OSTP_CHICK
ID OSTP_CHICK Reviewed; 264 AA.
AC P23498;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 112.
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;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2033080; DOI=10.1016/s0021-9258(18)92910-8;
RA Castagnola P., Bet P., Quarto R., Gennari M., Migliaccio G., Cancedda R.;
RT "cDNA cloning and gene expression of chicken osteopontin. Expression of
RT osteopontin mRNA in chondrocytes is enhanced by trypsin treatment of
RT cells.";
RL J. Biol. Chem. 266:9944-9949(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2001376; DOI=10.1021/bi00223a029;
RA Moore M.A., Gotoh Y., Rafidi K., Gerstenfeld L.C.;
RT "Characterization of a cDNA for chicken osteopontin: expression during bone
RT development, osteoblast differentiation, and tissue distribution.";
RL Biochemistry 30:2501-2508(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8144023; DOI=10.1016/0378-1119(94)90540-1;
RA Rafidi K., Simikina I., Johnson E., Moore M.A., Gerstenfeld L.C.;
RT "Characterization of the chicken osteopontin-encoding gene.";
RL Gene 140:163-169(1994).
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 on serine residues.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
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DR EMBL; X56772; CAA40091.1; -; mRNA.
DR EMBL; M59182; AAA62729.1; -; mRNA.
DR EMBL; U01844; AAA18584.1; -; Genomic_DNA.
DR PIR; I51384; A40019.
DR RefSeq; NP_989866.1; NM_204535.4.
DR AlphaFoldDB; P23498; -.
DR STRING; 9031.ENSGALP00000017754; -.
DR PaxDb; P23498; -.
DR GeneID; 395210; -.
DR KEGG; gga:395210; -.
DR CTD; 6696; -.
DR VEuPathDB; HostDB:geneid_395210; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR InParanoid; P23498; -.
DR OrthoDB; 1280650at2759; -.
DR PhylomeDB; P23498; -.
DR PRO; PR:P23498; -.
DR Proteomes; UP000000539; Unplaced.
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:0008201; F:heparin binding; ISS:AgBase.
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; 1.
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 CHAIN 17..264
FT /note="Osteopontin"
FT /id="PRO_0000020327"
FT REGION 21..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..134
FT /note="Cell attachment site"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..119
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 104
FT /note="D -> G (in Ref. 2; AAA62729)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="G -> D (in Ref. 1; CAA40091)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="R -> A (in Ref. 1; CAA40091)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="T -> A (in Ref. 1; CAA40091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29162 MW; CA2F17DB70A92591 CRC64;
MKLAFLCLCF ISIAAAWPVS KSRQHAISAS SEEKYDPRSH HTHRYHQDHV DSQSQEHLQQ
TQNDLASLQQ THYSSEENAD VPEQPDFPDI PSKSQEAVDD DDDDDNDSND TDESDEVVTD
FPTEAPVTPF NRGDNAGRGD SVAYGFRAKA HVVKASKLRK AARKLIEDDA TAEVGDSQLA
GLWLPKESRE QDSRELAQHQ SVENDSRPRF DSPEVGGGDS KASAGVDSRE SLASRSAVDT
SNQTLESAED AEDRHSIENN EVTR
