ID A0A093HJ13_STRCA Unreviewed; 1020 AA.
AC A0A093HJ13;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Vinculin {ECO:0000256|ARBA:ARBA00014125};
DE AltName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
DE Flags: Fragment;
GN ORFNames=N308_00249 {ECO:0000313|EMBL:KFV79405.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV79405.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV79405.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV79405.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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, 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; KL206163; KFV79405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HJ13; -.
DR STRING; 441894.ENSSCUP00000008234; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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; 7.
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:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 791..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..341
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 813..827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV79405.1"
FT NON_TER 1020
FT /evidence="ECO:0000313|EMBL:KFV79405.1"
SQ SEQUENCE 1020 AA; 112204 MW; 01B08447B96C0488 CRC64;
LLQVGKETVQ TTEDQILKRD MPPAFIKVEN ACTKLVRAAQ MLQADPYSVP ARDYLIDGSR
GILSGTSDLL LTFDEAEVRK IIRVCKGILE YLTVAEVVET MEDLVTYTKN LGPVMCRLCC
QDLKEECKLS FIFLPLLLNR TVLQNTSYEY ILLPSLYPFY KAMKIFVTTK NSKSHGIEEA
LKNRNFTVEK MSAEINEIIR VLQLTSWDED AWASKDTEAM KRALALIDSK MNQAKGWLRD
PNAPPGDAGE QAIRQILDEA GKAGELCAGK ERREILGTCK TLGQMTDQVA DLRARGQGAT
PMAMQKAQQV SQGLDLLTAK VENAARKLEA MTNSKQAIAK KIDAAQNWLA DPNGGSEGEE
HIRGIMAEAR KVAELCEEPK ERDDILRSLG EISALTAKLS DLRRHGKGDS PEARALAKQI
ATSLQNLQSK TNRAVANTRP VKAAVHLEGK IEQAQRWIDN PTVDDRGVGQ AAIRGLVAEG
RRLANVMMGP YRQDLLAKCD RVDQLAAQLA DLAARGEGES PQARAVAAQL QDSLKDLKTR
MQEAMTQEVS DVFSDTTTPI KLLAVAATAP SDAPNRDEVF DERAANFENH AARLGATAEK
AAAVGTANKT TVEGIQATVK SARELTPQVV SAARILLRNP GNQAAYEHFE TMKNQWIDNV
EKMTGLVDEA IDTKSLLDAS EEAIKKDLDK CKVAMANIQP QMLVAGATSI ARRANRILLV
AKREVENSED PKFREAVKAA SDELSKTISP MVMDAKAVAG NISDPGLQKS FLDSGYRILG
AVAKVREAFQ PQEPDFPPPP PDLEQLHLTD ELAPPKPPLP EGEVPPPRPP PPEEKDEEFP
EQKAGEAINQ PMMMAARQLH DEARKWSSKG NDIIAAAKRM ALLMAEMSRL VRGGSGNKRA
LIQCAKDIAK ASDEVTRLAK EVAKQCTDKR IRTNLLQVCE RIPTISTQLK ILSTVKATML
GRTNISDEES EQATEMLVHN AQNLMQSVKE TVREAEAASI KIRTDAGFTL RWVRKTPWYQ
//
