SVIL

Supervillin is a protein that in humans is encoded by the SVIL gene.

SVIL
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2K6M, 2K6N
Identifiers
Aliases	SVIL, supervillin, MFM10
External IDs	OMIM: 604126; MGI: 2147319; HomoloGene: 25090; GeneCards: SVIL; OMA:SVIL - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10p11.23 Start 29,457,338 bp End 29,736,959 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 A1 Start 4,920,540 bp End 5,119,299 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in glutes Skeletal muscle tissue of rectus abdominis vastus lateralis muscle biceps brachii Skeletal muscle tissue of biceps brachii deltoid muscle gastrocnemius muscle tibialis anterior muscle thoracic diaphragm body of tongue Top expressed in soleus muscle triceps brachii muscle vastus lateralis muscle right ventricle ankle digastric muscle temporal muscle sternocleidomastoid muscle atrium granulocyte More reference expression data BioGPS More reference expression data
Gene ontology Molecular function actin filament binding actin binding protein binding Cellular component cytoplasm microtubule minus-end podosome cell junction plasma membrane cell projection midbody cleavage furrow costamere cytoskeleton membrane nucleus focal adhesion actin cytoskeleton cytosol Biological process positive regulation of cytokinesis skeletal muscle tissue development cytoskeleton organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6840 225115 Ensembl ENSG00000197321 ENSMUSG00000024236 UniProt O95425 Q8K4L3 RefSeq (mRNA) NM_003174 NM_021738 NM_001323599 NM_001323600 NM_153153 NM_178046 NM_001347449 RefSeq (protein) NP_001310528 NP_001310529 NP_003165 NP_068506 NP_001334378 NP_694793 NP_001392206 NP_001392207 NP_001392209 NP_001392210 NP_001392211 NP_001392219 Location (UCSC) Chr 10: 29.46 – 29.74 Mb Chr 18: 4.92 – 5.12 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. Its function may include recruitment of actin and other cytoskeletal proteins into specialized structures at the plasma membrane and in the nuclei of growing cells. Two transcript variants encoding different isoforms of supervillin have been described.

Interactions

SVIL has been shown to interact with Androgen receptor.

Further reading

• Pope RK, Pestonjamasp KN, Smith KP, Wulfkuhle JD, Strassel CP, Lawrence JB, Luna EJ (Sep 1998). "Cloning, characterization, and chromosomal localization of human supervillin (SVIL)". Genomics. 52 (3): 342–51. doi:10.1006/geno.1998.5466. PMID 9867483.
• Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ (Jul 1999). "Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals". Journal of Cell Science. 112 ( Pt 13) (13): 2125–36. doi:10.1242/jcs.112.13.2125. PMID 10362542.
• Kim M, Jiang LH, Wilson HL, North RA, Surprenant A (Nov 2001). "Proteomic and functional evidence for a P2X7 receptor signalling complex". The EMBO Journal. 20 (22): 6347–58. doi:10.1093/emboj/20.22.6347. PMC 125721. PMID 11707406.
• Ting HJ, Yeh S, Nishimura K, Chang C (Jan 2002). "Supervillin associates with androgen receptor and modulates its transcriptional activity". Proceedings of the National Academy of Sciences of the United States of America. 99 (2): 661–6. Bibcode:2002PNAS...99..661T. doi:10.1073/pnas.022469899. PMC 117362. PMID 11792840.
• Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ (Jun 2003). "Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton". Journal of Cell Science. 116 (Pt 11): 2261–75. doi:10.1242/jcs.00422. hdl:2022/26449. PMID 12711699.
• Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ (Nov 2003). "F-actin and myosin II binding domains in supervillin". The Journal of Biological Chemistry. 278 (46): 46094–106. doi:10.1074/jbc.M305311200. PMID 12917436.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.