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Q8K4L3

- SVIL_MOUSE

UniProt

Q8K4L3 - SVIL_MOUSE

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Protein

Supervillin

Gene
Svil
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Forms a high-affinity link between the actin cytoskeleton and the membrane. Isoform 1 (archvillin) is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function. Isoform 2 may be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6 By similarity.

GO - Biological processi

  1. cytoskeleton organization Source: InterPro
  2. skeletal muscle tissue development Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Supervillin
Alternative name(s):
Archvillin
p205/p250
Gene namesi
Name:Svil
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:2147319. Svil.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectioninvadopodium By similarity. Cell projectionpodosome By similarity
Note: Tightly associated with both actin filaments and plasma membranes.

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. costamere Source: Ensembl
  3. invadopodium Source: UniProtKB-SubCell
  4. nucleus Source: Ensembl
  5. plasma membrane Source: UniProtKB-SubCell
  6. podosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21702170SupervillinPRO_0000218741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine By similarity
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei666 – 6661Phosphoserine By similarity
Modified residuei811 – 8111Phosphothreonine By similarity
Modified residuei857 – 8571Phosphoserine1 Publication
Modified residuei877 – 8771Phosphoserine By similarity
Modified residuei881 – 8811Phosphoserine By similarity
Modified residuei960 – 9601Phosphoserine2 Publications
Modified residuei1077 – 10771Phosphoserine By similarity
Modified residuei1181 – 11811Phosphoserine By similarity
Modified residuei1186 – 11861Phosphothreonine By similarity
Modified residuei1278 – 12781Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8K4L3.
PaxDbiQ8K4L3.
PRIDEiQ8K4L3.

PTM databases

PhosphoSiteiQ8K4L3.

Expressioni

Gene expression databases

ArrayExpressiQ8K4L3.
BgeeiQ8K4L3.
CleanExiMM_SVIL.
GenevestigatoriQ8K4L3.

Interactioni

Subunit structurei

Associates with F-actin. Interacts with NEB. Interacts with MYH9. Interacts with MYLK. Isoform 2 interacts with TRIP6. Isoform 2 interacts with DYNLT1 By similarity.

Protein-protein interaction databases

BioGridi230358. 1 interaction.
IntActiQ8K4L3. 1 interaction.
MINTiMINT-4136191.

Structurei

3D structure databases

ProteinModelPortaliQ8K4L3.
SMRiQ8K4L3. Positions 1398-1640, 1712-2079, 2104-2170.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1397 – 1496100Gelsolin-like 1Add
BLAST
Repeati1516 – 1638123Gelsolin-like 2Add
BLAST
Repeati1708 – 1818111Gelsolin-like 3Add
BLAST
Repeati1837 – 1938102Gelsolin-like 4Add
BLAST
Repeati1971 – 2078108Gelsolin-like 5Add
BLAST
Domaini2107 – 217064HPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 167167Interaction with MYLK By similarityAdd
BLAST
Regioni1375 – 1643269Interaction with NEB By similarityAdd
BLAST

Domaini

As opposed to other villin-type headpiece domains, supervillin HP (SVHP) doesn't bind F-actin due to the absence of a conformationally flexible region (V-loop) By similarity.

Sequence similaritiesi

Belongs to the villin/gelsolin family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG324767.
GeneTreeiENSGT00660000095502.
HOGENOMiHOG000006939.
HOVERGENiHBG052980.
InParanoidiQ8K4L3.
KOiK10369.
OMAiRSHTQPI.
OrthoDBiEOG7WX07J.
PhylomeDBiQ8K4L3.
TreeFamiTF316081.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 5 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR015628. Supervillin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
PTHR11977:SF28. PTHR11977:SF28. 1 hit.
PfamiPF00626. Gelsolin. 1 hit.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 5 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K4L3-1) [UniParc]FASTAAdd to Basket

