Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Osteopontin

Gene

Spp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
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.By similarity

GO - Molecular functioni

GO - Biological processi

  • biomineral tissue development Source: UniProtKB-KW
  • cell adhesion Source: RGD
  • cell differentiation Source: RGD
  • inflammatory response Source: RGD
  • negative regulation of collateral sprouting of intact axon in response to injury Source: RGD
  • osteoblast differentiation Source: RGD
  • positive regulation of bone resorption Source: RGD
  • response to organic substance Source: RGD
  • response to steroid hormone Source: RGD
  • response to vitamin D Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Biomineralization, Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-186797. Signaling by PDGF.
R-RNO-216083. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Osteopontin
Alternative name(s):
Bone sialoprotein 1
Secreted phosphoprotein 1
Short name:
SPP-1
Gene namesi
Name:Spp1
Synonyms:2b7, Spp-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3752. Spp1.

Subcellular locationi

GO - Cellular componenti

  • cell projection Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • membrane-bounded vesicle Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16163 PublicationsAdd
BLAST
Chaini17 – 317301OsteopontinPRO_0000020325Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei60 – 601PhosphoserineBy similarity
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei63 – 631PhosphoserineCombined sources
Modified residuei66 – 661PhosphothreonineBy similarity
Modified residuei76 – 761PhosphoserineBy similarity
Modified residuei78 – 781PhosphoserineBy similarity
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence analysis
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei112 – 1121PhosphoserineBy similarity
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Glycosylationi123 – 1231O-linked (GalNAc...)By similarity
Glycosylationi132 – 1321O-linked (GalNAc...)By similarity
Glycosylationi137 – 1371O-linked (GalNAc...)By similarity
Modified residuei170 – 1701PhosphothreonineBy similarity
Modified residuei175 – 1751PhosphothreonineBy similarity
Modified residuei176 – 1761PhosphoserineBy similarity
Modified residuei180 – 1801PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei222 – 2221PhosphothreonineBy similarity
Modified residuei224 – 2241PhosphoserineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Modified residuei257 – 2571PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei266 – 2661PhosphoserineBy similarity
Modified residuei270 – 2701PhosphoserineBy similarity
Modified residuei273 – 2731PhosphoserineBy similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Modified residuei283 – 2831PhosphoserineBy similarity
Modified residuei294 – 2941PhosphoserineBy similarity
Modified residuei306 – 3061PhosphoserineBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei314 – 3141PhosphoserineBy similarity

Post-translational modificationi

Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif.By similarity
N- and O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP08721.
PRIDEiP08721.

PTM databases

iPTMnetiP08721.
PhosphoSiteiP08721.

Expressioni

Gene expression databases

GenevisibleiP08721. RN.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Protein-protein interaction databases

BioGridi247392. 4 interactions.
IntActiP08721. 2 interactions.
MINTiMINT-8283233.
STRINGi10116.ENSRNOP00000062358.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi144 – 1463Cell attachment site

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi86 – 9611Poly-AspAdd
BLAST

Sequence similaritiesi

Belongs to the osteopontin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IVP1. Eukaryota.
ENOG41116B5. LUCA.
GeneTreeiENSGT00390000002509.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
InParanoidiP08721.
KOiK06250.
OMAiVICFCLL.
OrthoDBiEOG7R832D.
PhylomeDBiP08721.

Family and domain databases

InterProiIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERiPTHR10607. PTHR10607. 1 hit.
PfamiPF00865. Osteopontin. 2 hits.
[Graphical view]
PRINTSiPR00216. OSTEOPONTIN.
SMARTiSM00017. OSTEO. 1 hit.
[Graphical view]
PROSITEiPS00884. OSTEOPONTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLAVVCFCL FGLASCLPVK VAEFGSSEEK AHYSKHSDAV ATWLKPDPSQ
60 70 80 90 100
KQNLLAPQNS VSSEETDDFK QETLPSNSNE SHDHMDDDDD DDDDGDHAES
110 120 130 140 150
EDSVNSDESD ESHHSDESDE SFTASTQADV LTPIAPTVDV PDGRGDSLAY
160 170 180 190 200
GLRSKSRSFP VSDEQYPDAT DEDLTSRMKS QESDEAIKVI PVAQRLSVPS
210 220 230 240 250
DQDSNGKTSH ESSQLDEPSV ETHSLEQSKE YKQRASHEST EQSDAIDSAE
260 270 280 290 300
KPDAIDSAER SDAIDSQASS KASLEHQSHE FHSHEDKLVL DPKSKEDDRY
310
LKFRISHELE SSSSEVN
Length:317
Mass (Da):34,963
Last modified:April 1, 1993 - v2
Checksum:i73CB5C21FFF62310
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81F → L in AAA41762 (PubMed:3024151).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99252 mRNA. Translation: AAA41765.1.
M14656 mRNA. Translation: AAA41762.1.
BC078874 mRNA. Translation: AAH78874.1.
PIRiA25917.
JC5811.
RefSeqiNP_037013.2. NM_012881.2.
XP_008768218.1. XM_008769996.1.
UniGeneiRn.8871.

