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Protein

SPARC

Gene

SPARC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi274 – 285Add BLAST12

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • collagen binding Source: UniProtKB
  • extracellular matrix binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113140-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000497. Scavenging by Class H Receptors.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SPARC
Synonyms:ON
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:11219. SPARC.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB-SubCell
  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endocytic vesicle lumen Source: Reactome
  • extracellular region Source: UniProtKB
  • extracellular space Source: GO_Central
  • nuclear matrix Source: UniProtKB
  • platelet alpha granule Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
  • platelet alpha granule membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Osteogenesis imperfecta 17 (OI17)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae.
See also OMIM:616507
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075142166R → H in OI17; decreased secretion of the protein; altered secretion of procollagen type I. 1 Publication1
Natural variantiVAR_075143263E → K in OI17; no effect on expression and secretion of the protein; altered secretion of procollagen type I. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi166R → A, L or K: Strongly reduced collagen binding. 1 Publication1
Mutagenesisi173N → A or Q: Strongly reduced collagen binding. 1 Publication1
Mutagenesisi259L → A: Loss of collagen binding. 1 Publication1
Mutagenesisi262M → A: Strongly reduced collagen binding. 1 Publication1
Mutagenesisi263E → A: Loss of collagen binding. 1 Publication1

Keywords - Diseasei

Disease mutation, Osteogenesis imperfecta

Organism-specific databases

DisGeNETi6678.
MIMi616507. phenotype.
OpenTargetsiENSG00000113140.
PharmGKBiPA36055.

Polymorphism and mutation databases

BioMutaiSPARC.
DMDMi129283.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000002030418 – 303SPARCAdd BLAST286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi72 ↔ 83PROSITE-ProRule annotation1 Publication
Disulfide bondi77 ↔ 93PROSITE-ProRule annotation1 Publication
Disulfide bondi95 ↔ 130PROSITE-ProRule annotation1 Publication
Disulfide bondi101 ↔ 123PROSITE-ProRule annotation1 Publication
Disulfide bondi112 ↔ 149PROSITE-ProRule annotation1 Publication
Glycosylationi116N-linked (GlcNAc...)2 Publications1
Disulfide bondi155 ↔ 265PROSITE-ProRule annotation1 Publication
Disulfide bondi273 ↔ 289PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP09486.
MaxQBiP09486.
PaxDbiP09486.
PeptideAtlasiP09486.
PRIDEiP09486.

2D gel databases

OGPiP09486.

PTM databases

iPTMnetiP09486.
PhosphoSitePlusiP09486.
UniCarbKBiP09486.

Miscellaneous databases

PMAP-CutDBP09486.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiENSG00000113140.
CleanExiHS_SPARC.
ExpressionAtlasiP09486. baseline and differential.
GenevisibleiP09486. HS.

Organism-specific databases

HPAiCAB002306.
HPA002989.
HPA003020.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
fafQ2TV774EBI-2800983,EBI-6405263From a different organism.

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112560. 10 interactors.
DIPiDIP-46426N.
IntActiP09486. 11 interactors.
MINTiMINT-3006855.
STRINGi9606.ENSP00000231061.

Structurei

Secondary structure

1303
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni71 – 74Combined sources4
Beta strandi81 – 85Combined sources5
Beta strandi91 – 95Combined sources5
Helixi98 – 100Combined sources3
Helixi107 – 109Combined sources3
Beta strandi111 – 113Combined sources3
Turni114 – 116Combined sources3
Beta strandi118 – 121Combined sources4
Helixi122 – 131Combined sources10
Turni132 – 134Combined sources3
Helixi136 – 140Combined sources5
Beta strandi143 – 148Combined sources6
Helixi157 – 181Combined sources25
Beta strandi183 – 188Combined sources6
Helixi190 – 201Combined sources12
Helixi213 – 222Combined sources10
Helixi224 – 227Combined sources4
Helixi228 – 238Combined sources11
Beta strandi244 – 247Combined sources4
Turni249 – 252Combined sources4
Helixi253 – 256Combined sources4
Turni257 – 259Combined sources3
Helixi260 – 262Combined sources3
Helixi263 – 265Combined sources3
Helixi266 – 273Combined sources8
Beta strandi278 – 282Combined sources5
Helixi283 – 289Combined sources7
Helixi294 – 296Combined sources3
Helixi299 – 301Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BMOX-ray3.10A/B71-303[»]
1NUBX-ray2.80A/B71-303[»]
1SRAX-ray2.00A153-303[»]
2V53X-ray3.20A70-303[»]
ProteinModelPortaliP09486.
SMRiP09486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09486.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 93Follistatin-likeAdd BLAST23
Domaini89 – 151Kazal-likePROSITE-ProRule annotationAdd BLAST63
Domaini261 – 296EF-handAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi22 – 69Asp/Glu-rich (acidic; binds calcium)Add BLAST48

