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Protein

Supervillin

Gene

SVIL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: Forms a high-affinity link between the actin cytoskeleton and the membrane. 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 (By similarity).By similarity
Isoform 2: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6 (PubMed:16880273, PubMed:17925381). Plays a role in cytokinesis through KIF14 interaction (PubMed:20309963).3 Publications

GO - Biological processi

  • cytoskeleton organization Source: InterPro
  • positive regulation of cytokinesis Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Supervillin1 Publication
Alternative name(s):
ArchvillinBy similarity
p205/p2501 Publication
Gene namesi
Name:SVIL1 Publication
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cleavage furrow Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • invadopodium Source: UniProtKB-SubCell
  • microtubule minus-end Source: UniProtKB
  • midbody Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • podosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi828 – 8292RY → AA: Diminishes interaction with TRIP6 and DYNLT1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21942194SupervillinPRO_0000378515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei245 – 2451PhosphoserineBy similarity
Modified residuei262 – 2621PhosphoserineBy similarity
Modified residuei321 – 3211PhosphoserineBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei652 – 6521PhosphoserineBy similarity
Modified residuei686 – 6861PhosphoserineBy similarity
Modified residuei747 – 7471PhosphoserineBy similarity
Modified residuei781 – 7811PhosphoserineBy similarity
Modified residuei829 – 8291PhosphotyrosineBy similarity
Modified residuei831 – 8311PhosphothreonineBy similarity
Modified residuei893 – 8931PhosphoserineBy similarity
Modified residuei899 – 8991PhosphoserineBy similarity
Modified residuei903 – 9031PhosphoserineBy similarity
Modified residuei947 – 9471PhosphoserineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity
Modified residuei1031 – 10311PhosphoserineBy similarity
Modified residuei1099 – 10991PhosphoserineBy similarity
Modified residuei1205 – 12051PhosphoserineBy similarity
Modified residuei1210 – 12101PhosphothreonineBy similarity
Modified residuei1214 – 12141PhosphoserineBy similarity
Modified residuei1302 – 13021PhosphoserineBy similarity
Modified residuei1385 – 13851PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO46385.
PRIDEiO46385.

Interactioni

Subunit structurei

Associates with F-actin. Interacts with NEB (By similarity). Interacts with MYH9. Interacts with MYLK. Isoform 2: Interacts with TRIP6. Isoform 2: Interacts with DYNLT1. Isoform 2: Interacts with KIF14; at midbody during cytokinesis (PubMed:20309963).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q7LZ832EBI-6995105,EBI-6995234From a different organism.
Dynlt1P518074EBI-6995105,EBI-642797From a different organism.
KIF14Q150583EBI-6995105,EBI-1045252From a different organism.
LIMA1Q9UHB63EBI-6995105,EBI-351479From a different organism.
MYH9P355792EBI-6995105,EBI-350338From a different organism.
TRIP6Q156545EBI-6995105,EBI-742327From a different organism.

Protein-protein interaction databases

IntActiO46385. 50 interactions.
MINTiMINT-7898149.
STRINGi9913.ENSBTAP00000049248.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1421 – 1520100Gelsolin-like 1Add
BLAST
Repeati1540 – 1662123Gelsolin-like 2Add
BLAST
Repeati1732 – 1842111Gelsolin-like 3Add
BLAST
Repeati1861 – 1962102Gelsolin-like 4Add
BLAST
Repeati1995 – 2102108Gelsolin-like 5Add
BLAST
Domaini2131 – 219464HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 174174Interaction with MYLKAdd
BLAST
Regioni1399 – 1667269Interaction with NEBBy 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.Curated
Contains 5 gelsolin-like repeats.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0445. Eukaryota.
ENOG410XPWY. LUCA.
InParanoidiO46385.
KOiK10369.

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. SV/p205.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF45. PTHR11977:SF45. 2 hits.
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. AlignAdd to basket

