VINC_DROME
ID VINC_DROME Reviewed; 961 AA.
AC O46037;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Vinculin;
GN Name=Vinc; ORFNames=CG3299;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9280281; DOI=10.1016/s0014-5793(97)00901-0;
RA Alatortsev V.E., Kramerova I.A., Frolov M.V., Lavrov S.A., Westphal E.D.;
RT "Vinculin gene is non-essential in Drosophila melanogaster.";
RL FEBS Lett. 413:197-201(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-774, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Involved in cell adhesion. May be involved in the attachment
CC of the actin-based microfilaments to the plasma membrane.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- SUBUNIT: Exhibits self-association properties. {ECO:0000250}.
CC -!- INTERACTION:
CC O46037; A1Z866: CAP; NbExp=3; IntAct=EBI-121490, EBI-148231;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P85972}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell membrane
CC {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P12003}. Cell junction
CC {ECO:0000250|UniProtKB:P12003}. Note=Cytoplasmic face of adhesion
CC plaques. {ECO:0000250|UniProtKB:P12003}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAF45752.1; -; Genomic_DNA.
DR EMBL; AL009193; CAA15691.1; -; Genomic_DNA.
DR EMBL; AY128501; AAM75094.1; -; mRNA.
DR RefSeq; NP_001284813.1; NM_001297884.1.
DR RefSeq; NP_001284814.1; NM_001297885.1.
DR RefSeq; NP_476820.1; NM_057472.3.
DR AlphaFoldDB; O46037; -.
DR SMR; O46037; -.
DR BioGRID; 57740; 13.
DR IntAct; O46037; 7.
DR STRING; 7227.FBpp0070404; -.
DR iPTMnet; O46037; -.
DR PaxDb; O46037; -.
DR PRIDE; O46037; -.
DR DNASU; 31201; -.
DR EnsemblMetazoa; FBtr0070420; FBpp0070404; FBgn0004397.
DR EnsemblMetazoa; FBtr0342770; FBpp0309622; FBgn0004397.
DR EnsemblMetazoa; FBtr0342771; FBpp0309623; FBgn0004397.
DR GeneID; 31201; -.
DR KEGG; dme:Dmel_CG3299; -.
DR CTD; 31201; -.
DR FlyBase; FBgn0004397; Vinc.
DR VEuPathDB; VectorBase:FBgn0004397; -.
DR eggNOG; KOG3681; Eukaryota.
DR HOGENOM; CLU_012338_0_0_1; -.
DR InParanoid; O46037; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 270073at2759; -.
DR PhylomeDB; O46037; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-5674135; MAP2K and MAPK activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; O46037; -.
DR BioGRID-ORCS; 31201; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31201; -.
DR PRO; PR:O46037; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004397; Expressed in crop (Drosophila) and 25 other tissues.
DR ExpressionAtlas; O46037; baseline and differential.
DR Genevisible; O46037; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR46180; PTHR46180; 2.
DR Pfam; PF01044; Vinculin; 1.
DR SUPFAM; SSF47220; SSF47220; 6.
DR PROSITE; PS00664; VINCULIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..961
FT /note="Vinculin"
FT /id="PRO_0000064259"
FT REPEAT 258..362
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 371..470
FT /note="2"
FT /evidence="ECO:0000255"
FT REGION 258..470
FT /note="2 X repeats"
FT /evidence="ECO:0000255"
FT REGION 720..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 774
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 961 AA; 106302 MW; 17E50E11F507C875 CRC64;
MPVFHTKTIE SILDPVAQQV SRLVILHEEA EDGNAMPDLS RPVQVVSAAV ANLVKVGRDT
INSSDDKILR QDMPSALHRV EGASQLLEEA SDMLRSDPYS GPARKKLIEG SRGILQGTSS
LLLCFDESEV RKIIQECKRV LDYLAVAEVI NTMEQLVQFL KDLSPCLSKV HREVGAREKE
LTHQVHSEIL VRCLEQVKTL APILICSMKV YIHIVEQQGR GAEEAAENRN YLAARMSDEL
QEIIRVLQLT TYDEDTSELD NLTVLKKLSN AISNKMEQAN EWLSNPYALR GGVGEKALRQ
VIDNATEISE RCLPQDSYPI RKLADEVTAM ANTLCELRQE GKGQSPQAES LVRGIRDRMG
ELKSLVHQAV LGVDKAGVQQ TAHTIQGRLE QAVKWLQHPE INDGGLGERA INLIVEEGRK
VAEGCPGHQK AEIQQLCDEV ERLKRQAAGS GPAAKQAAKQ LTQKLYELKA AIQNALVNRI
VQDFMDVSTP LKQFTEAVLQ PEGTPGREQN FNQKSNNLQA FSDRASKTSR MVAAGGACGN
KKIAEILLSS AAQVDSLTPQ LISAGRIRMN YPGSKAADEH LQNLKQQYAD TVLRMRTLCD
QATDPADFIK TSEEHMQVYA KLCEDAIHAR QPQKMVDNTS NIARLINRVL LVAKQEADNS
EDPVFTERLN AAANRLERSL PAMVGDAKLV ATNIADPAAA AAWKNSFQRL LGDVREVRDA
IAPPQPPPLP TSLPPPIPEL SALHLSNQNA ERAPPRPPLP REGLAPVRPP PPETDDEDEG
VFRTMPHANQ PILIAARGLH QEVRQWSSKD NEIIAAAKRM AILMARLSEL VLSDSRGSKR
ELIATAKKIA EASEDVTRLA KELARQCTDR RIRTNLLQVC ERIPTIGTQL KILSTVKATM
LGAQGSDEDR EATEMLVGNA QNLMQSVKET VRAAEGASIK IRSDQTSNRL QWVRRQPWYQ
Y
