SVIL

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SVIL
Protein SVIL PDB 2K6M.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SVIL
External IDs MGI: 2147319 HomoloGene: 25090 GeneCards: SVIL
RNA expression pattern
PBB GE SVIL 202566 s at fs.png

PBB GE SVIL 202565 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
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_694793.1
NP_001334378
NP_694793

Location (UCSC) Chr 10: 29.46 – 29.74 Mb Chr 18: 4.92 – 5.12 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Supervillin is a protein that in humans is encoded by the SVIL gene.[3][4]

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.[5] 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.[4]

Interactions[edit]

SVIL has been shown to interact with Androgen receptor.[6]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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 2140202Freely accessible. PMID 9382871. 
  4. ^ a b "Entrez Gene: SVIL supervillin". 
  5. ^ 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. 
  6. ^ 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 117362Freely accessible. PMID 11792840. 

Further reading[edit]