SPARCL1

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.[4][5] It interacts with the extracellular matrix to create intermediate states of cell adhesion.[6] Due to its dynamic extracellular roles, being implicated in cancer metastasis and inflammation, it is considered a matricellular protein.[7][8] In humans hevin is encoded by the SPARCL1 gene.[9][10]

SPARCL1
Identifiers
Aliases	SPARCL1, MAST 9, MAST9, PIG33, SC1, SPARC like 1
External IDs	OMIM: 606041 MGI: 108110 HomoloGene: 3438 GeneCards: SPARCL1
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q22.1 Start 87,473,335 bp[1] End 87,531,061 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • calcium ion binding • collagen binding • extracellular matrix binding • GO:0001948 protein binding Cellular component • extracellular exosome • extracellular • endoplasmic reticulum lumen • extracellular region • collagen-containing extracellular matrix • glutamatergic synapse Biological process • signal transduction • anatomical structure development • post-translational modification • cellular protein metabolic process • synaptic membrane adhesion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8404	13602
Ensembl	ENSG00000152583	ENSMUSG00000029309
UniProt	Q14515	P70663
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 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

See also

• Thrombospondin
• Tenascin

References

1. GRCh38: Ensembl release 89: ENSG00000152583 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. 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. doi:10.1016/1074-7613(95)90083-7. PMID 7600298.
5. 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. doi:10.1074/jbc.M212291200. PMID 12538579.
6. 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. doi:10.1074/jbc.M510507200. PMID 16844696.
7. Morris AH, Kyriakides TR (Jul 2014). "Matricellular proteins and biomaterials". Matrix Biology. 37: 183–91. doi:10.1016/j.matbio.2014.03.002. PMC 4167162. PMID 24657843.
8. 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. doi:10.1016/j.biocel.2004.01.017. PMID 15094114.
9. 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. doi:10.1016/0168-9525(93)90216-5. PMID 8488563.
10. "Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)".

Further reading

• Girard JP, Springer TA (Feb 1996). "Modulation of endothelial cell adhesion by hevin, an acidic protein associated with high endothelial venules". The Journal of Biological Chemistry. 271 (8): 4511–7. doi:10.1074/jbc.271.8.4511. PMID 8626806.
• Claeskens A, Ongenae N, Neefs JM, Cheyns P, Kaijen P, Cools M, Kutoh E (Mar 2000). "Hevin is down-regulated in many cancers and is a negative regulator of cell growth and proliferation". British Journal of Cancer. 82 (6): 1123–30. doi:10.1054/bjoc.1999.1051. PMC 2363342. PMID 10735494.
• Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA (Jun 2004). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nature Biotechnology. 22 (6): 724–31. doi:10.1038/nbt969. PMID 15146195. S2CID 36630738.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Li Y, Aroca-Aguilar JD, Ghosh S, Sánchez-Sánchez F, Escribano J, Coca-Prados M (Jan 2006). "Interaction of myocilin with the C-terminal region of hevin". Biochemical and Biophysical Research Communications. 339 (3): 797–804. doi:10.1016/j.bbrc.2005.11.082. PMID 16316624.
• Liu T, Qian WJ, Gritsenko MA, Camp DG, Monroe ME, Moore RJ, Smith RD (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". Journal of Proteome Research. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
• Scalabrini D, Fenoglio C, Scarpini E, De Riz M, Comi C, Venturelli E, Cortini F, Piola M, Villa C, Naldi P, Monaco F, Bresolin N, Galimberti D (Oct 2007). "Candidate gene analysis of SPARCL1 gene in patients with multiple sclerosis". Neuroscience Letters. 425 (3): 173–6. doi:10.1016/j.neulet.2007.08.020. PMID 17825989. S2CID 9381979.