Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Vinculin

Gene

Vinc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: FlyBase
  • structural molecule activity Source: InterPro

GO - Biological processi

  • cell adhesion Source: FlyBase
  • cytoskeletal anchoring at plasma membrane Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • phagocytosis Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-DME-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Gene namesi
Name:Vinc
ORF Names:CG3299
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004397. Vinc.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: InterPro
  • cytoplasm Source: UniProtKB-KW
  • focal adhesion Source: FlyBase
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 961961VinculinPRO_0000064259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei774 – 7741Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO46037.
PRIDEiO46037.

PTM databases

iPTMnetiO46037.

Expressioni

Gene expression databases

BgeeiO46037.
ExpressionAtlasiO46037. differential.
GenevisibleiO46037. DM.

Interactioni

Subunit structurei

Exhibits self-association properties.By similarity

GO - Molecular functioni

  • actin binding Source: FlyBase

Protein-protein interaction databases

BioGridi57740. 10 interactions.
IntActiO46037. 4 interactions.
MINTiMINT-742946.
STRINGi7227.FBpp0070404.

Structurei

3D structure databases

ProteinModelPortaliO46037.
SMRiO46037. Positions 1-945.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati258 – 3621051Add
BLAST
Repeati371 – 4701002Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 4702132 X repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi723 – 77250Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
InParanoidiO46037.
KOiK05700.
OMAiTPGREQN.
OrthoDBiEOG73NG2V.
PhylomeDBiO46037.

Family and domain databases

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 4 hits.
PfamiPF01044. Vinculin. 1 hit.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 7 hits.
PROSITEiPS00664. VINCULIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O46037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVFHTKTIE SILDPVAQQV SRLVILHEEA EDGNAMPDLS RPVQVVSAAV
60 70 80 90 100
ANLVKVGRDT INSSDDKILR QDMPSALHRV EGASQLLEEA SDMLRSDPYS
110 120 130 140 150
GPARKKLIEG SRGILQGTSS LLLCFDESEV RKIIQECKRV LDYLAVAEVI
160 170 180 190 200
NTMEQLVQFL KDLSPCLSKV HREVGAREKE LTHQVHSEIL VRCLEQVKTL
210 220 230 240 250
APILICSMKV YIHIVEQQGR GAEEAAENRN YLAARMSDEL QEIIRVLQLT
260 270 280 290 300
TYDEDTSELD NLTVLKKLSN AISNKMEQAN EWLSNPYALR GGVGEKALRQ
310 320 330 340 350
VIDNATEISE RCLPQDSYPI RKLADEVTAM ANTLCELRQE GKGQSPQAES
360 370 380 390 400
LVRGIRDRMG ELKSLVHQAV LGVDKAGVQQ TAHTIQGRLE QAVKWLQHPE
410 420 430 440 450
INDGGLGERA INLIVEEGRK VAEGCPGHQK AEIQQLCDEV ERLKRQAAGS
460 470 480 490 500
GPAAKQAAKQ LTQKLYELKA AIQNALVNRI VQDFMDVSTP LKQFTEAVLQ
510 520 530 540 550
PEGTPGREQN FNQKSNNLQA FSDRASKTSR MVAAGGACGN KKIAEILLSS
560 570 580 590 600
AAQVDSLTPQ LISAGRIRMN YPGSKAADEH LQNLKQQYAD TVLRMRTLCD
610 620 630 640 650
QATDPADFIK TSEEHMQVYA KLCEDAIHAR QPQKMVDNTS NIARLINRVL
660 670 680 690 700
LVAKQEADNS EDPVFTERLN AAANRLERSL PAMVGDAKLV ATNIADPAAA
710 720 730 740 750
AAWKNSFQRL LGDVREVRDA IAPPQPPPLP TSLPPPIPEL SALHLSNQNA
760 770 780 790 800
ERAPPRPPLP REGLAPVRPP PPETDDEDEG VFRTMPHANQ PILIAARGLH
810 820 830 840 850
QEVRQWSSKD NEIIAAAKRM AILMARLSEL VLSDSRGSKR ELIATAKKIA
860 870 880 890 900
EASEDVTRLA KELARQCTDR RIRTNLLQVC ERIPTIGTQL KILSTVKATM
910 920 930 940 950
LGAQGSDEDR EATEMLVGNA QNLMQSVKET VRAAEGASIK IRSDQTSNRL
960
QWVRRQPWYQ Y
Length:961
Mass (Da):106,302
Last modified:June 1, 1998 - v1
Checksum:i17E50E11F507C875
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF45752.1.
AL009193 Genomic DNA. Translation: CAA15691.1.
AY128501 mRNA. Translation: AAM75094.1.
RefSeqiNP_001284813.1. NM_001297884.1.
NP_001284814.1. NM_001297885.1.
NP_476820.1. NM_057472.3.
UniGeneiDm.32.

Genome annotation databases

EnsemblMetazoaiFBtr0070420; FBpp0070404; FBgn0004397.
FBtr0342770; FBpp0309622; FBgn0004397.
FBtr0342771; FBpp0309623; FBgn0004397.
GeneIDi31201.
KEGGidme:Dmel_CG3299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF45752.1.
AL009193 Genomic DNA. Translation: CAA15691.1.
AY128501 mRNA. Translation: AAM75094.1.
RefSeqiNP_001284813.1. NM_001297884.1.
NP_001284814.1. NM_001297885.1.
NP_476820.1. NM_057472.3.
UniGeneiDm.32.

3D structure databases

ProteinModelPortaliO46037.
SMRiO46037. Positions 1-945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57740. 10 interactions.
IntActiO46037. 4 interactions.
MINTiMINT-742946.
STRINGi7227.FBpp0070404.

PTM databases

iPTMnetiO46037.

Proteomic databases

PaxDbiO46037.
PRIDEiO46037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070420; FBpp0070404; FBgn0004397.
FBtr0342770; FBpp0309622; FBgn0004397.
FBtr0342771; FBpp0309623; FBgn0004397.
GeneIDi31201.
KEGGidme:Dmel_CG3299.

Organism-specific databases

CTDi31201.
FlyBaseiFBgn0004397. Vinc.

Phylogenomic databases

eggNOGiKOG3681. Eukaryota.
ENOG410XSRU. LUCA.
InParanoidiO46037.
KOiK05700.
OMAiTPGREQN.
OrthoDBiEOG73NG2V.
PhylomeDBiO46037.

Enzyme and pathway databases

ReactomeiR-DME-114608. Platelet degranulation.

Miscellaneous databases

GenomeRNAii31201.
NextBioi772430.
PROiO46037.

Gene expression databases

BgeeiO46037.
ExpressionAtlasiO46037. differential.
GenevisibleiO46037. DM.

Family and domain databases

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 4 hits.
PfamiPF01044. Vinculin. 1 hit.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 7 hits.
PROSITEiPS00664. VINCULIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-774, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiVINC_DROME
AccessioniPrimary (citable) accession number: O46037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.