OSTP_PIG
ID OSTP_PIG Reviewed; 303 AA.
AC P14287;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Osteopontin;
DE AltName: Full=Bone sialoprotein 1;
DE AltName: Full=Secreted phosphoprotein 1;
DE Short=SPP-1;
DE Flags: Precursor;
GN Name=SPP1; Synonyms=OPN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RX PubMed=2602123; DOI=10.1093/nar/17.23.10119;
RA Wrana J.L., Zhang Q., Sodek J.;
RT "Full length cDNA sequence of porcine secreted phosphoprotein-I (SPP-I,
RT osteopontin).";
RL Nucleic Acids Res. 17:10119-10119(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=1633816; DOI=10.1111/j.1432-1033.1992.tb17092.x;
RA Zhang Q., Wrana J.L., Sodek J.;
RT "Characterization of the promoter region of the porcine opn (osteopontin,
RT secreted phosphoprotein 1) gene. Identification of positive and negative
RT regulatory elements and a 'silent' second promoter.";
RL Eur. J. Biochem. 207:649-659(1992).
RN [3]
RP PROTEIN SEQUENCE OF 17-36 AND 172-211.
RC TISSUE=Bone;
RX PubMed=2332443; DOI=10.1016/s0021-9258(19)39154-9;
RA Zhang Q., Domenicucci C., Goldberg H.A., Wrana J.L., Sodek J.;
RT "Characterization of fetal porcine bone sialoproteins, secreted
RT phosphoprotein I (SPPI, osteopontin), bone sialoprotein, and a 23-kDa
RT glycoprotein. Demonstration that the 23-kDa glycoprotein is derived from
RT the carboxyl terminus of SPPI.";
RL J. Biol. Chem. 265:7583-7589(1990).
CC -!- FUNCTION: Major non-collagenous bone protein that binds tightly to
CC hydroxyapatite. Appears to form an integral part of the mineralized
CC matrix. Probably important to cell-matrix interaction.
CC {ECO:0000250|UniProtKB:P31096}.
CC -!- FUNCTION: Acts as a cytokine involved in enhancing production of
CC interferon-gamma and interleukin-12 and reducing production of
CC interleukin-10 and is essential in the pathway that leads to type I
CC immunity. {ECO:0000250|UniProtKB:P10923}.
CC -!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Extensively phosphorylated by FAM20C in the extracellular medium
CC at multiple sites within the S-x-E/pS motif (By similarity). The
CC phosphorylated form inhibits hydroxyapatite crystallization.
CC Dephosphorylation via a mechanism involving ALPL/TNAP promotes
CC hydroxyapatite crystallization (By similarity).
CC {ECO:0000250|UniProtKB:P10451, ECO:0000250|UniProtKB:P10923}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P10451}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers, increasing its collagen
CC binding properties. {ECO:0000250|UniProtKB:P31096}.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
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DR EMBL; X16575; CAA34594.1; -; mRNA.
DR EMBL; M84121; AAA31094.1; -; Genomic_DNA.
DR PIR; S14903; GEPGO.
DR RefSeq; NP_999188.1; NM_214023.1.
DR RefSeq; XP_005667061.1; XM_005667004.2.
DR AlphaFoldDB; P14287; -.
DR STRING; 9823.ENSSSCP00000009825; -.
DR PaxDb; P14287; -.
DR PeptideAtlas; P14287; -.
DR PRIDE; P14287; -.
DR Ensembl; ENSSSCT00000010091; ENSSSCP00000009825; ENSSSCG00000009216.
DR Ensembl; ENSSSCT00025053980; ENSSSCP00025023011; ENSSSCG00025039675.
DR Ensembl; ENSSSCT00035084076; ENSSSCP00035034940; ENSSSCG00035062546.
DR Ensembl; ENSSSCT00055051287; ENSSSCP00055041003; ENSSSCG00055025973.
DR Ensembl; ENSSSCT00055051444; ENSSSCP00055041120; ENSSSCG00055025973.
DR Ensembl; ENSSSCT00065050638; ENSSSCP00065021942; ENSSSCG00065037058.
DR GeneID; 397087; -.
DR KEGG; ssc:397087; -.
DR CTD; 6696; -.
DR VGNC; VGNC:93419; SPP1.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR GeneTree; ENSGT00390000002509; -.
DR HOGENOM; CLU_953033_0_0_1; -.
DR InParanoid; P14287; -.
DR OMA; DHSVETH; -.
DR OrthoDB; 1280650at2759; -.
DR TreeFam; TF350201; -.
DR Reactome; R-SSC-1474228; Degradation of the extracellular matrix.
DR Reactome; R-SSC-186797; Signaling by PDGF.
DR Reactome; R-SSC-216083; Integrin cell surface interactions.
DR Reactome; R-SSC-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-SSC-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000009216; Expressed in pons and 43 other tissues.
DR ExpressionAtlas; P14287; baseline and differential.
DR Genevisible; P14287; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0006710; P:androgen catabolic process; IEA:Ensembl.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
DR GO; GO:2000866; P:positive regulation of estradiol secretion; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR InterPro; IPR002038; Osteopontin.
DR InterPro; IPR019841; Osteopontin_CS.
DR PANTHER; PTHR10607; PTHR10607; 1.
DR Pfam; PF00865; Osteopontin; 1.
DR PRINTS; PR00216; OSTEOPONTIN.
DR SMART; SM00017; OSTEO; 1.
DR PROSITE; PS00884; OSTEOPONTIN; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell adhesion; Cytokine; Direct protein sequencing;
KW Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Sialic acid;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..303
FT /note="Osteopontin"
FT /id="PRO_0000020323"
FT REGION 45..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..156
FT /note="Cell attachment site"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 130
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 139
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 142
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 147
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33669 MW; 87D6240E24013EF7 CRC64;
MRIAVIAFCL WGFASALPVK QTNSGSSEEK LLSNKYTDAV ATLLKPDPSQ KQTFLAPQNT
ISSEETDDFK QETLPSKSNE SPEQTDDVDD DDDEDHVDSR DTDSEEADHA DDADRSDESH
HSDESDELVT DFPTDTPATD VTPAVPTGDP NDGRGDSVVY GLRSKSKKFR RSEAQQLDAT
EEDLTSHVES EETDGTPKAI LVAQRLHVAS DLDSQEKDSQ ETSQPDDRSV ETRSQEQSKE
YTIKTYDGSN EHSNVIESQE NPKVSQEFHS HEDKLVPDSK SEEDKHLKLR VSHELESASS
EIN