Genome annotation databases

EnsembliENSRNOT00000067875; ENSRNOP00000062358; ENSRNOG00000043451.
ENSRNOT00000075989; ENSRNOP00000068511; ENSRNOG00000043451.
GeneIDi25353.
KEGGirno:25353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99252 mRNA. Translation: AAA41765.1.
M14656 mRNA. Translation: AAA41762.1.
BC078874 mRNA. Translation: AAH78874.1.
PIRiA25917.
JC5811.
RefSeqiNP_037013.2. NM_012881.2.
XP_008768218.1. XM_008769996.1.
UniGeneiRn.8871.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247392. 4 interactions.
IntActiP08721. 2 interactions.
MINTiMINT-8283233.
STRINGi10116.ENSRNOP00000062358.

PTM databases

iPTMnetiP08721.
PhosphoSiteiP08721.

Proteomic databases

PaxDbiP08721.
PRIDEiP08721.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000067875; ENSRNOP00000062358; ENSRNOG00000043451.
ENSRNOT00000075989; ENSRNOP00000068511; ENSRNOG00000043451.
GeneIDi25353.
KEGGirno:25353.

Organism-specific databases

CTDi6696.
RGDi3752. Spp1.

Phylogenomic databases

eggNOGiENOG410IVP1. Eukaryota.
ENOG41116B5. LUCA.
GeneTreeiENSGT00390000002509.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
InParanoidiP08721.
KOiK06250.
OMAiVICFCLL.
OrthoDBiEOG7R832D.
PhylomeDBiP08721.

Enzyme and pathway databases

ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-186797. Signaling by PDGF.
R-RNO-216083. Integrin cell surface interactions.

Miscellaneous databases

PROiP08721.

Gene expression databases

GenevisibleiP08721. RN.

Family and domain databases

InterProiIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERiPTHR10607. PTHR10607. 1 hit.
PfamiPF00865. Osteopontin. 2 hits.
[Graphical view]
PRINTSiPR00216. OSTEOPONTIN.
SMARTiSM00017. OSTEO. 1 hit.
[Graphical view]
PROSITEiPS00884. OSTEOPONTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential processing of osteopontin transcripts in rat kidney- and osteoblast-derived cell lines."
    Singh K., Mukherjee A.B., de Vouge M.W., Mukherjee B.B.
    J. Biol. Chem. 267:23847-23851(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence."
    Oldberg A., Franzen A., Heinegaard D.
    Proc. Natl. Acad. Sci. U.S.A. 83:8819-8823(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Osteopontin is elevated during neointima formation in rat arteries and is a novel component of human atherosclerotic plaques."
    Giachelli C.M., Bae N., Almeida M., Denhardt D.T., Alpers C.E., Schwartz S.M.
    J. Clin. Invest. 92:1686-1696(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Smooth muscle.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  5. "Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin."
    Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.
    Biochim. Biophys. Acta 996:43-48(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-25 AND 154-167.
  6. "Isolation, characterization, and biosynthesis of a phosphorylated glycoprotein from rat bone."
    Prince C.W., Oosawa T., Butler W.T., Tomana M., Bhown A.S., Bhown M., Schrohenloher R.E.
    J. Biol. Chem. 262:2900-2907(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-27.
    Tissue: Bone.
  7. "Secreted phosphoproteins associated with neoplastic transformation: close homology with plasma proteins cleaved during blood coagulation."
    Senger D.R., Perruzzi C.A., Gracey C.F., Papadopoulos A., Tenen D.G.
    Cancer Res. 48:5770-5774(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-25.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiOSTP_RAT
AccessioniPrimary (citable) accession number: P08721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1993
Last modified: July 6, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.