Sequence similaritiesi

Belongs to the SPARC family.Curated
Contains 1 EF-hand domain.Curated
Contains 1 follistatin-like domain.Curated
Contains 1 Kazal-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4004. Eukaryota.
ENOG41101WW. LUCA.
GeneTreeiENSGT00510000046787.
HOVERGENiHBG002746.
InParanoidiP09486.
OMAiKDFPRRM.
OrthoDBiEOG091G0CPG.
PhylomeDBiP09486.
TreeFamiTF319356.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. 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]
PfamiPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
[Graphical view]
SMARTiSM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS00612. OSTEONECTIN_1. 1 hit.
PS00613. OSTEONECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09486-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV
60 70 80 90 100
EVGEFDDGAE ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS
110 120 130 140 150
CPAPIGEFEK VCSNDNKTFD SSCHFFATKC TLEGTKKGHK LHLDYIGPCK
160 170 180 190 200
YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE RDEDNNLLTE KQKLRVKKIH
210 220 230 240 250
ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ HPIDGYLSHT
260 270 280 290 300
ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD

LVI
Length:303
Mass (Da):34,632
Last modified:July 1, 1989 - v1
Checksum:iB914599F79705945
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti42 – 43SV → PT AA sequence (PubMed:3597437).Curated2
Sequence conflicti205R → L in AAA60993 (PubMed:2790009).Curated1
Sequence conflicti269F → L in AAA60993 (PubMed:2790009).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05043119P → S.Corresponds to variant rs6874468dbSNPEnsembl.1
Natural variantiVAR_05953070N → S.Corresponds to variant rs13359508dbSNPEnsembl.1
Natural variantiVAR_075142166R → H in OI17; decreased secretion of the protein; altered secretion of procollagen type I. 1 Publication1
Natural variantiVAR_075143263E → K in OI17; no effect on expression and secretion of the protein; altered secretion of procollagen type I. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00755 mRNA. Translation: CAA68724.1.
J03040 mRNA. Translation: AAA60570.1.
M25746
, 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.
CCDSiCCDS4318.1.
PIRiA32821. GEHUN.
RefSeqiNP_001296372.1. NM_001309443.1.
NP_001296373.1. NM_001309444.1.
NP_003109.1. NM_003118.3.
UniGeneiHs.111779.

Genome annotation databases

EnsembliENST00000231061; ENSP00000231061; ENSG00000113140.
GeneIDi6678.
KEGGihsa:6678.
UCSCiuc003lui.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Osteonectin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00755 mRNA. Translation: CAA68724.1.
J03040 mRNA. Translation: AAA60570.1.
M25746
, 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.
CCDSiCCDS4318.1.
PIRiA32821. GEHUN.
RefSeqiNP_001296372.1. NM_001309443.1.
NP_001296373.1. NM_001309444.1.
NP_003109.1. NM_003118.3.
UniGeneiHs.111779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BMOX-ray3.10A/B71-303[»]
1NUBX-ray2.80A/B71-303[»]
1SRAX-ray2.00A153-303[»]
2V53X-ray3.20A70-303[»]
ProteinModelPortaliP09486.
SMRiP09486.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112560. 10 interactors.
DIPiDIP-46426N.
IntActiP09486. 11 interactors.
MINTiMINT-3006855.
STRINGi9606.ENSP00000231061.

PTM databases

iPTMnetiP09486.
PhosphoSitePlusiP09486.
UniCarbKBiP09486.

Polymorphism and mutation databases

BioMutaiSPARC.
DMDMi129283.

2D gel databases

OGPiP09486.

Proteomic databases

EPDiP09486.
MaxQBiP09486.
PaxDbiP09486.
PeptideAtlasiP09486.
PRIDEiP09486.

Protocols and materials databases

DNASUi6678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000231061; ENSP00000231061; ENSG00000113140.
GeneIDi6678.
KEGGihsa:6678.
UCSCiuc003lui.5. human.

Organism-specific databases

CTDi6678.
DisGeNETi6678.
GeneCardsiSPARC.
HGNCiHGNC:11219. SPARC.
HPAiCAB002306.
HPA002989.
HPA003020.
MIMi182120. gene.
616507. phenotype.
neXtProtiNX_P09486.
OpenTargetsiENSG00000113140.
PharmGKBiPA36055.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4004. Eukaryota.
ENOG41101WW. LUCA.
GeneTreeiENSGT00510000046787.
HOVERGENiHBG002746.
InParanoidiP09486.
OMAiKDFPRRM.
OrthoDBiEOG091G0CPG.
PhylomeDBiP09486.
TreeFamiTF319356.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113140-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000497. Scavenging by Class H Receptors.

Miscellaneous databases

ChiTaRSiSPARC. human.
EvolutionaryTraceiP09486.
GeneWikiiOsteonectin.
GenomeRNAii6678.
PMAP-CutDBP09486.
PROiP09486.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113140.
CleanExiHS_SPARC.
ExpressionAtlasiP09486. baseline and differential.
GenevisibleiP09486. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. 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]
PfamiPF09289. FOLN. 1 hit.
PF00050. Kazal_1. 1 hit.
PF10591. SPARC_Ca_bdg. 1 hit.
[Graphical view]
SMARTiSM00274. FOLN. 1 hit.
SM00280. KAZAL. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS51465. KAZAL_2. 1 hit.
PS00612. OSTEONECTIN_1. 1 hit.
PS00613. OSTEONECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPRC_HUMAN
AccessioniPrimary (citable) accession number: P09486
Secondary accession number(s): D3DQH9, Q6IBK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.