OSTP_BOVIN
ID OSTP_BOVIN Reviewed; 278 AA.
AC P31096; Q56NM9; Q8SPS6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 122.
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 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].
RX PubMed=1721033; DOI=10.1016/0378-1119(91)90439-i;
RA Kerr J.M., Fisher L.W., Termine J.D., Young M.F.;
RT "The cDNA cloning and RNA distribution of bovine osteopontin.";
RL Gene 108:237-243(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Korean; TISSUE=Kidney;
RA Lee T.Y., Ju S.K., Nam M.S.;
RT "Cloning of osteopontin (OPN) in Korean native cattle.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15867146; DOI=10.1073/pnas.0502398102;
RA Schnabel R.D., Kim J.J., Ashwell M.S., Sonstegard T.S., Van Tassell C.P.,
RA Connor E.E., Taylor J.F.;
RT "Fine-mapping milk production quantitative trait loci on BTA6: Analysis of
RT the bovine osteopontin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:6896-6901(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Holstein;
RX PubMed=15998908; DOI=10.1101/gr.3806705;
RA Cohen-Zinder M., Seroussi E., Larkin D.M., Loor J.J.,
RA Everts-van der Wind A., Lee J.-H., Drackley J.K., Band M.R.,
RA Hernandez A.G., Shani M., Lewin H.A., Weller J.I., Ron M.;
RT "Identification of a missense mutation in the bovine ABCG2 gene with a
RT major effect on the QTL on chromosome 6 affecting milk yield and
RT composition in Holstein cattle.";
RL Genome Res. 15:936-944(2005).
RN [5]
RP PROTEIN SEQUENCE OF 17-22; 44-54; 168-182 AND 221-243.
RC TISSUE=Milk;
RX PubMed=8320368; DOI=10.1017/s0022029900027503;
RA Soerensen E.S., Petersen T.E.;
RT "Purification and characterization of three proteins isolated from the
RT proteose peptone fraction of bovine milk.";
RL J. Dairy Res. 60:189-197(1993).
RN [6]
RP PROTEIN SEQUENCE OF 17-28, AND PHOSPHORYLATION.
RX PubMed=8663267; DOI=10.1074/jbc.271.28.16897;
RA Salih E., Zhou H.-Y., Glimcher M.J.;
RT "Phosphorylation of purified bovine bone sialoprotein and osteopontin by
RT protein kinases.";
RL J. Biol. Chem. 271:16897-16905(1996).
RN [7]
RP PHOSPHORYLATION AT SER-23; SER-24; SER-26; SER-27; SER-60; SER-62; SER-63;
RP SER-76; SER-78; SER-81; SER-95; SER-100; SER-103; SER-115; SER-121;
RP SER-124; THR-178; SER-184; SER-188; SER-205; SER-210; SER-233; SER-240;
RP SER-245; SER-256; SER-267; SER-272 AND SER-274.
RC TISSUE=Milk;
RX PubMed=8535240; DOI=10.1002/pro.5560041009;
RA Soerensen E.S., Hoejrup P., Petersen T.E.;
RT "Posttranslational modifications of bovine osteopontin: identification of
RT twenty-eight phosphorylation and three O-glycosylation sites.";
RL Protein Sci. 4:2040-2049(1995).
RN [8]
RP FUNCTION, AND TRANSGLUTAMINATION.
RX PubMed=9880554; DOI=10.1074/jbc.274.3.1729;
RA Kaartinen M.T., Pirhonen A., Linnala-Kankkunen A., Maeenpaeae P.H.;
RT "Cross-linking of osteopontin by tissue transglutaminase increases its
RT collagen binding properties.";
RL J. Biol. Chem. 274:1729-1735(1999).
CC -!- FUNCTION: Major non-collagenous bone protein that binds tightly to
CC hydroxyapatite (Probable). Appears to form an integral part of the
CC mineralized matrix (Probable). Probably important to cell-matrix
CC interaction (Probable). {ECO:0000305|PubMed:9880554}.
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 -!- TISSUE SPECIFICITY: Bone, inner ear, kidney, uterus, lung, brain,
CC epidermis.
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: 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:0000269|PubMed:9880554}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P10451}.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
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DR EMBL; M66236; AAA30462.1; -; mRNA.
DR EMBL; AF492837; AAL99081.1; -; mRNA.
DR EMBL; AY878328; AAX62809.1; -; Genomic_DNA.
DR EMBL; AJ871176; CAI38798.1; -; Genomic_DNA.
DR PIR; JS0638; JS0638.
DR RefSeq; NP_776612.1; NM_174187.2.
DR RefSeq; XP_005207799.1; XM_005207742.1.
DR AlphaFoldDB; P31096; -.
DR ELM; P31096; -.
DR STRING; 9913.ENSBTAP00000044782; -.
DR iPTMnet; P31096; -.
DR PaxDb; P31096; -.
DR PeptideAtlas; P31096; -.
DR PRIDE; P31096; -.
DR GeneID; 281499; -.
DR KEGG; bta:281499; -.
DR CTD; 6696; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR InParanoid; P31096; -.
DR OrthoDB; 1280650at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
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:8320368,
FT ECO:0000269|PubMed:8663267"
FT CHAIN 17..278
FT /note="Osteopontin"
FT /id="PRO_0000020320"
FT REGION 38..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..154
FT /note="Cell attachment site"
FT COMPBIAS 46..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..111
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 79
FT /note="Not glycosylated"
FT SITE 101
FT /note="Not glycosylated"
FT SITE 209
FT /note="Not glycosylated"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 214
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 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8535240"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 131
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 140
FT /note="O-linked (GalNAc...) threonine"
FT CARBOHYD 145
FT /note="O-linked (GalNAc...) threonine"
FT CONFLICT 27
FT /note="S -> K (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> I (in Ref. 1; AAA30462)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> T (in Ref. 1; AAA30462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 30904 MW; 8170204507864E87 CRC64;
MRIAVICFCL LGIASALPVK PTSSGSSEEK QLNNKYPDAV ATWLKPDPSQ KQTFLAPQNS
VSSEETDDNK QNTLPSKSNE SPEQTDDLDD DDDNSQDVNS NDSDDAETTD DPDHSDESHH
SDESDEVDFP TDIPTIAVFT PFIPTESAND GRGDSVAYGL KSRSKKFRRS NVQSPDATEE
DFTSHIESEE MHDAPKKTSQ LTDHSKETNS SELSKELTPK AKDKNKHSNL IESQENSKLS
QEFHSLEDKL DLDHKSEEDK HLKIRISHEL DSASSEVN
