ID   A0A3B3UPT5_9TELE        Unreviewed;      1066 AA.
AC   A0A3B3UPT5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000015380.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000015380.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Actin filament (F-actin)-binding protein involved in cell-
CC       matrix adhesion and cell-cell adhesion. Regulates cell-surface E-
CC       cadherin expression and potentiates mechanosensing by the E-cadherin
CC       complex. May also play important roles in cell morphology and
CC       locomotion. {ECO:0000256|ARBA:ARBA00024757}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004413}. Cell projection, podosome
CC       {ECO:0000256|ARBA:ARBA00004188}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC       {ECO:0000256|ARBA:ARBA00008376}.
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DR   AlphaFoldDB; A0A3B3UPT5; -.
DR   Ensembl; ENSPLAT00000024003.1; ENSPLAP00000015380.1; ENSPLAG00000019355.1.
DR   GeneTree; ENSGT01030000234543; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 2.
DR   Gene3D; 1.20.120.810; Vinculin, Vh2 four-helix bundle; 3.
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; VINCULIN; 1.
DR   PANTHER; PTHR46180:SF4; VINCULIN; 1.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00806; VINCULIN.
DR   SUPFAM; SSF47220; alpha-catenin/vinculin-like; 7.
DR   PROSITE; PS00663; VINCULIN_1; 1.
DR   PROSITE; PS00664; VINCULIN_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REGION          836..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..873
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1066 AA;  117015 MW;  D2EE5D4A37F83724 CRC64;
     MPVFHTKTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL SVPVAAVQAA VSNLVRVGKE
     TVQTTEDQVM KRDMPPAFIK VENSCSKLVQ AAQMLKADPY SVPARDYLID GSRGILSGTS
     DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLITY TKNLGPGMTK MSKMIEERQQ
     ELTHQEHRQM LVSSMNTIKE LLPVLISAIK IFVATKSSRG AGIEEAEKNR RFTFEKMSAE
     ISEIIRVLQL TTWDEDAWAN KDMEALKRSL ALIESKMVQA KSWLKDPQGQ PGDPGEVALR
     VILDEAGKVG ELCAGRERKD ILATSRALGQ MTDQIGDLRV RGQGQTPGCM QRAGQCLQGL
     DLLFGKVDSA ARRLEALINA KQAIARRLDA AQAWLADPNG GPEGEENIRA LLAEAKRIAD
     LCEDPKERDD ILRSINEIAG LTARLMELRK QGKGDSPEAR ALAKQIGAAL LNLQSKTNRA
     VANMRPAKPA VTLEGKMEQA LRWVNNPGVD DRGVGQAAIR GMVGEGKRLA GGLLGPYRQD
     MVGRCDRTEG LMTALADMAN RGEAEAPHAR ATAAQLQDTL KDLRQHMQEV MTQEVSDVFS
     DTTTPVKLLA VAATAPPDAP NRQEVFEERA GNFETHAGRL GATAEKAAAV GTANKSTVEG
     IHAAVKHARE LTPQVTSAAR ILLKNPGNKA AYEHFDTMKN QWIDNVERLT GLVDEAIDTK
     SLLDASEEAI KKDIDKCRVA MANVQPQMLV AGATSIARRA NRVLLVAKRE VENSEDPRFR
     DTVKHASDIL SHTISPMVMD AKAVAGNIQD KGLQKAYLDS CQRILAAVGK VREAFQPQEP
     DFPPPPPDLD QLHVSDEQAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKV GEVLSEPMMV
     AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE
     VTRLAKEVAK QCTDRRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISEEESEQAT
     EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ
//