ID A0A3Q2W139_HAPBU Unreviewed; 1066 AA.
AC A0A3Q2W139;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000014703.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000014703.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005919689.1; XM_005919627.2.
DR AlphaFoldDB; A0A3Q2W139; -.
DR STRING; 8153.ENSHBUP00000014703; -.
DR Ensembl; ENSHBUT00000022763.1; ENSHBUP00000014703.1; ENSHBUG00000016612.1.
DR GeneID; 102295228; -.
DR GeneTree; ENSGT01030000234543; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 2908505at2759; -.
DR Proteomes; UP000264840; 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 Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 837..892
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; 116689 MW; 11F6C4AFDE3D947F CRC64;
MPVFHTKTIE SILEPVAQQI SHLVIMHEEG EVDGKGIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQLM KRDMPPAFIK VENACAKLVQ AASMLKADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRRIIRVCRG ILEYLAVAEV VESMEDLITY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPILISGIK IYVTTKTSES HGVEEALKNR NFTFEKMSAE
INEIIRVLQL TSWDEDAWAN KDTEAMKRAL GLIDSKMAQA KNWLRDPNAQ PGDAGEQAIR
QILDEAGKVG ELCAGTERRD IVGTAKTLSQ MTDQVSEMRA RGHGASPVAM QKAQQVSQGL
DVLTGKVENA ARKLEAMTNS KQAIAKRIDA AQNWLADPNS GTEGEENVKA VLMEARKIAD
MCEDPKERDD IMRSVGEIAA MTAKLSDLRR QGKGDTPEAR ALAKQIATAL QNLQSKTNKA
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DSGVGQAAIR GLVAEGHRLA NALPGPYRQE
LLGKCEQVEQ LMAQLADLAA RGEGDSPQAR AVAQQLQAAL KDLKGKMQEA MTQEVSDIFS
DTTTPIKLLA VAATAPLDAP NRDEVFDERA ANFENHANKL GTTAEKAAAV GTANKSTVEG
IQAAVKSTRD LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEDAI KKDLDKCRVA MTNHQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EVVKAASDEL SQTISPMVMN AKAVAGNIQD PSLQKGFLDS GYKILGAVAK VREAFQPQEP
DFPPPPPELD QLNLNDEAAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GDMVNEPMMV
AARQLHDEAR KWSSKGNDII GAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISEEESEQAT
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLHWVR KTPWYQ
//
