ID A0A2U9CMM9_SCOMX Unreviewed; 1064 AA.
AC A0A2U9CMM9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
GN ORFNames=SMAX5B_017446 {ECO:0000313|EMBL:AWP17798.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17798.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17798.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026260; AWP17798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CMM9; -.
DR STRING; 52904.ENSSMAP00000001310; -.
DR OMA; WSSKWIN; -.
DR OrthoDB; 2908505at2759; -.
DR Proteomes; UP000246464; Chromosome 18.
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:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 837..886
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"
SQ SEQUENCE 1064 AA; 116405 MW; DA05892D594F8550 CRC64;
MPVFHTKTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIM KRDMPPAFIK VENACTKLVQ AASMLKADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VESMEDLITY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPILISGIK IFVTTKTSGS QGVEEALKNR NFTFEKMSAE
INEIIRVLQL TSWDEDAWAN KDTEAMKRAL GLIDSKMGQA KNWLRDPNAQ PGDQGEQAIR
QILDEAGKVG ELCAGKERRD ILGTAKTLGQ MTDQVSEMRA RGQGAAPAAM QKAQQVSQGL
DVLTGKVENA ARKLEAMTNS KQAIAKRIDA AQNWLADPNG GPEGEENIKA LLIEAKKIAD
MCEDPKERDD ILRSIGELAA MTAKLSDLRR QGKGDTPEAR ALAKQIATAL QNLQSKTNKA
VANSRPAKAA VHLEGKIEQA QRWIDNPTID DSGVGQAAIR GLVAEGRRLA NALPGPYRQE
LLGKCEQVEQ LMAQLADLAA RGEGDSPQAR AVAQQLQEAL KDLKGKMQEA MTQEVSDIFS
DTTTPIKLLA VAATAPLDAP NRDEVFDERA VNFENHANKL GTTAEKAAAV GTANKSTVEG
IQAAVKSTRD ITPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT VLVDEAIDTK
SLLDASEEAI KKDLDKCRVA MANHQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EMVKAASDEL SQTISPMVMN AKAVAGNIQD PSLQKGFLDS GYKILGAVAK VREAFQPQEP
DFPPPPPELE QLSLNDEAAP PKPPLPEGEV PPPRPPPPEE KDEEFPEAGD MANEPMMVAA
RQLHDEARKW SSKGNDIIGA AKRMALLMAE MSRLVRGGGG NKRALIQCAK DIAKASDEVT
RLAKEVAKQC TDKRIRTNLL QVCERIPTIS TQLKILSTVK ATMLGRTNIS EEESEQATEM
LVHNAQNLMQ SVKETVREAE AASIKIRTDA GFTLHWVRKT PWYQ
//