Isoform 1 (identifier: O46385-1) [UniParc]FASTAAdd to basket

Also known as: ArchvillinBy similarity

, p250By similarity

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

        10         20         30         40         50
MKRKERIARR LEGIETDTQP ILLQSCTGLV THRLLEEDTP RYMRATDPAS
60 70 80 90 100
PHIGRSNEEE ETSDSSLEKQ TRSKQCTETS GIHADSPYSS GIMDTQSLES
110 120 130 140 150
KAERIARYKA ERRRQLAEKY GLTLDPEADS ETPSRYSRSR KDPEAAEKRG
160 170 180 190 200
VRSERSAESS RDAGSSYSRT ELSGLRTCVA ESKDYGLHRS DGVSDTEVLL
210 220 230 240 250
NAENQRRGQE PSATGLARDL PLAGEVSSSF SFSGRDSALG EVPRSPKAVH
260 270 280 290 300
SLPSPSPGQP ASPSHSTSDL PLPAEARASI GKPKHEWFLQ KDSEGDTPSL
310 320 330 340 350
INWPSRVKVR EKLVREESAR SSPELTSESL TQRRHQTAPG HYLAFQSENS
360 370 380 390 400
AFDRVSGKVA SSARQPIRGY VQPAEPVHTI TLVTSDTPES ISEGSWVGPA
410 420 430 440 450
PQTVTKPPPS KVLEGERRDT PVLHICESKA EDVLFSDALE KTRKTLAVLE
460 470 480 490 500
DRGSGRSQEA PSGTEDLSQP AVGIVTAEPQ KESESLAHPP MAQQQPTERM
510 520 530 540 550
GRSEMVMYVQ SEAVSQGHRK EVPTRKHRVL TRSLSDYTGP PQLQALKAKA
560 570 580 590 600
PAPKRDAESQ TSKAELELGL LDTKVSVAQL RNAFLESARA SRKPELHSRV
610 620 630 640 650
EGSSEGPGVE RERGSRKPRR YFSPGENRKT SERFRTQPIT SAERKESDRS
660 670 680 690 700
TSNSEMPAAE DEEKVDERAR LSVAAKRLLF REMEKSFDEK SVPKRRSRNA
710 720 730 740 750
AVEQRLRRLQ DRSHTQPVTT EEVVIAAEPT PASCSVATHP VMTRHPSPTV
760 770 780 790 800
AKSPVQPART LQASAHQKAL ARDQTNESKD SAEQGEPDSS TLSLAEKLAL
810 820 830 840 850
FNKLSQPVSK AISTRNRLDM RQRRMNARYQ TQPVTLGEVE QVQSGKLMAF
860 870 880 890 900
SPTINTSVST VASTVPPMYA GNLRTKPLPD DSFGATEQKF ASSLENSDSP
910 920 930 940 950
VRSILKSQGW QPSVEGAGSK AMLREFEETE RKGGLTGGDG GVTKYGSFEE
960 970 980 990 1000
AELSYPVLSR VREGDNHKEA IYALPRKGSL ELAHPPIAQL GDDLKEFSTP
1010 1020 1030 1040 1050
KSTMQASPDW KERQLFEEKV DLENVTKRKF SLKAAEFGEP TSEQTGAAAG
1060 1070 1080 1090 1100
KPAAPTATPV SWKPQDPSEQ PQEKRYQSPC AMFAAGEIKA PAVEGSLDSP
1110 1120 1130 1140 1150
SKTMSIKERL ALLKKSGEED WRNRLNRKQE YGKASITSSL HIQETEQSLK
1160 1170 1180 1190 1200
KKRVTESRES QMTIEERKHL ITVREDAWKT RGKGAANDST QFTVAGRMVK
1210 1220 1230 1240 1250
RGLASPTAIT PVASPVSSKA RGTTPVSRPL EDIEARPDMQ LESDLKLDRL
1260 1270 1280 1290 1300
ETFLRRLNNK VGGMQETVLT VTGKSVKEVM KPDDDETFAK FYRSVDSSLP
1310 1320 1330 1340 1350
RSPVELDEDF DVIFDPYAPR LTSSVAEHKR AVRPKRRVQA SKNPLKMLAA
1360 1370 1380 1390 1400
REDLLQEYTE QRLNVAFVES KRMKVEKLSA NSSFSEVTLA GLASKENFSN
1410 1420 1430 1440 1450
VSLRSVNLTE QNSNNSAVPY KKLMLLQVKG RRHVQTRLVE PRAPSLNSGD
1460 1470 1480 1490 1500
CFLLLSPHHC FLWVGEFANV IEKAKASELA SLIQTKRELG CRATYIQTVE
1510 1520 1530 1540 1550
EGINTHTHAA KDFWKLLGGQ ASYQSAGDPK EDELYETAII ETNCIYRLMD
1560 1570 1580 1590 1600
DKLVPDDDYW GKIPKCSLLQ SKEVLVFDFG SEVYVWHGKE VTLAQRKIAF
1610 1620 1630 1640 1650
QLAKHLWNGT FDYENCDINP LDPGECNPLI PRKGQGRPDW AIFGRLTEHN
1660 1670 1680 1690 1700
ETILFKEKFL DWTELKRPNE KNASELAQHK DDARAEVKPY DVTRMVPVPQ
1710 1720 1730 1740 1750
TTAGTVLDGV NVGRGYGLVE GDDRRQFEIA SISVDVWHIL EFDYSRLPKQ
1760 1770 1780 1790 1800
SIGQFHEGDA YVVKWKFIVS TAVGSRQKGE HSVRVAGKEK CVYFFWQGRQ
1810 1820 1830 1840 1850
STVSEKGTSA LMTVELDEER GAQVQVLQGK EPPCFLQCFQ GGMVVHSGRR
1860 1870 1880 1890 1900
EEEEENTQSE WRLYCVRGEV PVEGNLLEVA CHCSSLRSRT SMVVLNVHKA
1910 1920 1930 1940 1950
LIYLWHGCKA QAHTKEVGRT AANKIKDQCP LEAGLHSSSK VTIHECDEGS
1960 1970 1980 1990 2000
EPLGFWDALG RRDRKAYDCM LQDPGNFNFT PRLFILSSSS GDFSATEFMY
2010 2020 2030 2040 2050
PARDPSVVNS MPFLQEDLYS APQPALFLVD NHHEVYLWQG WWPIENKITG
2060 2070 2080 2090 2100
SARIRWASDR KSAMETVLQY CRGKNLKKPP PKSYLIHAGL EPLTFTNMFP
2110 2120 2130 2140 2150
SWEHREDIAE ITEMDTEVSN QITLVEDVLA KLCKTIYPLA DLLARPLPEG
2160 2170 2180 2190
VDPLKLEIYL TDEDFEFALD MTRDEYNALP AWKQVNLKKA KGLF
Length:2,194
Mass (Da):244,892
Last modified:July 7, 2009 - v2
Checksum:i345C450DC2D8516C
GO
Isoform 2 (identifier: O46385-2) [UniParc]FASTAAdd to basket

