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

 OSTP_SHEEP              Reviewed;         278 AA.
Q9XSY9;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
11-DEC-2019, entry version 76.
RecName: Full=Osteopontin;
AltName: Full=Bone sialoprotein 1;
AltName: Full=Secreted phosphoprotein 1;
Short=SPP-1;
Flags: Precursor;
Name=SPP1; Synonyms=OPN;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endometrium;
PubMed=10491620; DOI=10.1095/biolreprod61.4.884;
Johnson G.A., Spencer T.E., Burghardt R.C., Bazer F.W.;
"Ovine osteopontin: I. Cloning and expression of messenger ribonucleic acid
in the uterus during the periimplantation period.";
Biol. Reprod. 61:884-891(1999).
-!- 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; AF152416; AAD38388.1; -; mRNA.
RefSeq; NP_001009224.1; NM_001009224.1.
STRING; 9940.ENSOARP00000002753; -.
GeneID; 443058; -.
KEGG; oas:443058; -.
CTD; 6696; -.
KO; K06250; -.
OrthoDB; 1280650at2759; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0001503; P:ossification; IEA:InterPro.
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.
2: Evidence at transcript level;
Biomineralization; Cell adhesion; Cytokine; Glycoprotein; Phosphoprotein;
Reference proteome; Secreted; Sialic acid; Signal.
SIGNAL 1..16
/evidence="ECO:0000250"
CHAIN 17..278
/note="Osteopontin"
/id="PRO_0000020326"
MOTIF 152..154
/note="Cell attachment site"
MOD_RES 24
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
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:0000250|UniProtKB:P10451"
MOD_RES 63
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
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 103
/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:P10451"
MOD_RES 121
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 124
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 178
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P31096"
MOD_RES 183
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 184
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 188
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 199
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 205
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 208
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 210
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 228
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 233
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 237
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 240
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 245
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 256
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 267
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 272
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 274
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
MOD_RES 275
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10451"
CARBOHYD 116
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 131
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
CARBOHYD 140
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
CARBOHYD 145
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000250"
SEQUENCE 278 AA; 31052 MW; 37D49E1DD1FBFD47 CRC64;
MRIAVICFCL LGIASALPVK PTSSGSSEEK QLNNKYPDAV ATWLKPDPSQ KQTFLEPQNS
VSSEETDDNK QNTLPSKSNE SPEQTDDLDD DDENSQEVNS DDSDDAETPD DSDHSNESHH
SDESDEADFP TDIPTIAVFT PPFPTESTND GRGDSVAYGL KSKSKKFRRS NVESPDATEE
DFTSHIESEE MHDAPKKTSQ LTDHSEETNS DELPKELTPK AKEESKHSNR IESQENSKLS
QEFHSLEDKL DLDHKSEEDK RLKIRISHEL DSVSSEVN


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