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Protein

Osteopontin

Gene

Spp1

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

  1. cytokine activity Source: UniProtKB
  2. extracellular matrix binding Source: MGI

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. negative regulation of apoptotic process Source: UniProtKB
  4. neutrophil chemotaxis Source: MGI
  5. ossification Source: InterPro
  6. positive regulation of cell-substrate adhesion Source: MGI
  7. response to vitamin D Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Biomineralization, Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_216309. Integrin cell surface interactions.
REACT_263353. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Osteopontin
Alternative name(s):
2AR
Bone sialoprotein 1
Calcium oxalate crystal growth inhibitor protein
Early T-lymphocyte activation 1 protein
Minopontin
Secreted phosphoprotein 1
Short name:
SPP-1
Gene namesi
Name:Spp1
Synonyms:Eta-1, Op, Spp-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:98389. Spp1.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: MGI
  2. cytoplasm Source: MGI
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: MGI
  5. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 294278OsteopontinPRO_0000020322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei27 – 271PhosphoserineBy similarity
Modified residuei61 – 611PhosphoserineBy similarity
Modified residuei62 – 621PhosphoserineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Modified residuei80 – 801PhosphoserineBy 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 residuei176 – 1761PhosphoserineBy similarity
Modified residuei180 – 1801PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei219 – 2191PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity
Modified residuei255 – 2551PhosphoserineBy similarity
Modified residuei260 – 2601PhosphoserineBy similarity
Modified residuei271 – 2711PhosphoserineBy similarity
Modified residuei283 – 2831Phosphoserine2 Publications
Modified residuei288 – 2881Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine2 Publications

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.

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP10923.
PaxDbiP10923.
PRIDEiP10923.

PTM databases

PhosphoSiteiP10923.

Expressioni

Gene expression databases

BgeeiP10923.
CleanExiMM_SPP1.
ExpressionAtlasiP10923. baseline and differential.
GenevestigatoriP10923.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Protein-protein interaction databases

BioGridi203467. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP10923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the osteopontin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73598.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
InParanoidiP10923.
KOiK06250.
PhylomeDBiP10923.
TreeFamiTF350201.

Family and domain databases

InterProiIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERiPTHR10607. PTHR10607. 1 hit.
PfamiPF00865. Osteopontin. 1 hit.
[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.

P10923-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLAVICFCL FGIASSLPVK VTDSGSSEEK LYSLHPDPIA TWLVPDPSQK
60 70 80 90 100
QNLLAPQNAV SSEEKDDFKQ ETLPSNSNES HDHMDDDDDD DDDDGDHAES
110 120 130 140 150
EDSVDSDESD ESHHSDESDE TVTASTQADT FTPIVPTVDV PNGRGDSLAY
160 170 180 190 200
GLRSKSRSFQ VSDEQYPDAT DEDLTSHMKS GESKESLDVI PVAQLLSMPS
210 220 230 240 250
DQDNNGKGSH ESSQLDEPSL ETHRLEHSKE SQESADQSDV IDSQASSKAS
260 270 280 290
LEHQSHKFHS HKDKLVLDPK SKEDDRYLKF RISHELESSS SEVN
Length:294
Mass (Da):32,459
Last modified:July 1, 1989 - v1
Checksum:i9D5F32D67ABC53EA
GO

Sequence cautioni

The sequence AAH14284.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431L → P in CAA34276 (PubMed:2787378).Curated
Sequence conflicti99 – 991E → G in AAA57265 (PubMed:2722855).Curated
Sequence conflicti100 – 1001S → N in AAH14284 (PubMed:15489334).Curated
Sequence conflicti122 – 1221V → F in CAA32165 (PubMed:2726465).Curated
Sequence conflicti122 – 1221V → F in AAH14284 (PubMed:15489334).Curated
Sequence conflicti142 – 1421N → D in AAH14284 (PubMed:15489334).Curated
Sequence conflicti171 – 1711D → Y in AAH14284 (PubMed:15489334).Curated
Sequence conflicti188 – 1881D → N in AAH14284 (PubMed:15489334).Curated
Sequence conflicti207 – 2071K → R in AAH14284 (PubMed:15489334).Curated
Sequence conflicti224 – 2241R → S in AAH14284 (PubMed:15489334).Curated
Sequence conflicti232 – 2321Q → H in AAH14284 (PubMed:15489334).Curated
Sequence conflicti277 – 2771Y → H in AAH14284 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04806 mRNA. Translation: AAA57265.1.
X16151 mRNA. Translation: CAA34276.1.
X13986 mRNA. Translation: CAA32165.1.
X51834 Genomic DNA. Translation: CAA36132.1.
BC014284 mRNA. Translation: AAH14284.1. Different initiation.
BC057858 mRNA. Translation: AAH57858.1.
CCDSiCCDS19486.1.
PIRiA37818.
RefSeqiNP_001191162.1. NM_001204233.1.
NP_033289.2. NM_009263.3.
UniGeneiMm.288474.

