VINC_CAEEL
ID VINC_CAEEL Reviewed; 1090 AA.
AC P19826; Q8MPS2; Q9BI31; Q9BI32; V6CJ36; V6CK82; V6CLG2; V6CLK1; V6CLL2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Vinculin;
DE AltName: Full=P107B;
GN Name=deb-1 {ECO:0000312|WormBase:ZC477.9d};
GN ORFNames=ZC477.9 {ECO:0000312|WormBase:ZC477.9d};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=2498337; DOI=10.1016/s0021-9258(18)81782-3;
RA Barstead R.J., Waterston R.H.;
RT "The basal component of the nematode dense-body is vinculin.";
RL J. Biol. Chem. 264:10177-10185(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17326220; DOI=10.1002/dvdy.21091;
RA Ono K., Yu R., Ono S.;
RT "Structural components of the nonstriated contractile apparatuses in the
RT Caenorhabditis elegans gonadal myoepithelial sheath and their essential
RT roles for ovulation.";
RL Dev. Dyn. 236:1093-1105(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20385102; DOI=10.1016/j.bbrc.2010.04.049;
RA Zaidel-Bar R., Miller S., Kaminsky R., Broday L.;
RT "Molting-specific downregulation of C. elegans body-wall muscle attachment
RT sites: the role of RNF-5 E3 ligase.";
RL Biochem. Biophys. Res. Commun. 395:509-514(2010).
RN [5]
RP INTERACTION WITH SORB-1, AND SUBCELLULAR LOCATION.
RX PubMed=28978740; DOI=10.1091/mbc.e16-06-0455;
RA Loveless T., Qadota H., Benian G.M., Hardin J.;
RT "Caenorhabditis elegans SORB-1 localizes to integrin adhesion sites and is
RT required for organization of sarcomeres and mitochondria in myocytes.";
RL Mol. Biol. Cell 28:3621-3633(2017).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31411810; DOI=10.1111/febs.15039;
RA Ono K., Qin Z., Johnsen R.C., Baillie D.L., Ono S.;
RT "Kettin, the large actin-binding protein with multiple immunoglobulin
RT domains, is essential for sarcomeric actin assembly and larval development
RT in Caenorhabditis elegans.";
RL FEBS J. 287:659-670(2020).
CC -!- FUNCTION: Involved in cell adhesion (PubMed:20385102). May be involved
CC in the attachment of the actin-based microfilaments to the plasma
CC membrane (PubMed:17326220, PubMed:31411810). Involved in ovulation
CC (PubMed:17326220). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:31411810}.
CC -!- SUBUNIT: May interact with sorb-1. {ECO:0000269|PubMed:28978740}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell membrane
CC {ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:28978740}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
CC junction {ECO:0000269|PubMed:20385102}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:20385102}. Note=Cytoplasmic face of adhesion
CC plaques (By similarity). In myoepithelial sheath cells, colocalizes in
CC dense body-like structures with actin thin filaments and pat-3
CC (PubMed:17326220). In body wall muscles, localizes to integrin adhesion
CC structures (M line and dense bodies) (PubMed:20385102). Requires unc-95
CC for the localization to nascent muscle attachments during embryogenesis
CC (PubMed:20385102). Co-localizes with sorb-1 at dense bodies
CC (PubMed:28978740). {ECO:0000250|UniProtKB:P12003,
CC ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:20385102,
CC ECO:0000269|PubMed:28978740}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=d {ECO:0000312|WormBase:ZC477.9d};
CC IsoId=P19826-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZC477.9a};
CC IsoId=P19826-2; Sequence=VSP_060229;
CC Name=b {ECO:0000312|WormBase:ZC477.9b};
CC IsoId=P19826-3; Sequence=VSP_060228;
CC Name=c {ECO:0000312|WormBase:ZC477.9c};
CC IsoId=P19826-4; Sequence=VSP_060229, VSP_060230;
CC Name=e {ECO:0000312|WormBase:ZC477.9e};
CC IsoId=P19826-5; Sequence=VSP_060230;
CC Name=f {ECO:0000312|WormBase:ZC477.9f};
CC IsoId=P19826-6; Sequence=VSP_060228, VSP_060230;
CC Name=g {ECO:0000312|WormBase:ZC477.9g};
CC IsoId=P19826-7; Sequence=VSP_060227, VSP_060230;
CC Name=h {ECO:0000312|WormBase:ZC477.9h};
CC IsoId=P19826-8; Sequence=VSP_060227;
CC -!- TISSUE SPECIFICITY: Expressed in gonadal sheath cells and the
CC spermatheca (PubMed:17326220). Expressed in body wall muscles
CC (PubMed:20385102). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:20385102}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult animals.
