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 01-MAY-2013, entry version 92.
DE RecName: Full=Vinculin;
GN Name=Vinc; ORFNames=CG3299;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; 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.,
RA 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.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA 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.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA 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.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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;
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.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic 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.,
RA Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
RA Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
RA Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
RA Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
RA Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
RA Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
RA 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;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., 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 MASS
RP SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
RA Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy
RT for (quantitative) phosphoproteomics: application to Drosophila
RT melanogaster Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Involved in cell adhesion. May be involved in the
CC attachment of the actin-based microfilaments to the plasma
CC membrane (By similarity).
CC -!- SUBUNIT: Exhibits self-association properties (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cell junction, adherens junction (By similarity). Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Cell junction (By similarity). Note=Cytoplasmic face of adhesion
CC plaques (By similarity).
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
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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_476820.1; NM_057472.2.
DR UniGene; Dm.32; -.
DR ProteinModelPortal; O46037; -.
DR SMR; O46037; 1-955.
DR IntAct; O46037; 2.
DR MINT; MINT-742946; -.
DR STRING; 7227.FBpp0070404; -.
DR PaxDb; O46037; -.
DR PRIDE; O46037; -.
DR EnsemblMetazoa; FBtr0070420; FBpp0070404; FBgn0004397.
DR GeneID; 31201; -.
DR KEGG; dme:Dmel_CG3299; -.
DR CTD; 31201; -.
DR FlyBase; FBgn0004397; Vinc.
DR eggNOG; NOG329927; -.
DR GeneTree; ENSGT00550000074411; -.
DR InParanoid; O46037; -.
DR KO; K05700; -.
DR OMA; ELTHQVH; -.
DR OrthoDB; EOG4M37QG; -.
DR PhylomeDB; O46037; -.
DR GenomeRNAi; 31201; -.
DR NextBio; 772430; -.
DR Bgee; O46037; -.
DR GermOnline; CG3299; Drosophila melanogaster.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:FlyBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; ISS:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR Pfam; PF01044; Vinculin; 1.
DR PRINTS; PR00806; VINCULIN.
DR SUPFAM; SSF47220; Vinculin/catenin; 6.
DR PROSITE; PS00663; VINCULIN_1; FALSE_NEG.
DR PROSITE; PS00664; VINCULIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Cell junction; Cell membrane;
KW Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1 961 Vinculin.
FT /FTId=PRO_0000064259.
FT REPEAT 258 362 1.
FT REPEAT 371 470 2.
FT REGION 258 470 2 X repeats.
FT COMPBIAS 723 772 Pro-rich.
FT MOD_RES 774 774 Phosphothreonine.
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
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