ID U3B7Z2_CALJA Unreviewed; 1066 AA.
AC U3B7Z2; F7I9H2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Vinculin {ECO:0000256|ARBA:ARBA00014125};
DE AltName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
GN Name=VCL {ECO:0000313|EMBL:JAB08888.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB08888.1};
RN [1] {ECO:0000313|EMBL:JAB08888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB08888.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB44161.1}, and Hippocampus
RC {ECO:0000313|EMBL:JAB14432.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. 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; GAMT01002973; JAB08888.1; -; mRNA.
DR EMBL; GAMS01008704; JAB14432.1; -; mRNA.
DR EMBL; GAMP01008594; JAB44161.1; -; mRNA.
DR RefSeq; XP_002756260.1; XM_002756214.3.
DR AlphaFoldDB; U3B7Z2; -.
DR GeneID; 100410985; -.
DR CTD; 7414; -.
DR OrthoDB; 2908505at2759; -.
DR GO; GO:0005903; C:brush border; ISS:AgBase.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
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:SF1; 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; 2.
PE 2: Evidence at transcript level;
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 857..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 116750 MW; A1743384E049BA28 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGSSPVAM QKAQQVSQGL
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE
LCDDPKERDD ILRSLGEISA LTSKLADLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR VLASQLQDSL KDLKARMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGKL GATAEKAAAV GTANKSTVEG
IQASVKTARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ
//