Genome annotation databases

EnsembliENSMUST00000031243; ENSMUSP00000031243; ENSMUSG00000029304.
ENSMUST00000112747; ENSMUSP00000108367; ENSMUSG00000029304.
ENSMUST00000112748; ENSMUSP00000108368; ENSMUSG00000029304.
GeneIDi20750.
KEGGimmu:20750.
UCSCiuc008yki.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04806 mRNA. Translation: AAA57265.1.
X16151 mRNA. Translation: CAA34276.1.
X13986 mRNA. Translation: CAA32165.1.
X51834 Genomic DNA. Translation: CAA36132.1.
BC014284 mRNA. Translation: AAH14284.1. Different initiation.
BC057858 mRNA. Translation: AAH57858.1.
CCDSiCCDS19486.1.
PIRiA37818.
RefSeqiNP_001191162.1. NM_001204233.1.
NP_033289.2. NM_009263.3.
UniGeneiMm.288474.

3D structure databases

ProteinModelPortaliP10923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203467. 1 interaction.

PTM databases

PhosphoSiteiP10923.

Proteomic databases

MaxQBiP10923.
PaxDbiP10923.
PRIDEiP10923.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031243; ENSMUSP00000031243; ENSMUSG00000029304.
ENSMUST00000112747; ENSMUSP00000108367; ENSMUSG00000029304.
ENSMUST00000112748; ENSMUSP00000108368; ENSMUSG00000029304.
GeneIDi20750.
KEGGimmu:20750.
UCSCiuc008yki.2. mouse.

Organism-specific databases

CTDi6696.
MGIiMGI:98389. Spp1.

Phylogenomic databases

eggNOGiNOG73598.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
InParanoidiP10923.
KOiK06250.
PhylomeDBiP10923.
TreeFamiTF350201.

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_216309. Integrin cell surface interactions.
REACT_263353. Signaling by PDGF.

Miscellaneous databases

ChiTaRSiSpp1. mouse.
NextBioi299411.
PROiP10923.
SOURCEiSearch...

Gene expression databases

BgeeiP10923.
CleanExiMM_SPP1.
ExpressionAtlasiP10923. baseline and differential.
GenevestigatoriP10923.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Osteopontin, a transformation-associated cell adhesion phosphoprotein, is induced by 12-O-tetradecanoylphorbol 13-acetate in mouse epidermis."
    Craig A.M., Smith J.H., Denhardt D.T.
    J. Biol. Chem. 264:9682-9689(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene. Definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection."
    Patarca R., Freeman G.J., Singh R.P., Wei F.-Y., Durfee T., Blattner F., Regnier D.C., Kozak C.A., Mock B.A., Morse H.C. III, Jerrells T.R., Cantor H.
    J. Exp. Med. 170:145-161(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Nucleotide sequence of cDNA for mouse osteopontin-like protein."
    Miyazaki Y., Setoguchi M., Yoshida S., Higuchi Y., Akizuki S., Yamamoto S.
    Nucleic Acids Res. 17:3298-3298(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  4. "The mouse osteopontin gene. Expression in monocytic lineages and complete nucleotide sequence."
    Miyazaki Y., Setoguchi M., Yoshida S.Y., Akizuki S., Yamamoto S.
    J. Biol. Chem. 265:14432-14438(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
    Tissue: Liver.
  5. "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].
    Strain: NMRI.
    Tissue: Mammary gland.
  6. "The calcium oxalate crystal growth inhibitor protein produced by mouse kidney cortical cells in culture is osteopontin."
    Worcester E.M., Blumenthal S.S., Beshensky A.M., Lewand D.L.
    J. Bone Miner. Res. 7:1029-1036(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-37.
    Tissue: Kidney.
  7. "Definition of a specific interaction between the early T lymphocyte activation 1 (Eta-1) protein and murine macrophages in vitro and its effect upon macrophages in vivo."
    Singh R.P., Patarca R., Schwartz J., Singh P., Cantor H.
    J. Exp. Med. 171:1931-1942(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 158-176, FUNCTION.
  8. Cited for: FUNCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-288 AND SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiOSTP_MOUSE
AccessioniPrimary (citable) accession number: P10923
Secondary accession number(s): P19008, Q91VH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 4, 2015
This is version 146 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.