VINC_BRUMA
ID VINC_BRUMA Reviewed; 993 AA.
AC Q17162;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Vinculin;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dissanayake S.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell adhesion. May be involved in the attachment
CC of the actin-based microfilaments to the plasma membrane.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- SUBUNIT: Exhibits self-association properties.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P85972}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell membrane
CC {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P12003}. Cell junction
CC {ECO:0000250|UniProtKB:P12003}. Note=Cytoplasmic face of adhesion
CC plaques. {ECO:0000250|UniProtKB:P12003}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; U07023; AAB96842.1; -; mRNA.
DR AlphaFoldDB; Q17162; -.
DR SMR; Q17162; -.
DR STRING; 6279.Q17162; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR46180; PTHR46180; 2.
DR Pfam; PF01044; Vinculin; 1.
DR SUPFAM; SSF47220; SSF47220; 6.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell adhesion; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome; Repeat.
FT CHAIN 1..993
FT /note="Vinculin"
FT /id="PRO_0000064257"
FT REPEAT 258..364
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 373..480
FT /note="2"
FT /evidence="ECO:0000255"
FT REGION 258..480
FT /note="2 X repeats"
FT /evidence="ECO:0000255"
FT REGION 730..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 110188 MW; 318CB75FA33E4E2A CRC64;
MPVFHTKTIE GILEPVAQQV SRLVILHEEA EDGNAVLDLT LPVGAVSRAV DNLIKVGYDT
CHSSDDRILQ ADMPPALQRV EASSRLLEDA CHMLRADPYS SVARKKLIEG ARGILQGTSA
LLLSFDESEV RKIIRGCRKV LDYLAVAEVI ESMDDLAQFV KDISPWLTRV SRNIDAREKE
LTHQVHREIL LRCMDTVKTL SPIMICAMKI FIQITEESQR GQQEAAENRN YLAQRMTDEM
NEIIRVLQLT TYDEDEWDSD NVTVMRKALS AAQSLLTSAL DWLADSRGRA GATGEKAIRR
IVDYSERIAA RALPEDARLI RATVSDITSM TDSLCELRNQ GGDSQGLASG CANRLKELVG
TKEISGILPS ALTNTQRTGG THPAHTVTGR LEQALRWMDN PGVDDNGLGL QAVKAMTSEA
GNLQPIYSHL QNVRKFVDLC VEIDRQADQL ADLEHRGLGN PPAAHAIRNQ LRNKLRELVD
IMKKVITDRV VEDFADISTP LKQFVDAVYA SPTIVNRELS FEEKAHNLDD HSSRCANTAL
LVAKCGPCKN KKTVEAIIEA ANQVNAMTPQ VIKAGKIRLH NDSDSANLHF DNLRREYSDV
LNRLRSHVDD AIDTSDFIRA SEQAMRQYTV YCENAIRNNE PQQMVDNTSQ IARFGNRVLM
TAKNEADNSE EPSFVHRVNN AARRLHSAIP PMVNQAKQVA LNPRHGGNAQ SWRDANEHLL
SAVRQVGDAI TGAGGSRPPS QNLLVESVPP KAPTSPIVHD RIYIREDIPT PPRPPPPVEI
SPPPRPPPPP ETDDEEETRA FWERYPLLGA SSQPILSAAH NLHQELRQWS SHENEIVAAA
KRMAILMARL SQLVRGEGGT KKDLVDCAKA IADSSEEVTR LAVQLARQCT VIKMRMTLLQ
VCERIPTIAT QLKILSTVKA TMLGSQATIG PYGQPIDGSE EDEEAMQQLV LNAQNLMQSV
KDTVRAAEAA SIKIRTNSGL RLRWIRKPMW SNF