Osteopontin precursor - Rattus norvegicus (Rat)

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P08721 (OSTP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

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

Documents (1) |

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):
Bone sialoprotein 1
Secreted phosphoprotein 1
Short name=SPP-1

Gene names

Name:	Spp1
Synonyms:	2b7, Spp-1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	317 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. 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.
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.

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 direct assay PubMed 11792563. Source: RGD inflammatory response Inferred from expression pattern PubMed 16679731. Source: RGD negative regulation of collateral sprouting of intact axon in response to injury Inferred from expression pattern PubMed 15625076. Source: RGD neutrophil chemotaxis Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from mutant phenotype PubMed 15598896. Source: RGD positive regulation of bone resorption Inferred from direct assay PubMed 11792563. Source: RGD positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from direct assay PubMed 11250650. Source: RGD response to vitamin D Inferred from electronic annotation. Source: Compara
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara cell projection Inferred from direct assay PubMed 12162503. Source: RGD extracellular space Inferred from direct assay PubMed 18758911. Source: RGD membrane-bounded vesicle Inferred from direct assay PubMed 18758911. Source: RGD perinuclear region of cytoplasm Inferred from direct assay PubMed 12162503. Source: RGD
Molecular_function	extracellular matrix binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Ref.5 Ref.6 Ref.7

Chain

17 – 317

301

Osteopontin

PRO_0000020325

Regions

Motif

144 – 146

Cell attachment site

Compositional bias

86 – 96

Poly-Asp

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

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

204

Phosphoserine By similarity

Modified residue

209

Phosphoserine By similarity

Modified residue

213

Phosphoserine By similarity

Modified residue

219

Phosphoserine By similarity

Modified residue

224

Phosphoserine By similarity

Modified residue

257

Phosphoserine By similarity

Modified residue

266

Phosphoserine By similarity

Modified residue

270

Phosphoserine By similarity

Modified residue

273

Phosphoserine By similarity

Modified residue

278

Phosphoserine By similarity

Modified residue

283

Phosphoserine By similarity

Modified residue

306

Phosphoserine By similarity

Modified residue

311

Phosphoserine By similarity

Modified residue

313

Phosphoserine By similarity

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

F → L in AAA41762. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P08721 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 73CB5C21FFF62310
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FASTA

317

34,963

        10         20         30         40         50         60 
MRLAVVCFCL FGLASCLPVK VAEFGSSEEK AHYSKHSDAV ATWLKPDPSQ KQNLLAPQNS 

        70         80         90        100        110        120 
VSSEETDDFK QETLPSNSNE SHDHMDDDDD DDDDGDHAES EDSVNSDESD ESHHSDESDE 

       130        140        150        160        170        180 
SFTASTQADV LTPIAPTVDV PDGRGDSLAY GLRSKSRSFP VSDEQYPDAT DEDLTSRMKS 

       190        200        210        220        230        240 
QESDEAIKVI PVAQRLSVPS DQDSNGKTSH ESSQLDEPSV ETHSLEQSKE YKQRASHEST 

       250        260        270        280        290        300 
EQSDAIDSAE KPDAIDSAER SDAIDSQASS KASLEHQSHE FHSHEDKLVL DPKSKEDDRY 

       310 
LKFRISHELE SSSSEVN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M99252 mRNA. Translation: AAA41765.1. M14656 mRNA. Translation: AAA41762.1. BC078874 mRNA. Translation: AAH78874.1.
IPI	IPI00327895.
PIR	A25917. JC5811.
RefSeq	NP_037013.2. NM_012881.2.
UniGene	Rn.8871.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000062358.
PTM databases
PhosphoSite	P08721.
Proteomic databases
PaxDb	P08721.
PRIDE	P08721.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000067875; ENSRNOP00000062358; ENSRNOG00000043451.
GeneID	25353.
KEGG	rno:25353.
Organism-specific databases
CTD	6696.
RGD	3752. Spp1.
Phylogenomic databases
eggNOG	NOG73598.
GeneTree	ENSGT00390000002509.
HOGENOM	HOG000059656.
HOVERGEN	HBG001731.
KO	K06250.
OrthoDB	EOG408N8S.
Gene expression databases
ArrayExpress	P08721.
Genevestigator	P08721.
Family and domain databases
InterPro	IPR002038. Osteopontin. IPR019841. Osteopontin_CS. [Graphical view]
PANTHER	PTHR10607. PTHR10607. 1 hit.
Pfam	PF00865. Osteopontin. 2 hits. [Graphical view]
PRINTS	PR00216. OSTEOPONTIN.
SMART	SM00017. OSTEO. 1 hit. [Graphical view]
PROSITE	PS00884. OSTEOPONTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	606305.

Entry information

Entry name

OSTP_RAT

Accession

Primary (citable) accession number: P08721

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Protein-protein interaction 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