SVIL

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Supervillin
Protein SVIL PDB 2K6M.png
Rendering based on PDB 2K6M​.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SVIL ; DKFZp686A17191
External IDs OMIM604126 MGI2147319 HomoloGene25090 GeneCards: SVIL Gene
RNA expression pattern
PBB GE SVIL 202565 s at tn.png
PBB GE SVIL 202566 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6840 225115
Ensembl ENSG00000197321 ENSMUSG00000024236
UniProt O95425 Q8K4L3
RefSeq (mRNA) NM_003174 NM_153153
RefSeq (protein) NP_003165 NP_694793
Location (UCSC) Chr 10:
29.46 – 29.74 Mb
Chr 18:
4.92 – 5.12 Mb
PubMed search [1] [2]

Supervillin is a protein that in humans is encoded by the SVIL gene.[1][2]

Function[edit]

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.[3] 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.[2]

Interactions[edit]

SVIL has been shown to interact with Androgen receptor.[4]

References[edit]

  1. ^ Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ (Dec 1997). "Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily". The Journal of Cell Biology 139 (5): 1255–69. doi:10.1083/jcb.139.5.1255. PMC 2140202. PMID 9382871. 
  2. ^ a b "Entrez Gene: SVIL supervillin". 
  3. ^ Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (Nov 2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. 
  4. ^ 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. 

Further reading[edit]