CC {ECO:0000269|PubMed:20385102}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an accumulation in
CC the proximal gonad of endomitotic mature oocytes in 30 percent of
CC animals (PubMed:17326220). RNAi-mediated knockdown disrupts the
CC assembly of actin into myofibrils, and furthermore reduces the co-
CC localization of ketn-1 and actin in early embryos (PubMed:31411810).
CC {ECO:0000269|PubMed:31411810}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; J04804; AAA28002.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD66633.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD66634.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD66635.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13445.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13446.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13447.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13448.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13449.1; -; Genomic_DNA.
DR PIR; A33509; A33509.
DR RefSeq; NP_001293743.1; NM_001306814.1. [P19826-1]
DR RefSeq; NP_001293744.1; NM_001306815.1. [P19826-5]
DR RefSeq; NP_001293745.1; NM_001306816.1. [P19826-6]
DR RefSeq; NP_001293746.1; NM_001306817.1.
DR RefSeq; NP_001293747.1; NM_001306818.1.
DR RefSeq; NP_501104.2; NM_068703.5. [P19826-2]
DR RefSeq; NP_501105.2; NM_068704.5. [P19826-3]
DR RefSeq; NP_741437.1; NM_171374.4. [P19826-4]
DR AlphaFoldDB; P19826; -.
DR SMR; P19826; -.
DR BioGRID; 42601; 15.
DR IntAct; P19826; 3.
DR STRING; 6239.ZC477.9a; -.
DR iPTMnet; P19826; -.
DR EPD; P19826; -.
DR PaxDb; P19826; -.
DR PeptideAtlas; P19826; -.
DR EnsemblMetazoa; ZC477.9a.1; ZC477.9a.1; WBGene00000942. [P19826-2]
DR EnsemblMetazoa; ZC477.9b.1; ZC477.9b.1; WBGene00000942. [P19826-3]
DR EnsemblMetazoa; ZC477.9c.1; ZC477.9c.1; WBGene00000942. [P19826-4]
DR EnsemblMetazoa; ZC477.9d.1; ZC477.9d.1; WBGene00000942. [P19826-1]
DR EnsemblMetazoa; ZC477.9e.1; ZC477.9e.1; WBGene00000942. [P19826-5]
DR EnsemblMetazoa; ZC477.9f.1; ZC477.9f.1; WBGene00000942. [P19826-6]
DR EnsemblMetazoa; ZC477.9g.1; ZC477.9g.1; WBGene00000942. [P19826-7]
DR EnsemblMetazoa; ZC477.9h.1; ZC477.9h.1; WBGene00000942. [P19826-8]
DR GeneID; 177482; -.
DR KEGG; cel:CELE_ZC477.9; -.
DR UCSC; ZC477.9b; c. elegans.
DR CTD; 177482; -.
DR WormBase; ZC477.9a; CE31396; WBGene00000942; deb-1. [P19826-2]
DR WormBase; ZC477.9b; CE31397; WBGene00000942; deb-1. [P19826-3]
DR WormBase; ZC477.9c; CE31398; WBGene00000942; deb-1. [P19826-4]
DR WormBase; ZC477.9d; CE49192; WBGene00000942; deb-1. [P19826-1]
DR WormBase; ZC477.9e; CE49210; WBGene00000942; deb-1. [P19826-5]
DR WormBase; ZC477.9f; CE49354; WBGene00000942; deb-1. [P19826-6]
DR WormBase; ZC477.9g; CE49463; WBGene00000942; deb-1. [P19826-7]
DR WormBase; ZC477.9h; CE49419; WBGene00000942; deb-1. [P19826-8]
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_012338_0_0_1; -.
DR InParanoid; P19826; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 270073at2759; -.
DR PhylomeDB; P19826; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; P19826; -.
DR PRO; PR:P19826; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000942; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0097433; C:dense body; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
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:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
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; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Reference proteome;
KW Repeat.
