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P09486 (SPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SPARC
Alternative name(s):
Basement-membrane protein 40
Short name=BM-40
Osteonectin
Short name=ON
Secreted protein acidic and rich in cysteine
Gene names
Name:SPARC
Synonyms:ON
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca2+ with a low affinity and an EF-hand loop that binds a Ca2+ ion with a high affinity.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: In or around the basement membrane. Ref.10 Ref.11 Ref.12 Ref.13

Developmental stage

Expressed at high levels in tissues undergoing morphogenesis, remodeling and wound repair.

Sequence similarities

Belongs to the SPARC family.

Contains 1 EF-hand domain.

Contains 1 follistatin-like domain.

Contains 1 Kazal-like domain.

Sequence caution

The sequence AAA60993.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Ontologies

Keywords
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Copper
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

bone development

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

inner ear development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

ossification

Traceable author statement PubMed 7034958. Source: ProtInc

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to L-ascorbic acid

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to gravity

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endocytic vesicle lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

platelet alpha granule lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Traceable author statement PubMed 7034958. Source: ProtInc

   Molecular_functioncalcium ion binding

Traceable author statement PubMed 7034958. Source: ProtInc

collagen binding

Traceable author statement PubMed 7034958. Source: ProtInc

extracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 18808384. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fafQ2TV774EBI-2800983,EBI-6405263From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.9 Ref.10
Chain18 – 303286SPARC
PRO_0000020304

Regions

Domain71 – 9323Follistatin-like
Domain89 – 15163Kazal-like
Domain261 – 29636EF-hand
Calcium binding274 – 28512
Compositional bias22 – 6948Asp/Glu-rich (acidic; binds calcium)

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...) Ref.15 Ref.16
Disulfide bond72 ↔ 83 Ref.15
Disulfide bond77 ↔ 93 Ref.15
Disulfide bond95 ↔ 130 Ref.15
Disulfide bond101 ↔ 123 Ref.15
Disulfide bond112 ↔ 149 Ref.15
Disulfide bond155 ↔ 265 Ref.15
Disulfide bond273 ↔ 289 Ref.15

Natural variations

Natural variant191P → S.
Corresponds to variant rs6874468 [ dbSNP | Ensembl ].
VAR_050431
Natural variant701N → S.
Corresponds to variant rs13359508 [ dbSNP | Ensembl ].
VAR_059530

Experimental info

Mutagenesis1661R → A, L or K: Strongly reduced collagen binding. Ref.16
Mutagenesis1731N → A or Q: Strongly reduced collagen binding. Ref.16
Mutagenesis2591L → A: Loss of collagen binding. Ref.16
Mutagenesis2621M → A: Strongly reduced collagen binding. Ref.16
Mutagenesis2631E → A: Loss of collagen binding. Ref.16
Sequence conflict42 – 432SV → PT AA sequence Ref.9
Sequence conflict2051R → L in AAA60993. Ref.3
Sequence conflict2691F → L in AAA60993. Ref.3

Secondary structure

................................................. 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09486 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: B914599F79705945

FASTA30334,632
        10         20         30         40         50         60 
MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV EVGEFDDGAE 

        70         80         90        100        110        120 
ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS CPAPIGEFEK VCSNDNKTFD 

       130        140        150        160        170        180 
SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE 

       190        200        210        220        230        240 
RDEDNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ 

       250        260        270        280        290        300 
HPIDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD 