Also known as: Supervillin1 Publication

, p2051 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     279-648: Missing.
     728-759: Missing.

Show »
Length:1,792
Mass (Da):200,627
Checksum:iE7683787B0187DA0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei279 – 648370Missing in isoform 2. 1 PublicationVSP_037598Add
BLAST
Alternative sequencei728 – 75932Missing in isoform 2. 1 PublicationVSP_037599Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025996 mRNA. Translation: AAC48783.1.
AAFC03127701 Genomic DNA. No translation available.
AAFC03076280 Genomic DNA. No translation available.
AAFC03076281 Genomic DNA. No translation available.
AAFC03076282 Genomic DNA. No translation available.
DV816343 mRNA. No translation available.
PIRiT08878.
RefSeqiNP_776615.1. NM_174190.2. [O46385-2]
UniGeneiBt.64122.

Genome annotation databases

GeneIDi281509.
KEGGibta:281509.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025996 mRNA. Translation: AAC48783.1.
AAFC03127701 Genomic DNA. No translation available.
AAFC03076280 Genomic DNA. No translation available.
AAFC03076281 Genomic DNA. No translation available.
AAFC03076282 Genomic DNA. No translation available.
DV816343 mRNA. No translation available.
PIRiT08878.
RefSeqiNP_776615.1. NM_174190.2. [O46385-2]
UniGeneiBt.64122.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO46385. 50 interactions.
MINTiMINT-7898149.
STRINGi9913.ENSBTAP00000049248.

Proteomic databases

PaxDbiO46385.
PRIDEiO46385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281509.
KEGGibta:281509.

Organism-specific databases

CTDi6840.

Phylogenomic databases

eggNOGiKOG0445. Eukaryota.
ENOG410XPWY. LUCA.
InParanoidiO46385.
KOiK10369.

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. SV/p205.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF45. PTHR11977:SF45. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily."
    Pestonjamasp K.N., Pope R.K., Wulfkuhle J.D., Luna E.J.
    J. Cell Biol. 139:1255-1269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION WITH ACTIN.
  2. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
    The bovine genome sequencing and analysis consortium
    Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hereford.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-712 (ISOFORM 1).
  4. "Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes."
    Nebl T., Pestonjamasp K.N., Leszyk J.D., Crowley J.L., Oh S.W., Luna E.J.
    J. Biol. Chem. 277:43399-43409(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  5. Cited for: INTERACTION WITH MYH9.
  6. Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH TRIP6 AND DYNLT1 (ISOFORM 2), MUTAGENESIS OF 828-ARG-TYR-829.
  7. "Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery."
    Takizawa N., Ikebe R., Ikebe M., Luna E.J.
    J. Cell Sci. 120:3792-3803(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH MLCK AND MYH9.
  8. "Novel interactors and a role for supervillin in early cytokinesis."
    Smith T.C., Fang Z., Luna E.J.
    Cytoskeleton 67:346-364(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH KIF14, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSVIL_BOVIN
AccessioniPrimary (citable) accession number: O46385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: July 7, 2009
Last modified: June 8, 2016
This is version 92 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.