SPARCL1

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SPARCL1
Identifiers
Aliases SPARCL1, MAST 9, MAST9, PIG33, SC1, SPARC like 1
External IDs MGI: 108110 HomoloGene: 3438 GeneCards: SPARCL1
Gene location (Human)
Chromosome 4 (human)
Chr. Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for SPARCL1
Genomic location for SPARCL1
Band No data available Start 87,473,335 bp[1]
End 87,531,061 bp[1]
RNA expression pattern
PBB GE SPARCL1 200795 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004684
NM_001128310
NM_001291976
NM_001291977

NM_010097

RefSeq (protein)

NP_001121782
NP_001278905
NP_001278906
NP_004675

NP_034227

Location (UCSC) Chr 4: 87.47 – 87.53 Mb Chr 4: 104.08 – 104.11 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

SPARC-like protein 1 (SPARCL1 or SC1), also known as hevin (short for high endothelial venule protein), is a secreted protein with high structural similarity to SPARC.[5][6] It interacts with the extracellular matrix to create intermediate states of cell adhesion.[7] Due to its dynamic extracellular roles, being implicated in cancer metastasis and inflammation, it is considered a matricellular protein.[8][9] In humans hevin is encoded by the SPARCL1 gene.[10][11]

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000152583 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029309 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ Girard JP, Springer TA (Jan 1995). "Cloning from purified high endothelial venule cells of hevin, a close relative of the antiadhesive extracellular matrix protein SPARC". Immunity. 2 (1): 113–23. PMID 7600298. doi:10.1016/1074-7613(95)90083-7. 
  6. ^ Hambrock HO, Nitsche DP, Hansen U, Bruckner P, Paulsson M, Maurer P, Hartmann U (Mar 2003). "SC1/hevin. An extracellular calcium-modulated protein that binds collagen I". The Journal of Biological Chemistry. 278 (13): 11351–8. PMID 12538579. doi:10.1074/jbc.M212291200. 
  7. ^ Sullivan MM, Barker TH, Funk SE, Karchin A, Seo NS, Höök M, Sanders J, Starcher B, Wight TN, Puolakkainen P, Sage EH (Sep 2006). "Matricellular hevin regulates decorin production and collagen assembly". The Journal of Biological Chemistry. 281 (37): 27621–32. PMID 16844696. doi:10.1074/jbc.M510507200. 
  8. ^ Morris AH, Kyriakides TR (Jul 2014). "Matricellular proteins and biomaterials". Matrix Biology. 37: 183–91. PMC 4167162Freely accessible. PMID 24657843. doi:10.1016/j.matbio.2014.03.002. 
  9. ^ Sullivan MM, Sage EH (Jun 2004). "Hevin/SC1, a matricellular glycoprotein and potential tumor-suppressor of the SPARC/BM-40/Osteonectin family". The International Journal of Biochemistry & Cell Biology. 36 (6): 991–6. PMID 15094114. doi:10.1016/j.biocel.2004.01.017. 
  10. ^ Schraml P, Shipman R, Stulz P, Ludwig CU (Mar 1993). "cDNA subtraction library construction using a magnet-assisted subtraction technique (MAST)". Trends in Genetics. 9 (3): 70–1. PMID 8488563. doi:10.1016/0168-9525(93)90216-5. 
  11. ^ "Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)". 

Further reading[edit]