Also known as: Archvillin

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MKRKERIARR LEGIENDSQP ILLQSCTGLV THRLLEEDTP RYMRATDPAS     50
PHIGRSKEEE DTPGSSLEKQ TPSKYCIETS GIHSSGSMDT HSLESKAERI 100
ARYKAERRRQ LAEKYGLTLD PEADSEYLSR YAKSRKDPDV TERRGKSDKQ 150
EEQSKDANSR HSRTESGPRT SLVASQDCTP LGSNMSDQEQ LLNVENQRRV 200
QDPPLGEDGS SAFFSERSIS FPEVPRSPKQ IPSSPLQQPA SPNHPGDSPL 250
PTEARASTGK PTHEWFLQRD SEGDTPSLIN WPSRVKVREK LVKEESARSS 300
PELTSESLTQ RRQQPAPAHF LPIQSESSTF DRVTSKAVSS LQPSQSGVLP 350
TDPVHAIKLV TMDTPESTSE FSWVGSATPK VIKSTTLKIL EGGSRDAPVL 400
HICESKAEDW LSPEPLERSP KSLLTSEDDR LVRGHKDPSG NKDLDKAIIC 450
SIDVESERER QVQHLPTQRT GRSEMLLYVQ SGPVSQDATL TSHTKEASPK 500
KRKVLARSLS DYTGPPQLQV PRHKDEAPSQ ELELQSSRAE GPGAEASVLD 550
TRVSVAQLRN IFMESTRASK KPELQSRVER SAEGIGLPME RERGSRKPRR 600
YLSPGESRKT SERFRTQPIT SAERKESDRY PSGSEIPVVE DEEKVDERAK 650
LSVAAKRLLF REMEKSFDEH TVPKRHSRNA AVEQRLRRLQ DRSHTQPITT 700
EEVVIAATEP IPASCSGVTH PVTARLPSPT VARSSVQPAR LQASAHQKAL 750
ARDQANEGRE SAEPGEPDSS TLSLAEKLAL FNKLSQPVSK AISTRNRIDV 800
RQRRMNARYQ TQPVTLGEVE QVQSGKLISF SPTVNTSVSI MASAVAPTYA 850
GDLRKLSVDN NTSATDYKSP PAENSDSPVR SILKPQAWRP LVEHSGSKGM 900
PGESGKTESK NALTVAAEDS GVQTRGAFEE EEEPSYPILG RVREGDGQKE 950
PKHVVLRRGS LELGNPSAAH LGDELKEVST AKSSLQENLD LKDKQASEEN 1000
TDVETVMRKF SLKEFGETTS EQTEVAARKA SVQMATPGAW KQQESSEQLA 1050
EKLFKNPCAM FASGEVKVPV GDSFLDSPSK TMSIKERLAL LKKSGEEDWK 1100
NRLIRKQEYG KATGGLHTQE VEQSLKKKRV TESRESQMTI EERKHLITVR 1150
EEAWKTKGRG AANDSTQFTV AGRMVKKGLA SPTSITPISS PLCSKSRGTT 1200
PVSKPLEDIE ARPDMQLESD LKLDRLETFL RRLNNKVAGI QETVLTVTGK 1250
SVKEVMKLDD DETFAKFYRS VDHSIPRSPV ELEEDFDVIF DPYAPKLTSS 1300
VAEHKRQVRP KRRVQASKNP LKLLAARDDL LQEYTEQRLN VAFMESKRMK 1350
VEKMSSNSNF SEVTLAGLAS RENFSNINLR SVNLMEQNSN NSAMPYKKLM 1400
LLQIKGRRHV QTRLVEPRAS SLNSGDCFLL LSPQYCFLWV GEFSNVIEKA 1450
KASELATLIQ TKRELGCRAT YIQTIEEGIN THTHAAKDFW KLLGGQTSYQ 1500
SAGDPKEDEL YETAIIETNC VYRLTDDKLV PDDDYWGKIP KCSLLQSKEV 1550
LVFDFGSEVY VWHGKEVTLA QRKIAFQLAK HLWNGTFDYE NCDINPLDPG 1600
ECNPLIPRKG QGRPDWAIFG RVTEHNETIL FKEKFLDWTE LKRPTEKNSG 1650
EVVQQKDDPR ADVKPYDVTR MVATPQITAG TILDGVNVGR GYGLVEGDDR 1700
RQFEIATVSV DVWHILEFDY SRLPRQSIGQ FHEGDAYVVK WKYMASTAVG 1750
SRQKGEHLVR VAGKEKCVYF FWQGRHSTVS EKGTSALMTV ELDEERGAQV 1800
QVLQGKEPPC FLQCFQGGMV VHSGRREEEE ENVQSEWRLY CVRGEVPMEG 1850
NLLEVACHCS SLRSRTSMVV LNINKALIYL WHGCKAQGHT KEVGRTAANK 1900
IKEECPLEAG LHSSSNVTIH ECDEGSEPLG FWDALGRRDR KAYDCMLQDP 1950
GSFNFAPRLF ILSSSSGDFS ATEFVYPAQA PSAVSSMPFL QEDLYSAPQP 2000
ALFLVDNHHE VYLWQGWWPT ENKITGSARI RWASDRKSAM ETVLQYCRGK 2050
NLKRPPPKSY LIHAGLEPLT FTNMFPSWEH REDIAEITEM DTEVSNQITL 2100
VEDVLAKLCK TIYPLADLLA RPLPEGVDPL KLEIYLTDED FEFALDMSRD 2150
EFNALPTWKQ VNLKKSKGLF 2170
Length:2,170
Mass (Da):243,162
Last modified:October 1, 2002 - v1
Checksum:iAEAB710184FB71C6
GO
Isoform 2 (identifier: Q8K4L3-2)

