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]

SPARCL1
Identifiers
AliasesSPARCL1, MAST 9, MAST9, PIG33, SC1, SPARC like 1
External IDsOMIM: 606041; MGI: 108110; HomoloGene: 3438; GeneCards: SPARCL1; OMA:SPARCL1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004684
NM_001128310
NM_001291976
NM_001291977

NM_010097
NM_001359014
NM_001359016

RefSeq (protein)

NP_001121782
NP_001278905
NP_001278906
NP_004675

NP_034227
NP_001345943
NP_001345945

Location (UCSC)Chr 4: 87.47 – 87.53 MbChr 5: 104.23 – 104.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Interactions

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See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000152583Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029309Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Girard JP, Springer TA (January 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. doi:10.1016/1074-7613(95)90083-7. PMID 7600298.
  6. ^ Hambrock HO, Nitsche DP, Hansen U, Bruckner P, Paulsson M, Maurer P, Hartmann U (March 2003). "SC1/hevin. An extracellular calcium-modulated protein that binds collagen I". The Journal of Biological Chemistry. 278 (13): 11351–8. doi:10.1074/jbc.M212291200. PMID 12538579.
  7. ^ Sullivan MM, Barker TH, Funk SE, Karchin A, Seo NS, Höök M, et al. (September 2006). "Matricellular hevin regulates decorin production and collagen assembly". The Journal of Biological Chemistry. 281 (37): 27621–32. doi:10.1074/jbc.M510507200. PMID 16844696.
  8. ^ Morris AH, Kyriakides TR (July 2014). "Matricellular proteins and biomaterials". Matrix Biology. 37: 183–91. doi:10.1016/j.matbio.2014.03.002. PMC 4167162. PMID 24657843.
  9. ^ Sullivan MM, Sage EH (June 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. doi:10.1016/j.biocel.2004.01.017. PMID 15094114.
  10. ^ Schraml P, Shipman R, Stulz P, Ludwig CU (March 1993). "cDNA subtraction library construction using a magnet-assisted subtraction technique (MAST)". Trends in Genetics. 9 (3): 70–1. doi:10.1016/0168-9525(93)90216-5. PMID 8488563.
  11. ^ "Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)".
  12. ^ Kim JH, Jung HG, Kim A, Shim HS, Hyeon SJ, Lee YS, et al. (March 2021). "Hevin-calcyon interaction promotes synaptic reorganization after brain injury". Cell Death and Differentiation. 28 (9): 2571–2588. doi:10.1038/s41418-021-00772-5. ISSN 1350-9047. PMC 8408247. PMID 33753902.

Further reading

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