LVI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and complete amino acid sequences of human and murine basement membrane protein BM-40 (SPARC, osteonectin)."
Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., Krieg T.
FEBS Lett. 236:352-356(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Placenta.
[2]"Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40: sequence, expression, and localization of the gene to chromosome 5q31-q33."
Swaroop A., Hogan B.L.M., Francke U.
Genomics 2:37-47(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of human osteonectin based upon analysis of cDNA and genomic sequences."
Villarreal X.C., Mann K.G., Long G.L.
Biochemistry 28:6483-6491(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure and expression of osteonectin mRNA in human tissue."
Young M.F., Day A.A., Dominquez P., McQuillan C.I., Fisher L.W., Termine J.D.
Connect. Tissue Res. 24:17-28(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Muscle, PNS and Skin.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
[9]"Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-53, CHARACTERIZATION.
[10]"Human platelet osteonectin: release, surface expression, and partial characterization."
Kelm R.J. Jr., Mann K.G.
Blood 75:1105-1113(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-41, CHARACTERIZATION, SUBCELLULAR LOCATION.
[11]"Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues characterized by de novo formation of basement membrane."
Wewer U.M., Albrechtsen R., Fisher L.W., Young M.F., Termine J.D.
Am. J. Pathol. 132:345-355(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Immunolocalization of SPARC, tenascin, and thrombospondin in pulmonary fibrosis."
Kuhn C., Mason R.J.
Am. J. Pathol. 147:1759-1769(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"BM-40 (osteonectin, SPARC) is expressed both in the epidermal and in the dermal compartment of adult human skin."
Hunzelmann N., Hafner M., Anders S., Krieg T., Nischt R.
J. Invest. Dermatol. 110:122-126(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Structure of a novel extracellular Ca(2+)-binding module in BM-40."
Hohenester E., Maurer P., Hahoenadl C., Timpl R., Jansonius J.N., Engel J.
Nat. Struct. Biol. 3:67-73(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-303.
[15]"Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40."
Hohenester E., Maurer P., Timpl R.
EMBO J. 16:3778-3786(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-116, DISULFIDE BONDS.
[16]"Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin."
Sasaki T., Hohenester E., Gohring W., Timpl R.
EMBO J. 17:1625-1634(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 71-303 IN COMPLEX WITH CALCIUM IONS, GLYCOSYLATION AT ASN-116, INTERACTION WITH COLLAGEN, MUTAGENESIS OF ARG-166; ASN-173; LEU-259; MET-262 AND GLU-263.
+Additional computationally mapped references.

Web resources

Wikipedia

Osteonectin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00755 mRNA. Translation: CAA68724.1.
J03040 mRNA. Translation: AAA60570.1.
M25746 expand/collapse EMBL AC list , M25738, M25739, M25740, M25741, M25742, M25743, M25744, M25745 Genomic DNA. Translation: AAA60993.1. Sequence problems.
CR456799 mRNA. Translation: CAG33080.1.
CH471062 Genomic DNA. Translation: EAW61668.1.
CH471062 Genomic DNA. Translation: EAW61669.1.
CH471062 Genomic DNA. Translation: EAW61670.1.
CH471062 Genomic DNA. Translation: EAW61672.1.
BC004974 mRNA. Translation: AAH04974.1.
BC008011 mRNA. Translation: AAH08011.1.
BC072457 mRNA. Translation: AAH72457.1.
AL709729 mRNA. No translation available.
CCDSCCDS4318.1.
PIRGEHUN. A32821.
RefSeqNP_003109.1. NM_003118.3.
UniGeneHs.111779.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMOX-ray3.10A/B71-303[»]
1NUBX-ray2.80A/B71-303[»]
1SRAX-ray2.00A153-303[»]
2V53X-ray3.20A70-303[»]
ProteinModelPortalP09486.
SMRP09486. Positions 71-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112560. 9 interactions.
DIPDIP-46426N.
IntActP09486. 4 interactions.
MINTMINT-3006855.
STRING9606.ENSP00000231061.

Chemistry

DrugBankDB00102. Becaplermin.

PTM databases

PhosphoSiteP09486.

Polymorphism databases

DMDM129283.

2D gel databases

OGPP09486.

Proteomic databases

MaxQBP09486.
PaxDbP09486.
PeptideAtlasP09486.
PRIDEP09486.

Protocols and materials databases

DNASU6678.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231061; ENSP00000231061; ENSG00000113140.
GeneID6678.
KEGGhsa:6678.
UCSCuc003lui.4. human.

Organism-specific databases

CTD6678.
GeneCardsGC05M151021.
HGNCHGNC:11219. SPARC.
HPACAB002306.
HPA002989.
HPA003020.
MIM182120. gene.
neXtProtNX_P09486.
PharmGKBPA36055.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147672.
HOVERGENHBG002746.
InParanoidP09486.
OMACFGIKEK.
OrthoDBEOG738059.
PhylomeDBP09486.
TreeFamTF319356.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP09486.
BgeeP09486.
CleanExHS_SPARC.
GenevestigatorP09486.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR003645. Fol_N.
IPR015369. Follistatin/Osteonectin_EGF.
IPR002350. Kazal_dom.
IPR001999. Osteonectin_CS.
IPR019577. SPARC/Testican_Ca-bd-dom.
[Graphical view]
PfamPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
[Graphical view]
SMARTSM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS00612. OSTEONECTIN_1. 1 hit.
PS00613. OSTEONECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPARC. human.
EvolutionaryTraceP09486.
GeneWikiOsteonectin.
GenomeRNAi6678.
NextBio26041.
PMAP-CutDBP09486.
PROP09486.
SOURCESearch...

Entry information

Entry nameSPRC_HUMAN
AccessionPrimary (citable) accession number: P09486
Secondary accession number(s): D3DQH9, Q6IBK4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM