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Osteopontin (Bone sialoprotein 1) (Secreted phosphoprotein 1) (SPP-1)

 OSTP_RAT                Reviewed;         317 AA.
P08721;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 2.
17-JUN-2020, entry version 149.
RecName: Full=Osteopontin;
AltName: Full=Bone sialoprotein 1;
AltName: Full=Secreted phosphoprotein 1;
Short=SPP-1;
Flags: Precursor;
Name=Spp1; Synonyms=2b7, Spp-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=1429723;
Singh K., Mukherjee A.B., de Vouge M.W., Mukherjee B.B.;
"Differential processing of osteopontin transcripts in rat kidney- and
osteoblast-derived cell lines.";
J. Biol. Chem. 267:23847-23851(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3024151; DOI=10.1073/pnas.83.23.8819;
Oldberg A., Franzen A., Heinegaard D.;
"Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA
reveals an Arg-Gly-Asp cell-binding sequence.";
Proc. Natl. Acad. Sci. U.S.A. 83:8819-8823(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Smooth muscle;
PubMed=8408622; DOI=10.1172/jci116755;
Giachelli C.M., Bae N., Almeida M., Denhardt D.T., Alpers C.E.,
Schwartz S.M.;
"Osteopontin is elevated during neointima formation in rat arteries and is
a novel component of human atherosclerotic plaques.";
J. Clin. Invest. 92:1686-1696(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 17-25 AND 154-167.
PubMed=2736258; DOI=10.1016/0167-4838(89)90092-7;
Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.;
"Purification of a human milk protein closely similar to tumor-secreted
phosphoproteins and osteopontin.";
Biochim. Biophys. Acta 996:43-48(1989).
[6]
PROTEIN SEQUENCE OF 17-27.
TISSUE=Bone;
PubMed=3469201;
Prince C.W., Oosawa T., Butler W.T., Tomana M., Bhown A.S., Bhown M.,
Schrohenloher R.E.;
"Isolation, characterization, and biosynthesis of a phosphorylated
glycoprotein from rat bone.";
J. Biol. Chem. 262:2900-2907(1987).
[7]
PROTEIN SEQUENCE OF 17-25.
PubMed=3167835;
Senger D.R., Perruzzi C.A., Gracey C.F., Papadopoulos A., Tenen D.G.;
"Secreted phosphoproteins associated with neoplastic transformation: close
homology with plasma proteins cleaved during blood coagulation.";
Cancer Res. 48:5770-5774(1988).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-63, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Binds tightly to hydroxyapatite. Appears to form an integral
part of the mineralized matrix. Probably important to cell-matrix
interaction.
-!- FUNCTION: Acts as a cytokine involved in enhancing production of
interferon-gamma and interleukin-12 and reducing production of
interleukin-10 and is essential in the pathway that leads to type I
immunity. {ECO:0000250}.
-!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Extensively phosphorylated by FAM20C in the extracellular medium
at multiple sites within the S-x-E/pS motif.
{ECO:0000250|UniProtKB:P10451}.
-!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P10451}.
-!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
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EMBL; M99252; AAA41765.1; -; mRNA.
EMBL; M14656; AAA41762.1; -; mRNA.
EMBL; BC078874; AAH78874.1; -; mRNA.
PIR; A25917; A25917.
PIR; JC5811; JC5811.
RefSeq; NP_037013.2; NM_012881.2.
RefSeq; XP_008768218.1; XM_008769996.2.
BioGRID; 247392; 4.
ELM; P08721; -.
IntAct; P08721; 2.
MINT; P08721; -.
STRING; 10116.ENSRNOP00000062358; -.
iPTMnet; P08721; -.
PhosphoSitePlus; P08721; -.
PaxDb; P08721; -.
PRIDE; P08721; -.
Ensembl; ENSRNOT00000067875; ENSRNOP00000062358; ENSRNOG00000043451.
Ensembl; ENSRNOT00000075989; ENSRNOP00000068511; ENSRNOG00000043451.
GeneID; 25353; -.
KEGG; rno:25353; -.
CTD; 6696; -.
