SPARCL1

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]
End	87,531,061 bp[1]
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)[2]
End	104,261,599 bp[2]
RNA expression pattern
	Top expressed in
	middle temporal gyrus; ; postcentral gyrus; ; superior frontal gyrus; ; Brodmann area 23; ; orbitofrontal cortex; ; external globus pallidus; ; Region I of hippocampus proper; ; occipital lobe; ; Brodmann area 46; ; entorhinal cortex;
	Top expressed in
	dorsal tegmental nucleus; ; medial vestibular nucleus; ; cerebellar vermis; ; ventral tegmental area; ; globus pallidus; ; pontine nuclei; ; dorsomedial hypothalamic nucleus; ; paraventricular nucleus of hypothalamus; ; mammillary body; ; lateral geniculate nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	metal ion binding; calcium ion binding; collagen binding; extracellular matrix binding; protein binding;
Cellular component	extracellular exosome; extracellular space; endoplasmic reticulum lumen; extracellular region; collagen-containing extracellular matrix; glutamatergic synapse;
Biological process	signal transduction; anatomical structure development; post-translational protein modification; synaptic membrane adhesion;
	Sources:Amigo / QuickGO
Orthologs
	8404
	13602
	ENSG00000152583
	ENSMUSG00000029309
	Q14515
	P70663
	NM_004684; NM_001128310; NM_001291976; NM_001291977
	NM_010097; NM_001359014; NM_001359016
	NP_001121782; NP_001278905; NP_001278906; NP_004675
	NP_034227; NP_001345943; NP_001345945
	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]

Interactions

CALY (calcyon)[12]

References

GRCh38: Ensembl release 89: ENSG00000152583 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000029309 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
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.
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.
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.
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.
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.
"Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)".
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.

Girard JP, Springer TA (February 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 (March 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, et al. (June 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, et al. (July 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 (January 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, et al. (October 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000152583 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029309 - Ensembl, 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.

[pmid7600298-5] 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.

[pmid16844696-7] 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.

[pmid8488563-10] 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.

[entrez-11] "Entrez Gene: SPARCL1 SPARC-like 1 (mast9, hevin)".

[KimJung2021-12] 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.

SPARCL1

Interactions

See also

References

Further reading