:bone remodeling; IEA:InterPro.
DR   GO; GO:0065003; P:protein-containing complex assembly; IPI:RGD.
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   Disulfide bond; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..203
FT                   /note="Secreted phosphoprotein 24"
FT                   /id="PRO_0000072146"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13103"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   DISULFID        86..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..127
FT                   /evidence="ECO:0000250"
FT   CONFLICT        130
FT                   /note="A -> R (in Ref. 2; AAA87903)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   203 AA;  23170 MW;  5B9BCA590DC7F63E CRC64;
     MELATMKTLV MLVLGMHYWC ASGFPVYDYD PSSLQEALSA SVAKVNSQSL SPYLFRATRS
     SLKRVNVLDE DTLVMNLEFT VQETTCLRES GDPSTCAFQR GYSVPTAACR STVQMSKGQV
     KDVWAHCRWA STSESNSSEE MIFGDMARSH RRRNDYLLGF LYDEPKGEQF YDRSIEITRR
     GHPPAHRRFL NLQRRARVNS GFE