Also known as: Supervillin

Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF317422 mRNA. Translation: AAM89518.1.
CCDSiCCDS37720.1. [Q8K4L3-1]
RefSeqiNP_694793.1. NM_153153.3. [Q8K4L3-1]
UniGeneiMm.136791.

Genome annotation databases

EnsembliENSMUST00000025079; ENSMUSP00000025079; ENSMUSG00000024236. [Q8K4L3-1]
ENSMUST00000126977; ENSMUSP00000115078; ENSMUSG00000024236. [Q8K4L3-1]
ENSMUST00000140448; ENSMUSP00000119803; ENSMUSG00000024236. [Q8K4L3-1]
GeneIDi225115.
KEGGimmu:225115.
UCSCiuc008dyr.2. mouse. [Q8K4L3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF317422 mRNA. Translation: AAM89518.1 .
CCDSi CCDS37720.1. [Q8K4L3-1 ]
RefSeqi NP_694793.1. NM_153153.3. [Q8K4L3-1 ]
UniGenei Mm.136791.

3D structure databases

ProteinModelPortali Q8K4L3.
SMRi Q8K4L3. Positions 1398-1640, 1712-2079, 2104-2170.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230358. 1 interaction.
IntActi Q8K4L3. 1 interaction.
MINTi MINT-4136191.

PTM databases

PhosphoSitei Q8K4L3.

Proteomic databases

MaxQBi Q8K4L3.
PaxDbi Q8K4L3.
PRIDEi Q8K4L3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025079 ; ENSMUSP00000025079 ; ENSMUSG00000024236 . [Q8K4L3-1 ]
ENSMUST00000126977 ; ENSMUSP00000115078 ; ENSMUSG00000024236 . [Q8K4L3-1 ]
ENSMUST00000140448 ; ENSMUSP00000119803 ; ENSMUSG00000024236 . [Q8K4L3-1 ]
GeneIDi 225115.
KEGGi mmu:225115.
UCSCi uc008dyr.2. mouse. [Q8K4L3-1 ]

Organism-specific databases

CTDi 6840.
MGIi MGI:2147319. Svil.

Phylogenomic databases

eggNOGi NOG324767.
GeneTreei ENSGT00660000095502.
HOGENOMi HOG000006939.
HOVERGENi HBG052980.
InParanoidi Q8K4L3.
KOi K10369.
OMAi RSHTQPI.
OrthoDBi EOG7WX07J.
PhylomeDBi Q8K4L3.
TreeFami TF316081.

Miscellaneous databases

ChiTaRSi SVIL. mouse.
NextBioi 377534.
PROi Q8K4L3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8K4L3.
Bgeei Q8K4L3.
CleanExi MM_SVIL.
Genevestigatori Q8K4L3.

Family and domain databases

Gene3Di 1.10.950.10. 1 hit.
3.40.20.10. 5 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR015628. Supervillin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
PTHR11977:SF28. PTHR11977:SF28. 1 hit.
Pfami PF00626. Gelsolin. 1 hit.
PF02209. VHP. 1 hit.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 5 hits.
SM00153. VHP. 1 hit.
[Graphical view ]
SUPFAMi SSF47050. SSF47050. 1 hit.
PROSITEi PS51089. HP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton."
    Oh S.W., Pope R.K., Smith K.P., Crowley J.L., Nebl T., Lawrence J.B., Luna E.J.
    J. Cell Sci. 116:2261-2275(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSVIL_MOUSE
AccessioniPrimary (citable) accession number: Q8K4L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi