ID A0A3B3C5F8_ORYME Unreviewed; 1066 AA.
AC A0A3B3C5F8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000012819.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000012819.1}
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; A0A3B3C5F8; -.
DR STRING; 30732.ENSOMEP00000012819; -.
DR PaxDb; 30732-ENSOMEP00000012819; -.
DR Ensembl; ENSOMET00000032881.1; ENSOMEP00000012819.1; ENSOMEG00000014258.1.
DR GeneTree; ENSGT01030000234543; -.
DR OMA; WSSKWIN; -.
DR OrthoDB; 2908505at2759; -.
DR Proteomes; UP000261560; 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:SF5; VINCULIN; 1.
DR Pfam; PF01044; Vinculin; 1.
DR PRINTS; PR00806; VINCULIN.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 7.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 835..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 538..593
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116659 MW; 9E8D1CF03C309C20 CRC64;
MPVFHTKTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIM KRDMPPAFIK VENACTKLVQ AASMLKADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VESMEDLITY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPILISGIK IFVTTKTSGG QGVEEALKNR NFTFEKMSAE
INEIIRVLQL TSWDEDAWAN KDTEAMKRAL GLIDSKMLQA KNWLRDPNAP PGDAGEQAIR
QILDEAGKVG ELCTGKERRD IVGTAKTLGQ ITDQVSEMRA RGQGASPVAM QKAQQVSHGL
DVLTNKVENA ARKLEAMTNS KQAIAKRIDA AQNWLADPNG GPEGEENIKA LLAEAKKIAD
MCEDPKERED ALRSIAELAA MTAKLSELRR QGKGDTPEAR ALAKQIATAL QNLQSKTNKI
VANSRPAKAA VHLEGKIEQA QRWIENPTVD DNGVGQTAIR GLVAEGRRLA NALPGPYRQE
LMGKCERVEQ LMAQLADLAA RGEGDSPQAR AVAQQLQEAL KDLKGQMQEA MTQEVSDIFS
DTTTPIKLLA VAATAPLDAP NRNEVFEERA ANFENHANKL GATAEKAAAV GTANKSTVEG
IQAAVKSTRD LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KNDLDKCRVA MANHQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EVVKAASDEL SQTISPMVMS AKAVAAKIQD PSLQKGFLDS GYKILGAVAK VREAFQPPEP
DFPPPPPEID QLSLNDEAAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GDVVNEPMMV
AARQLHDEAR KWSSKGNDII GAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISEEESEQAT
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLHWVR KTPWYQ
//
