ID A0A3B3Y110_9TELE Unreviewed; 1066 AA.
AC A0A3B3Y110;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000021042.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000021042.1}
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 RefSeq; XP_014859997.1; XM_015004511.1.
DR AlphaFoldDB; A0A3B3Y110; -.
DR STRING; 48701.ENSPMEP00000021042; -.
DR Ensembl; ENSPMET00000016239.1; ENSPMEP00000021042.1; ENSPMEG00000000981.1.
DR GeneID; 106928330; -.
DR KEGG; pmei:106928330; -.
DR CTD; 100334859; -.
DR OrthoDB; 2908505at2759; -.
DR Proteomes; UP000261480; 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; 6.
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 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 837..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..894
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116600 MW; 5B37A725FDB114F7 CRC64;
MPVFHTKTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL SAPVAAVQAA VSNLVRVGKD
TVQTTEDQIM KRDMPPAFIK VENACTKLVQ AASMLKADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLSVAEV VESMEDLITY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPILISGIK IFVTTKTSGS QGVEEALKNR NFTYEKMSAE
INEIIRVLQL TSWDEDAWAN KDTEAMKRAL GLIDSKMAQA KSWLRDPNAP PGDAGEQAVR
QILDEAGKVG ELCAGKERRD ILGTAKTLGQ MTDQVSEMRA RGQGASPAAM QKAQQVSQGL
DVLAGKVGNA ARKLEAMTNS KQAIAKRIDA AQGWLADPHG SPEGEENIKA LLNEARKIAD
MCEDPKEREE ILRSAGELAA MTAKLSELRR QGKGDTPEAR ALAKQIATAL QNLQSKTNKA
VANSRPAKAA VHLEGKTEQA QRWIDNPTVD DSGVGQAAIR GLVAEGRRLA NALQGPYRQE
LMGKCEQVEQ LMAQLADLAA RGEGDTPQAR AVAQQLQEAL KDLKGKMQEA MTQEVSDIFS
DTTTPIKLLA VAATAPLDAP NRDEVFEDRA ANFENHANRL GATAEKAAAV GTANKSTVEG
IQAAVKSTRD LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT VLVDEAIDTK
SLLDASEDAI KKDLDKCRVA MTNHQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EMVKAASDEL SQTISPMVMN AKAVAGNIQD PNLQKGFLDS GYKILGAVAK VREAFQPQEP
DFPPPPPELD QLNLNDEAAP PKPPLPEGEV PPPRPPPPEE KDEEFPEHKA GEKVNEPMMV
AARQLHDEAR KWSSKGNDII GAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISEEESEQAT
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLHWVR KTPWYQ
//
