OSTP_RAT
ID OSTP_RAT Reviewed; 317 AA.
AC P08721;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 157.
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=2b7, Spp-1;
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 [MRNA].
RC TISSUE=Kidney;
RX PubMed=1429723; DOI=10.1016/s0021-9258(18)35914-3;
RA Singh K., Mukherjee A.B., de Vouge M.W., Mukherjee B.B.;
RT "Differential processing of osteopontin transcripts in rat kidney- and
RT osteoblast-derived cell lines.";
RL J. Biol. Chem. 267:23847-23851(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3024151; DOI=10.1073/pnas.83.23.8819;
RA Oldberg A., Franzen A., Heinegaard D.;
RT "Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA
RT reveals an Arg-Gly-Asp cell-binding sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8819-8823(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Smooth muscle;
RX PubMed=8408622; DOI=10.1172/jci116755;
RA Giachelli C.M., Bae N., Almeida M., Denhardt D.T., Alpers C.E.,
RA Schwartz S.M.;
RT "Osteopontin is elevated during neointima formation in rat arteries and is
RT a novel component of human atherosclerotic plaques.";
RL J. Clin. Invest. 92:1686-1696(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP PROTEIN SEQUENCE OF 17-25 AND 154-167.
RX PubMed=2736258; DOI=10.1016/0167-4838(89)90092-7;
RA Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.;
RT "Purification of a human milk protein closely similar to tumor-secreted
RT phosphoproteins and osteopontin.";
RL Biochim. Biophys. Acta 996:43-48(1989).
RN [6]
RP PROTEIN SEQUENCE OF 17-27.
RC TISSUE=Bone;
RX PubMed=3469201; DOI=10.1016/s0021-9258(18)61592-3;
RA Prince C.W., Oosawa T., Butler W.T., Tomana M., Bhown A.S., Bhown M.,
RA Schrohenloher R.E.;
RT "Isolation, characterization, and biosynthesis of a phosphorylated
RT glycoprotein from rat bone.";
RL J. Biol. Chem. 262:2900-2907(1987).
RN [7]
RP PROTEIN SEQUENCE OF 17-25.
RX PubMed=3167835;
RA Senger D.R., Perruzzi C.A., Gracey C.F., Papadopoulos A., Tenen D.G.;
RT "Secreted phosphoproteins associated with neoplastic transformation: close
RT homology with plasma proteins cleaved during blood coagulation.";
RL Cancer Res. 48:5770-5774(1988).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-63, 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: 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; M99252; AAA41765.1; -; mRNA.
DR EMBL; M14656; AAA41762.1; -; mRNA.
DR EMBL; BC078874; AAH78874.1; -; mRNA.
DR PIR; A25917; A25917.
DR PIR; JC5811; JC5811.
DR RefSeq; NP_037013.2; NM_012881.2.
DR RefSeq; XP_008768218.1; XM_008769996.2.
DR AlphaFoldDB; P08721; -.
DR BioGRID; 247392; 4.
DR ELM; P08721; -.
DR IntAct; P08721; 2.
DR MINT; P08721; -.
DR STRING; 10116.ENSRNOP00000062358; -.
DR GlyGen; P08721; 3 sites.
DR iPTMnet; P08721; -.
DR PhosphoSitePlus; P08721; -.
DR PaxDb; P08721; -.
DR Ensembl; ENSRNOT00000067875; ENSRNOP00000062358; ENSRNOG00000043451.
DR GeneID; 25353; -.
DR KEGG; rno:25353; -.
DR CTD; 6696; -.
DR RGD; 3752; Spp1.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR GeneTree; ENSGT00390000002509; -.
DR HOGENOM; CLU_953033_0_0_1; -.
DR InParanoid; P08721; -.
DR OMA; DHSVETH; -.
DR OrthoDB; 1280650at2759; -.
DR PhylomeDB; P08721; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
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:P08721; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000043451; Expressed in kidney and 18 other tissues.
DR Genevisible; P08721; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0006710; P:androgen catabolic process; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0030154; P:cell differentiation; IEP:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:RGD.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:RGD.
DR GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:RGD.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
DR GO; GO:0072044; P:collecting duct development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0048685; P:negative regulation of collateral sprouting of intact axon in response to injury; IEP:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; IDA:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:2000866; P:positive regulation of estradiol secretion; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IDA:RGD.
DR GO; GO:0033280; P:response to vitamin D; ISO:RGD.
DR GO; GO:0034418; P:urate biosynthetic process; ISO:RGD.
DR InterPro; IPR002038; Osteopontin.
DR InterPro; IPR019841; Osteopontin_CS.
DR PANTHER; PTHR10607; PTHR10607; 1.
DR Pfam; PF00865; Osteopontin; 2.
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:0000269|PubMed:2736258,
FT ECO:0000269|PubMed:3167835, ECO:0000269|PubMed:3469201"
FT CHAIN 17..317
FT /note="Osteopontin"
FT /id="PRO_0000020325"
FT REGION 43..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..146
FT /note="Cell attachment site"
FT COMPBIAS 46..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 213
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 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 266
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 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 123
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="F -> L (in Ref. 2; AAA41762)"
FT /evidence="ECO:0000305"
SQ 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
