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Showing Protein SPARC (HMDBP02109)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP02109
Secondary Accession Numbers
  • 7591
Name SPARC
Synonyms
  1. BM-40
  2. Basement-membrane protein 40
  3. ON
  4. Osteonectin
  5. Secreted protein acidic and rich in cysteine
Gene Name SPARC
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific 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 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity
Pathways Not Available
Reactions Not Available
GO Classification
Component
extracellular region part
extracellular matrix
proteinaceous extracellular matrix
Function
ion binding
cation binding
metal ion binding
binding
calcium ion binding
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
Cellular Location
  1. Secreted
  2. extracellular space
  3. extracellular matrix
  4. basement membrane
Gene Properties
Chromosome Location Chromosome:5
Locus 5q31.3-q32
SNPs SPARC
Gene Sequence 
>912 bp
ATGAGGGCCTGGATCTTCTTTCTCCTTTGCCTGGCCGGGAGGGCTCTGGCAGCCCCTCAG
CAAGAAGCCCTGCCTGATGAGACAGAGGTGGTGGAAGAAACTGTGGCAGAGGTGACTGAG
GTATCTGTGGGAGCTAATCCTGTCCAGGTGGAAGTAGGAGAATTTGATGATGGTGCAGAG
GAAACCGAAGAGGAGGTGGTGGCGGAAAATCCCTGCCAGAACCACCACTGCAAACACGGC
AAGGTGTGCGAGCTGGATGAGAACAACACCCCCATGTGCGTGTGCCAGGACCCCACCAGC
TGCCCAGCCCCCATTGGCGAGTTTGAGAAGGTGTGCAGCAATGACAACAAGACCTTCGAC
TCTTCCTGCCACTTCTTTGCCACAAAGTGCACCCTGGAGGGCACCAAGAAGGGCCACAAG
CTCCACCTGGACTACATCGGGCCTTGCAAATACATCCCCCCTTGCCTGGACTCTGAGCTG
ACCGAATTCCCCCTGCGCATGCGGGACTGGCTCAAGAACGTCCTGGTCACCCTGTATGAG
AGGGATGAGGACAACAACCTTCTGACTGAGAAGCAGAAGCTGCGGGTGAAGAAGATCCAT
GAGAATGAGAAGCGCCTGGAGGCAGGAGACCACCCCGTGGAGCTGCTGGCCCGGGACTTC
GAGAAGAACTATAACATGTACATCTTCCCTGTACACTGGCAGTTCGGCCAGCTGGACCAG
CACCCCATTGACGGGTACCTCTCCCACACCGAGCTGGCTCCACTGCGTGCTCCCCTCATC
CCCATGGAGCATTGCACCACCCGCTTTTTCGAGACCTGTGACCTGGACAATGACAAGTAC
ATCGCCCTGGATGAGTGGGCCGGCTGCTTCGGCATCAAGCAGAAGGATATCGACAAGGAT
CTTGTGATCTAA
Protein Properties
Number of Residues 303
Molecular Weight 34631.9
Theoretical pI 4.47
Pfam Domain Function
Signals
  • 1-17
Transmembrane Regions
  • None
Protein Sequence 
>SPARC
MRAWIFFLLCLAGRALAAPQQEALPDETEVVEETVAEVTEVSVGANPVQVEVGEFDDGAE
ETEEEVVAENPCQNHHCKHGKVCELDENNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFD
SSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIPPCLDSELTEFPLRMRDWLKNVLVTLYE
RDEDNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQ
HPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALDEWAGCFGIKQKDIDKD
LVI
GenBank ID Protein 29462
UniProtKB/Swiss-Prot ID P09486
UniProtKB/Swiss-Prot Entry Name SPRC_HUMAN
PDB IDs
GenBank Gene ID Y00755
GeneCard ID SPARC
GenAtlas ID SPARC
HGNC ID HGNC:11219
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  3. Fisher LW, Hawkins GR, Tuross N, Termine JD: 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. J Biol Chem. 1987 Jul 15;262(20):9702-8. [PubMed:3597437 ]
  4. Lankat-Buttgereit B, Mann K, Deutzmann R, Timpl R, Krieg T: Cloning and complete amino acid sequences of human and murine basement membrane protein BM-40 (SPARC, osteonectin). FEBS Lett. 1988 Aug 29;236(2):352-6. [PubMed:3410046 ]
  5. Swaroop A, Hogan BL, Francke U: Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40: sequence, expression, and localization of the gene to chromosome 5q31-q33. Genomics. 1988 Jan;2(1):37-47. [PubMed:2838412 ]
  6. Villarreal XC, Mann KG, Long GL: Structure of human osteonectin based upon analysis of cDNA and genomic sequences. Biochemistry. 1989 Jul 25;28(15):6483-91. [PubMed:2790009 ]
  7. Young MF, Day AA, Dominquez P, McQuillan CI, Fisher LW, Termine JD: Structure and expression of osteonectin mRNA in human tissue. Connect Tissue Res. 1990;24(1):17-28. [PubMed:2338025 ]
  8. Kelm RJ Jr, Mann KG: Human platelet osteonectin: release, surface expression, and partial characterization. Blood. 1990 Mar 1;75(5):1105-13. [PubMed:2306517 ]
  9. Wewer UM, Albrechtsen R, Fisher LW, Young MF, Termine JD: Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues characterized by de novo formation of basement membrane. Am J Pathol. 1988 Aug;132(2):345-55. [PubMed:3400777 ]
  10. Kuhn C, Mason RJ: Immunolocalization of SPARC, tenascin, and thrombospondin in pulmonary fibrosis. Am J Pathol. 1995 Dec;147(6):1759-69. [PubMed:7495300 ]
  11. Hunzelmann N, Hafner M, Anders S, Krieg T, Nischt R: BM-40 (osteonectin, SPARC) is expressed both in the epidermal and in the dermal compartment of adult human skin. J Invest Dermatol. 1998 Feb;110(2):122-6. [PubMed:9457905 ]
  12. Hohenester E, Maurer P, Hohenadl C, Timpl R, Jansonius JN, Engel J: Structure of a novel extracellular Ca(2+)-binding module in BM-40. Nat Struct Biol. 1996 Jan;3(1):67-73. [PubMed:8548457 ]
  13. Hohenester E, Maurer P, Timpl R: Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. EMBO J. 1997 Jul 1;16(13):3778-86. [PubMed:9233787 ]
  14. Sasaki T, Hohenester E, Gohring W, Timpl R: Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin. EMBO J. 1998 Mar 16;17(6):1625-34. [PubMed:9501084 ]