Osteopontin precursor - Mus musculus (Mouse)

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P10923 (OSTP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Spp1
Synonyms:	Eta-1, Op, Spp-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Ref.7 Ref.8 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. Ref.7 Ref.8
Subunit structure	Ligand for integrin alpha-V/beta-3.
Subcellular location	Secreted.
Post-translational modification	Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif By similarity. N- and O-glycosylated.
Sequence similarities	Belongs to the osteopontin family.
Sequence caution	The sequence AAH14284.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Biomineralization Cell adhesion
Cellular component	Secreted
Domain	Signal
Ligand	Sialic acid
Molecular function	Cytokine
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	biomineral tissue development Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Non-traceable author statement PubMed 12183442. Source: UniProtKB neutrophil chemotaxis Inferred from direct assay PubMed 21321126. Source: MGI ossification Inferred from electronic annotation. Source: InterPro positive regulation of cell-substrate adhesion Inferred from direct assay PubMed 18757743. Source: MGI
Cellular_component	apical part of cell Inferred from direct assay PubMed 16518820. Source: MGI cytoplasm Inferred from direct assay PubMed 16518820. Source: MGI extracellular region Non-traceable author statement PubMed 11264474. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine activity Non-traceable author statement PubMed 11264474. Source: UniProtKB extracellular matrix binding Inferred from direct assay PubMed 18757743. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Potential

Chain

17 – 294

278

Osteopontin

PRO_0000020322

Regions

Motif

144 – 146

Cell attachment site

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

106

Phosphoserine By similarity

Modified residue

109

Phosphoserine By similarity

Modified residue

112

Phosphoserine By similarity

Modified residue

115

Phosphoserine By similarity

Modified residue

118

Phosphoserine By similarity

Modified residue

170

Phosphothreonine By similarity

Modified residue

176

Phosphoserine By similarity

Modified residue

180

Phosphoserine By similarity

Modified residue

200

Phosphoserine By similarity

Modified residue

209

Phosphoserine By similarity

Modified residue

213

Phosphoserine By similarity

Modified residue

219

Phosphoserine By similarity

Modified residue

231

Phosphoserine Ref.11

Modified residue

234

Phosphoserine Ref.11

Modified residue

243

Phosphoserine By similarity

Modified residue

247

Phosphoserine By similarity

Modified residue

250

Phosphoserine By similarity

Modified residue

255

Phosphoserine By similarity

Modified residue

260

Phosphoserine By similarity

Modified residue

283

Phosphoserine Ref.9 Ref.10

Modified residue

288

Phosphoserine Ref.9

Modified residue

290

Phosphoserine Ref.9

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

123

O-linked (GalNAc...) By similarity

Glycosylation

132

O-linked (GalNAc...) By similarity

Glycosylation

137

O-linked (GalNAc...) By similarity

Experimental info

Sequence conflict

L → P in CAA34276. Ref.2

Sequence conflict

E → G in AAA57265. Ref.1

Sequence conflict

100

S → N in AAH14284. Ref.5

Sequence conflict

122

V → F in CAA32165. Ref.3

Sequence conflict

122

V → F in AAH14284. Ref.5

Sequence conflict

142

N → D in AAH14284. Ref.5

Sequence conflict

171

D → Y in AAH14284. Ref.5

Sequence conflict

188

D → N in AAH14284. Ref.5

Sequence conflict

207

K → R in AAH14284. Ref.5

Sequence conflict

224

R → S in AAH14284. Ref.5

Sequence conflict

232

Q → H in AAH14284. Ref.5

Sequence conflict

277

Y → H in AAH14284. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P10923 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 9D5F32D67ABC53EA
Show »

FASTA

294

32,459

        10         20         30         40         50         60 
MRLAVICFCL FGIASSLPVK VTDSGSSEEK LYSLHPDPIA TWLVPDPSQK QNLLAPQNAV 

        70         80         90        100        110        120 
SSEEKDDFKQ ETLPSNSNES HDHMDDDDDD DDDDGDHAES EDSVDSDESD ESHHSDESDE 

       130        140        150        160        170        180 
TVTASTQADT FTPIVPTVDV PNGRGDSLAY GLRSKSRSFQ VSDEQYPDAT DEDLTSHMKS 

       190        200        210        220        230        240 
GESKESLDVI PVAQLLSMPS DQDNNGKGSH ESSQLDEPSL ETHRLEHSKE SQESADQSDV 

       250        260        270        280        290 
IDSQASSKAS LEHQSHKFHS HKDKLVLDPK SKEDDRYLKF RISHELESSS SEVN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity." Ashkar S., Weber G.F., Panoutsakopoulou V., Sanchirico M.E., Jansson M., Zawaideh S., Rittling S.R., Denhardt D.T., Glimcher M.J., Cantor H. Science 287:860-864(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-288 AND SER-290, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-27; SER-61; SER-62 AND SER-283, MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"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-231 AND SER-234, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00309133.
PIR	A37818.
RefSeq	NP_001191162.1. NM_001204233.1. NP_033289.2. NM_009263.3.
UniGene	Mm.288474.
3D structure databases
ProteinModelPortal	P10923.
ModBase	Search...
PTM databases
PhosphoSite	P10923.
Proteomic databases
PaxDb	P10923.
PRIDE	P10923.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031243; ENSMUSP00000031243; ENSMUSG00000029304. ENSMUST00000112747; ENSMUSP00000108367; ENSMUSG00000029304. ENSMUST00000112748; ENSMUSP00000108368; ENSMUSG00000029304.
GeneID	20750.
KEGG	mmu:20750.
Organism-specific databases
CTD	6696.
MGI	MGI:98389. Spp1.
Phylogenomic databases
eggNOG	NOG73598.
HOGENOM	HOG000059656.
HOVERGEN	HBG001731.
KO	K06250.
OrthoDB	EOG408N8S.
Gene expression databases
ArrayExpress	P10923.
Bgee	P10923.
CleanEx	MM_SPP1.
Genevestigator	P10923.
GermOnline	ENSMUSG00000029304. Mus musculus.
Family and domain databases
InterPro	IPR002038. Osteopontin. IPR019841. Osteopontin_CS. [Graphical view]
PANTHER	PTHR10607. PTHR10607. 1 hit.
Pfam	PF00865. Osteopontin. 1 hit. [Graphical view]
PRINTS	PR00216. OSTEOPONTIN.
SMART	SM00017. OSTEO. 1 hit. [Graphical view]
PROSITE	PS00884. OSTEOPONTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SPP1. mouse.
NextBio	299411.
SOURCE	Search...

Entry information

Entry name

OSTP_MOUSE

Accession

Primary (citable) accession number: P10923
Secondary accession number(s): P19008, Q91VH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents