VINC_DICDI
ID VINC_DICDI Reviewed; 842 AA.
AC Q54MH2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable vinculin;
DE AltName: Full=Ddalpha-catenin;
GN Name=ctnnA; Synonyms=vcl, vinA; ORFNames=DDB_G0285939;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19065153; DOI=10.1038/cr.2008.318;
RA Nagasaki A., Kanada M., Uyeda T.Q.;
RT "Cell adhesion molecules regulate contractile ring-independent cytokinesis
RT in Dictyostelium discoideum.";
RL Cell Res. 19:236-246(2009).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH AARA, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21393547; DOI=10.1126/science.1199633;
RA Dickinson D.J., Nelson W.J., Weis W.I.;
RT "A polarized epithelium organized by beta- and alpha-catenin predates
RT cadherin and metazoan origins.";
RL Science 331:1336-1339(2011).
RN [4]
RP FUNCTION, AND INTERACTION WITH CTXA; CTXB AND RGAA.
RX PubMed=22902739; DOI=10.1016/j.devcel.2012.06.008;
RA Dickinson D.J., Robinson D.N., Nelson W.J., Weis W.I.;
RT "Alpha-catenin and IQGAP regulate myosin localization to control epithelial
RT tube morphogenesis in Dictyostelium.";
RL Dev. Cell 23:533-546(2012).
CC -!- FUNCTION: Involved in cell adhesion. Thought to play an important role
CC in cytokinesis B, probably by providing substrate adhesion and traction
CC forces. Required to organize and polarize the tip epithelium during
CC cytokinesis. Required for the normal distribution of myosin in the tip
CC epithelium. Involved in the localization of ctxA, ctxB, dcsA, exoc6 and
CC rgaA. Thought to form a complex with ctxA, ctxB, and rgaA which
CC regulates myosin accumulation to the apical plasma membrane.
CC {ECO:0000269|PubMed:19065153, ECO:0000269|PubMed:21393547,
CC ECO:0000269|PubMed:22902739}.
CC -!- SUBUNIT: Monomer. Associates with F-actin. Interacts with aarA, ctxA,
CC ctxB and rgaA. {ECO:0000269|PubMed:21393547,
CC ECO:0000269|PubMed:22902739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19065153}. Cell junction
CC {ECO:0000269|PubMed:21393547}. Note=Localized during interphase over
CC the cell basal surface with levels decreasing at the basal surface when
CC cells enter the mitotic phase. At this time, there is intense
CC localization along the polar edges (PubMed:19065153). Also found at
CC cell-cell contacts in the slug and fruiting body and in columnar cells
CC of the tip epithelium (PubMed:21393547). {ECO:0000269|PubMed:19065153,
CC ECO:0000269|PubMed:21393547}.
CC -!- TISSUE SPECIFICITY: Epithelium. {ECO:0000269|PubMed:21393547}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout lifespan; expressed at low
CC levels in single cells but increased during multicellular development,
CC peaking at 10 h. {ECO:0000269|PubMed:19065153}.
CC -!- DISRUPTION PHENOTYPE: Cytokinetic defects when knocked out with mhcA.
CC Aberrant epithelial organization and localization of exoc6. Mis-
CC localization of myosin in the tip epithelium causing actomyosin ring
CC malformation in stalk, which appears significantly wider. Distribution
CC of Golgi and centrosomes not polarized. Abnormal intracellular
CC distribution of dcsA. {ECO:0000269|PubMed:19065153,
CC ECO:0000269|PubMed:21393547}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000082; EAL64504.1; -; Genomic_DNA.
DR RefSeq; XP_638018.1; XM_632926.1.
DR AlphaFoldDB; Q54MH2; -.
DR SMR; Q54MH2; -.
DR STRING; 44689.DDB0232320; -.
DR PaxDb; Q54MH2; -.
DR PRIDE; Q54MH2; -.
DR EnsemblProtists; EAL64504; EAL64504; DDB_G0285939.
DR GeneID; 8625369; -.
DR KEGG; ddi:DDB_G0285939; -.
DR dictyBase; DDB_G0285939; ctnnA.
DR eggNOG; KOG3681; Eukaryota.
DR HOGENOM; CLU_338163_0_0_1; -.
DR InParanoid; Q54MH2; -.
DR OMA; ANNLCEL; -.
DR PhylomeDB; Q54MH2; -.
DR PRO; PR:Q54MH2; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045180; C:basal cortex; IDA:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:dictyBase.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IPI:dictyBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:dictyBase.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:dictyBase.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IMP:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0140509; P:epithelium-like organization; IMP:dictyBase.
DR GO; GO:0061245; P:establishment or maintenance of bipolar cell polarity; IMP:dictyBase.
DR GO; GO:0051645; P:Golgi localization; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IGI:dictyBase.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0008104; P:protein localization; IMP:dictyBase.
DR GO; GO:0009306; P:protein secretion; IMP:dictyBase.
DR GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP:dictyBase.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR46180; PTHR46180; 1.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Cell junction; Coiled coil; Cytoplasm;
KW Reference proteome.
FT CHAIN 1..842
FT /note="Probable vinculin"
FT /id="PRO_0000333271"
FT COILED 585..679
FT /evidence="ECO:0000255"
SQ SEQUENCE 842 AA; 92839 MW; 4EF7513D65DA1AC3 CRC64;
MDEVLEMIAD AVSSLVVAIT DSEEKNTLFG DMVPGVELIQ QAVNGMAEAA EETVSLIDEE
FIGQLESTSK QLKNSAGQLY VHAVRAREDP WNRVPQKDAI KAAKQILQNV VLLVLIEEQS
NIKVLVNIAK KAAEGVRRID EIENIKQLDV MIGDVNQLQN ELVKRSQRRS EGSHNPELRS
KLEDIATMVN ILSEQHQASA RDVCRNPREE TLRSKRSELS SKLLSAIDDL IYTIKLIFEN
NTKFVDLAFK WKPVRTMAED EVTRASAVLI DNLRTLPKSI EAGNGPAAAR EIVNAANLQI
SNAIIVANRC QDPVKKKMLL KQIEELKKLT PMLISAMKPV LENPNDQEAQ KHLESVIYST
QKASEALATA VVSSPAEIVA ASGVSLARDL DSLEEAIASG DKKRAQVILS HIPSAIDKHI
ELANALLETI TDPGQRHQIK QSIERLQTLK PRIIENANRA IANPNDHEAR KNLSSDIKEA
KKAIGQISQP YEVVSALNTK IHNDLDSLIK CIDEGGPDMQ VKGVQYAKDI ANSIKKQIEA
AEAYAQTITD PDRKKQVLDS IEQLKKLTPQ LLEAIRACLA NPDDKEARKR LDDVVRRVKE
ASSNLSQVIQ PTADELKEEK RKRNEEIARI EAEEKAKARA LLKAAELARI EAEEEKKRLA
IIEEEKKRLA AEEEERKRAP KLVVPEGPVN KAVFGAAADV AQALESKVRD GTPLGILVQL
SDEIAQQMAL IASFAMNGDV KGMITAARKI ADTIKQVQTQ AKHIADNCTD PRLKQNVLTY
CDCGGNFSTQ LKILCAVKSN DFNDPTAEEQ LVTCAKGLSG AVINLVKSSE AASIKQRKVP
QQ