RGD; 3752; Spp1.
eggNOG; ENOG410IVP1; Eukaryota.
eggNOG; ENOG41116B5; LUCA.
GeneTree; ENSGT00390000002509; -.
HOGENOM; CLU_953033_0_0_1; -.
InParanoid; P08721; -.
KO; K06250; -.
OMA; DHSVETH; -.
OrthoDB; 1280650at2759; -.
PhylomeDB; P08721; -.
Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
Reactome; R-RNO-186797; Signaling by PDGF.
Reactome; R-RNO-216083; Integrin cell surface interactions.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
PRO; PR:P08721; -.
Proteomes; UP000002494; Chromosome 14.
Bgee; ENSRNOG00000043451; Expressed in adult mammalian kidney and 9 other tissues.
Genevisible; P08721; RN.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0042995; C:cell projection; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
GO; GO:0005178; F:integrin binding; ISO:RGD.
GO; GO:0006710; P:androgen catabolic process; ISO:RGD.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IDA:RGD.
GO; GO:0030154; P:cell differentiation; IEP:RGD.
GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:RGD.
GO; GO:0006954; P:inflammatory response; IEP:RGD.
GO; GO:0048685; P:negative regulation of collateral sprouting of intact axon in response to injury; IEP:RGD.
GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
GO; GO:0001649; P:osteoblast differentiation; IMP:RGD.
GO; GO:0045780; P:positive regulation of bone resorption; IDA:RGD.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
GO; GO:2000866; P:positive regulation of estradiol secretion; ISO:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
GO; GO:0048545; P:response to steroid hormone; IDA:RGD.
GO; GO:0033280; P:response to vitamin D; ISO:RGD.
InterPro; IPR002038; Osteopontin.
InterPro; IPR019841; Osteopontin_CS.
PANTHER; PTHR10607; PTHR10607; 1.
Pfam; PF00865; Osteopontin; 2.
PRINTS; PR00216; OSTEOPONTIN.
SMART; SM00017; OSTEO; 1.
PROSITE; PS00884; OSTEOPONTIN; 1.
1: Evidence at protein level;
Biomineralization; Cell adhesion; Cytokine; Direct protein sequencing;
Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Sialic acid;
Signal.
SIGNAL 1..16
/evidence="ECO:0000269|PubMed:2736258,
ECO:0000269|PubMed:3167835, ECO:0000269|PubMed:3469201"
CHAIN 17..317
/note="Osteopontin"
/id="PRO_0000020325"
MOTIF 144..146
/note="Cell attachment site"
COMPBIAS 86..96
/note="Poly-Asp"
MOD_RES 26
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 27
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 60
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 62
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 63
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:22673903"
MOD_RES 66
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 76
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 78
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 81
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 106
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 109
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 112
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 115
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 118
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 170
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 175
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 176
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 180
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 200
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 204
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 209
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 213
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 219
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 222
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 224
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 228
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 257
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 261
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 266
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 270
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 273
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 278
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 283
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 294
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 306
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 311
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 313
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 314
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
CARBOHYD 123
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
CARBOHYD 132
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
CARBOHYD 137
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
CONFLICT 8
/note="F -> L (in Ref. 2; AAA41762)"
/evidence="ECO:0000305"
SEQUENCE 317 AA; 34963 MW; 73CB5C21FFF62310 CRC64;
MRLAVVCFCL FGLASCLPVK VAEFGSSEEK AHYSKHSDAV ATWLKPDPSQ KQNLLAPQNS
VSSEETDDFK QETLPSNSNE SHDHMDDDDD DDDDGDHAES EDSVNSDESD ESHHSDESDE
SFTASTQADV LTPIAPTVDV PDGRGDSLAY GLRSKSRSFP VSDEQYPDAT DEDLTSRMKS
QESDEAIKVI PVAQRLSVPS DQDSNGKTSH ESSQLDEPSV ETHSLEQSKE YKQRASHEST
EQSDAIDSAE KPDAIDSAER SDAIDSQASS KASLEHQSHE FHSHEDKLVL DPKSKEDDRY
LKFRISHELE SSSSEVN


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