OSTP_RABIT
ID OSTP_RABIT Reviewed; 311 AA.
AC P31097; P46631;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Osteopontin;
DE AltName: Full=Bone sialoprotein 1;
DE AltName: Full=OC-1;
DE AltName: Full=Secreted phosphoprotein 1;
DE Short=SPP-1;
DE Flags: Precursor;
GN Name=SPP1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Osteoclast;
RX PubMed=1379809; DOI=10.1016/0006-291x(92)90832-6;
RA Tezuka K., Sato T., Kamioka H., Nijweide P.J., Tanaka K., Matsuo T.,
RA Ohta M., Kurihara N., Hakeda Y., Kumegawa M.;
RT "Identification of osteopontin in isolated rabbit osteoclasts.";
RL Biochem. Biophys. Res. Commun. 186:911-917(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Myeloid;
RX PubMed=7717985; DOI=10.1042/bj3070257;
RA Nasu K., Ishida T., Setoguchi M., Higuchi Y., Akizuki S., Yamamoto S.;
RT "Expression of wild-type and mutated rabbit osteopontin in Escherichia
RT coli, and their effects on adhesion and migration of P388D1 cells.";
RL Biochem. J. 307:257-265(1995).
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; D11411; BAA01993.1; -; mRNA.
DR EMBL; D16544; BAA03980.1; -; mRNA.
DR PIR; JC1191; JC1191.
DR RefSeq; NP_001075663.1; NM_001082194.1.
DR AlphaFoldDB; P31097; -.
DR STRING; 9986.ENSOCUP00000021885; -.
DR GeneID; 100008982; -.
DR KEGG; ocu:100008982; -.
DR CTD; 6696; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR InParanoid; P31097; -.
DR OrthoDB; 1280650at2759; -.
DR Proteomes; UP000001811; 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; 2.
DR Pfam; PF00865; Osteopontin; 1.
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..311
FT /note="Osteopontin"
FT /id="PRO_0000020324"
FT REGION 28..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 155..157
FT /note="Cell attachment site"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..302
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 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 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 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 264
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 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 130
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 139
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="M -> V (in Ref. 2; BAA03980)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="R -> Q (in Ref. 2; BAA03980)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="E -> ESDE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="T -> I (in Ref. 2; BAA03980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 35172 MW; 692750F63B7CB5A5 CRC64;
MRIAVICFCL LGMAYALPVK HADSGSSEEK QLYHKHPDAL ATWLNPDPSQ KQNLLTPQNA
MSSEEKDDLK QETLPSKSIE SHDHMDDIDE DEDDDHVDNR DSNESDDADH PDDSHHSDES
HQSDESDEVT VYPTEDAATT VFTEVVPTVE TYDGRGDSVA YRLKRSKSKM FHVSNAQYPG
ASEEDLSSHV DSEDLDDTPR AIPVAQHLNV PSDWDSQEKD SHDVSQVDDH SVETQSHEQA
RQYKREANDN SVEHSHSIDS QESSKVSQES QSREFRSHED KLAIEPKSEE DEEHRQLRVS
HELDSTSSEI N
