OSTP_SHEEP
ID OSTP_SHEEP Reviewed; 278 AA.
AC Q9XSY9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 82.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endometrium;
RX PubMed=10491620; DOI=10.1095/biolreprod61.4.884;
RA Johnson G.A., Spencer T.E., Burghardt R.C., Bazer F.W.;
RT "Ovine osteopontin: I. Cloning and expression of messenger ribonucleic acid
RT in the uterus during the periimplantation period.";
RL Biol. Reprod. 61:884-891(1999).
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; AF152416; AAD38388.1; -; mRNA.
DR RefSeq; NP_001009224.1; NM_001009224.1.
DR AlphaFoldDB; Q9XSY9; -.
DR STRING; 9940.ENSOARP00000002753; -.
DR GeneID; 443058; -.
DR KEGG; oas:443058; -.
DR CTD; 6696; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR OrthoDB; 1280650at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
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 2: Evidence at transcript level;
KW Biomineralization; Cell adhesion; Cytokine; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Sialic acid; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..278
FT /note="Osteopontin"
FT /id="PRO_0000020326"
FT REGION 18..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..154
FT /note="Cell attachment site"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 166..233
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 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 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
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 103
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:P10451"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 210
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:0000250|UniProtKB:P10451"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
SQ 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
