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P10923

- OSTP_MOUSE

UniProt

P10923 - OSTP_MOUSE

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Protein
Osteopontin
Gene
Spp1, Eta-1, Op, Spp-1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications
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.2 Publications

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
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.

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: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Chaini17 – 294278Osteopontin
PRO_0000020322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine By similarity
Modified residuei26 – 261Phosphoserine By similarity
Modified residuei27 – 271Phosphoserine By similarity
Modified residuei61 – 611Phosphoserine By similarity
Modified residuei62 – 621Phosphoserine By similarity
Modified residuei75 – 751Phosphoserine By similarity
Modified residuei77 – 771Phosphoserine By similarity
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Modified residuei80 – 801Phosphoserine By similarity
Modified residuei106 – 1061Phosphoserine By similarity
Modified residuei109 – 1091Phosphoserine By similarity
Modified residuei112 – 1121Phosphoserine By similarity
Modified residuei115 – 1151Phosphoserine By similarity
Modified residuei118 – 1181Phosphoserine By similarity
Glycosylationi123 – 1231O-linked (GalNAc...) By similarity
Glycosylationi132 – 1321O-linked (GalNAc...) By similarity
Glycosylationi137 – 1371O-linked (GalNAc...) By similarity
Modified residuei170 – 1701Phosphothreonine By similarity
Modified residuei176 – 1761Phosphoserine By similarity
Modified residuei180 – 1801Phosphoserine By similarity
Modified residuei200 – 2001Phosphoserine By similarity
Modified residuei209 – 2091Phosphoserine By similarity
Modified residuei213 – 2131Phosphoserine By similarity
Modified residuei219 – 2191Phosphoserine By similarity
Modified residuei234 – 2341Phosphoserine By similarity
Modified residuei243 – 2431Phosphoserine By similarity
Modified residuei247 – 2471Phosphoserine By similarity
Modified residuei250 – 2501Phosphoserine By similarity
Modified residuei255 – 2551Phosphoserine By similarity
Modified residuei260 – 2601Phosphoserine By similarity
Modified residuei271 – 2711Phosphoserine By 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

PaxDbiP10923.
PRIDEiP10923.

PTM databases

PhosphoSiteiP10923.

Expressioni

Gene expression databases

ArrayExpressiP10923.
BgeeiP10923.
CleanExiMM_SPP1.
GenevestigatoriP10923.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Protein-protein interaction databases

BioGridi203467. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP10923.

Family & Domainsi

Motif

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

Sequence similaritiesi

Belongs to the osteopontin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73598.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
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

MRLAVICFCL FGIASSLPVK VTDSGSSEEK LYSLHPDPIA TWLVPDPSQK    50
QNLLAPQNAV SSEEKDDFKQ ETLPSNSNES HDHMDDDDDD DDDDGDHAES 100
EDSVDSDESD ESHHSDESDE TVTASTQADT FTPIVPTVDV PNGRGDSLAY 150
GLRSKSRSFQ VSDEQYPDAT DEDLTSHMKS GESKESLDVI PVAQLLSMPS 200
DQDNNGKGSH ESSQLDEPSL ETHRLEHSKE SQESADQSDV IDSQASSKAS 250
LEHQSHKFHS HKDKLVLDPK SKEDDRYLKF RISHELESSS SEVN 294
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431L → P in CAA34276. 1 Publication
Sequence conflicti99 – 991E → G in AAA57265. 1 Publication
Sequence conflicti100 – 1001S → N in AAH14284. 1 Publication
Sequence conflicti122 – 1221V → F in CAA32165. 1 Publication
Sequence conflicti122 – 1221V → F in AAH14284. 1 Publication
Sequence conflicti142 – 1421N → D in AAH14284. 1 Publication
Sequence conflicti171 – 1711D → Y in AAH14284. 1 Publication
Sequence conflicti188 – 1881D → N in AAH14284. 1 Publication
Sequence conflicti207 – 2071K → R in AAH14284. 1 Publication
Sequence conflicti224 – 2241R → S in AAH14284. 1 Publication
Sequence conflicti232 – 2321Q → H in AAH14284. 1 Publication
Sequence conflicti277 – 2771Y → H in AAH14284. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS19486.1.
PIRi A37818.
RefSeqi NP_001191162.1. NM_001204233.1.
NP_033289.2. NM_009263.3.
UniGenei Mm.288474.

3D structure databases

ProteinModelPortali P10923.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203467. 1 interaction.

PTM databases

PhosphoSitei P10923.

Proteomic databases

PaxDbi P10923.
PRIDEi P10923.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031243 ; ENSMUSP00000031243 ; ENSMUSG00000029304 .
ENSMUST00000112747 ; ENSMUSP00000108367 ; ENSMUSG00000029304 .
ENSMUST00000112748 ; ENSMUSP00000108368 ; ENSMUSG00000029304 .
GeneIDi 20750.
KEGGi mmu:20750.
UCSCi uc008yki.2. mouse.

Organism-specific databases

CTDi 6696.
MGIi MGI:98389. Spp1.

Phylogenomic databases

eggNOGi NOG73598.
HOGENOMi HOG000059656.
HOVERGENi HBG001731.
KOi K06250.
PhylomeDBi P10923.
TreeFami TF350201.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi SPP1. mouse.
NextBioi 299411.
PROi P10923.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10923.
Bgeei P10923.
CleanExi MM_SPP1.
Genevestigatori P10923.

Family and domain databases

InterProi IPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view ]
PANTHERi PTHR10607. PTHR10607. 1 hit.
Pfami PF00865. Osteopontin. 1 hit.
[Graphical view ]
PRINTSi PR00216. OSTEOPONTIN.
SMARTi SM00017. OSTEO. 1 hit.
[Graphical view ]
PROSITEi PS00884. OSTEOPONTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 140 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

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