FT CHAIN 1..1090
FT /note="Vinculin"
FT /id="PRO_0000064258"
FT REPEAT 339..446
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 455..561
FT /note="2"
FT /evidence="ECO:0000255"
FT REGION 339..561
FT /note="2 X repeats"
FT /evidence="ECO:0000255"
FT REGION 811..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..885
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..858
FT /note="Missing (in isoform g and isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_060227"
FT VAR_SEQ 3..767
FT /note="VFHTKTIENILEPVAQQLHYVLAMAEKNATSVDEVRHLGTSMPNLDRFASRS
FT ALALSRASSRRSIPEYITPDTVRHVVNDDDCPVCQLMMPRGKDGCVSRLVILHEEANDG
FT NAMPDLTGPVGMVSRAVGNLIQVGYDTCDHSDDRILQQDMPPALQRVEGSSKLLEESSY
FT SLKHDPYSVPARKKLIDGARGILQGTSALLLCFDESEVRKIIRVCRKANDYVAVSEVIE
FT SMADLQQFVKDISPVLHDVTNDVNLRQQELTHQVHREILIRCMDSIKVIAPILICSMKT
FT SIELGTPHPRQGHAEAIANRNFMSQRMTEEMNEIIRVLQLTTYDEDEWDADNVTVMRKA
FT LSAAKSLLTAALDWLADPHARSGAVGEKAIRRICEYADRISARALPEDAQSIKRSIFEI
FT TSFTDELCNLRNNGQPDRENLAAQTARRLKDLVGSQNSSGLMGDALQNAQRHGGANPAH
FT TAAGRLEQALRWLDNPGLDDGGLGLQALRLLTADARKLADRLNPQDRNRLLGLCSDIDR
FT LAAQLADLERRGLGNSPEAHQIRNQLKNALRDLGDFMRRVLTDRVVDDFADITTPLKQF
FT VEAVHADPYDPNREQNFVDKSQRLTDHSQSMTTTARLVASCGPSKSKKTVEAILDTAEK
FT VEQLTPQLVNAGRVRLHNPGSEQHFENIHKQYADALHRLRSHVDDAIDTGEFVRASETA
FT MRRYTNHCEGAINGADAHGLVNNSSQIARLGNRVLMTAQNEADNSEEPSFVSRVRNAAD
FT QLHNA -> INRYSSSVSDHYDSSDEYDNYSEQNYEYVYKTRLVPFNPQVLIT (in
FT isoform b and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_060228"
FT VAR_SEQ 20..99
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060229"
FT VAR_SEQ 1024..1035
FT /note="NVIGPYGQPVEG -> S (in isoform c, isoform e, isoform
FT f and isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060230"
SQ SEQUENCE 1090 AA; 120779 MW; D3432083F942AB7B CRC64;
MPVFHTKTIE NILEPVAQQL HYVLAMAEKN ATSVDEVRHL GTSMPNLDRF ASRSALALSR
ASSRRSIPEY ITPDTVRHVV NDDDCPVCQL MMPRGKDGCV SRLVILHEEA NDGNAMPDLT
GPVGMVSRAV GNLIQVGYDT CDHSDDRILQ QDMPPALQRV EGSSKLLEES SYSLKHDPYS
VPARKKLIDG ARGILQGTSA LLLCFDESEV RKIIRVCRKA NDYVAVSEVI ESMADLQQFV
KDISPVLHDV TNDVNLRQQE LTHQVHREIL IRCMDSIKVI APILICSMKT SIELGTPHPR
QGHAEAIANR NFMSQRMTEE MNEIIRVLQL TTYDEDEWDA DNVTVMRKAL SAAKSLLTAA
LDWLADPHAR SGAVGEKAIR RICEYADRIS ARALPEDAQS IKRSIFEITS FTDELCNLRN
NGQPDRENLA AQTARRLKDL VGSQNSSGLM GDALQNAQRH GGANPAHTAA GRLEQALRWL
DNPGLDDGGL GLQALRLLTA DARKLADRLN PQDRNRLLGL CSDIDRLAAQ LADLERRGLG
NSPEAHQIRN QLKNALRDLG DFMRRVLTDR VVDDFADITT PLKQFVEAVH ADPYDPNREQ
NFVDKSQRLT DHSQSMTTTA RLVASCGPSK SKKTVEAILD TAEKVEQLTP QLVNAGRVRL
HNPGSEQHFE NIHKQYADAL HRLRSHVDDA IDTGEFVRAS ETAMRRYTNH CEGAINGADA
HGLVNNSSQI ARLGNRVLMT AQNEADNSEE PSFVSRVRNA ADQLHNAIPP MVNNAKQIAQ
NPHDQYAAQN WRGTNDHLLN SVRAVGDAIT GVPMSNGRHS SYQESISRAS PYNPPPPSSQ
VIRSVNASPP TAPIIHNKMI IREDIPAPPR PPPPVELSPP PRPPPPPEYD EEEETRAFWE
RYPLPQASHQ PMLAAAHNLH NELKQWSSQE NDIVAAAKRM AILMARLSQL VRGEGGTKKD
LINCSKAIAD SSEEVTRLAV QLARLCTDIK MRTALLQVSE RIPTIATQLK VLSTVKATML
GSANVIGPYG QPVEGSEEDD EAMQQLVHNA QNLMQSVKDV VRAAEAASIK IRTNSGLRLR
WLRKPMWSNF
