VINC_RAT
ID VINC_RAT Reviewed; 1066 AA.
AC P85972; A6KKR4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Vinculin {ECO:0000250|UniProtKB:P18206};
DE AltName: Full=Metavinculin {ECO:0000250|UniProtKB:P18206};
GN Name=Vcl {ECO:0000250|UniProtKB:P18206};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-260; SER-272;
RP SER-275; SER-290; SER-346; SER-434; SER-574; SER-579; SER-721; SER-795 AND
RP TYR-822, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P18206}.
CC -!- SUBUNIT: Exhibits self-association properties. Part of a complex
CC composed of THSD1, PTK2/FAK1, TLN1 and VCL (By similarity). Interacts
CC with APBB1IP, NRAP and TLN1. Interacts with CTNNB1 and this interaction
CC is necessary for its localization to the cell-cell junctions and for
CC its function in regulating cell surface expression of E-cadherin (By
CC similarity). Interacts with SORBS1 (By similarity). Interacts with SYNM
CC (By similarity). Interacts with CTNNA1 (By similarity). Binds to ACTN4;
CC this interaction triggers conformational changes (By similarity).
CC {ECO:0000250|UniProtKB:P12003, ECO:0000250|UniProtKB:P18206,
CC ECO:0000250|UniProtKB:Q64727}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12003};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19343716}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions
CC occurs in a myosin II-dependent manner. Interaction with CTNNB1 is
CC necessary for its localization to the cell-cell junctions.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC 'inactive' conformation, extensive interactions between the head and
CC tail domains prevent detectable binding to most of its ligands. It
CC takes on an 'active' conformation after cooperative and simultaneous
CC binding of two different ligands. This activation involves displacement
CC of the head-tail interactions and leads to a significant accumulation
CC of ternary complexes. The active form then binds a number of proteins
CC that have both signaling and structural roles that are essential for
CC cell adhesion. {ECO:0000250|UniProtKB:P18206}.
CC -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-
CC D4. The C-terminal tail (Vt) binds F-actin and cross-links actin
CC filaments into bundles. An intramolecular interaction between Vh and Vt
CC masks the F-actin-binding domain located in Vt. The binding of talin
CC and alpha-actinin to the D1 subdomain of vinculin induces a helical
CC bundle conversion of this subdomain, leading to the disruption of the
CC intramolecular interaction and the exposure of the cryptic F-actin-
CC binding domain of Vt. Vt inhibits actin filament barbed end elongation
CC without affecting the critical concentration of actin assembly.
CC {ECO:0000250|UniProtKB:P18206}.
CC -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC Phosphorylation on Tyr-1065 in activated platelets affects head-tail
CC interactions and cell spreading but has no effect on actin binding nor
CC on localization to focal adhesion plaques (By similarity).
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- PTM: Acetylated; mainly by myristic acid but also by a small amount of
CC palmitic acid. {ECO:0000250|UniProtKB:P12003}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000255}.
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 EMBL; CH474061; EDL86258.1; -; Genomic_DNA.
DR RefSeq; NP_001100718.1; NM_001107248.1.
DR AlphaFoldDB; P85972; -.
DR BMRB; P85972; -.
DR SMR; P85972; -.
DR BioGRID; 258242; 3.
DR IntAct; P85972; 4.
DR MINT; P85972; -.
DR STRING; 10116.ENSRNOP00000015179; -.
DR iPTMnet; P85972; -.
DR PhosphoSitePlus; P85972; -.
DR World-2DPAGE; 0004:P85972; -.
DR jPOST; P85972; -.
DR PaxDb; P85972; -.
DR PRIDE; P85972; -.
DR Ensembl; ENSRNOT00000015179; ENSRNOP00000015179; ENSRNOG00000010765.
DR GeneID; 305679; -.
DR KEGG; rno:305679; -.
DR UCSC; RGD:1311217; rat.
DR CTD; 7414; -.
DR RGD; 1311217; Vcl.
DR eggNOG; KOG3681; Eukaryota.
DR InParanoid; P85972; -.
DR PhylomeDB; P85972; -.
DR TreeFam; TF313686; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P85972; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0005903; C:brush border; ISS:AgBase.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005916; C:fascia adherens; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0002102; C:podosome; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0002162; F:dystroglycan binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0034333; P:adherens junction assembly; ISO:RGD.
DR GO; GO:0043297; P:apical junction assembly; ISO:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISO:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; ISO:RGD.
DR GO; GO:0002009; P:morphogenesis of an epithelium; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:1904702; P:regulation of protein localization to adherens junction; ISO:RGD.
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; PTHR46180; 1.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 6.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1066
FT /note="Vinculin"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT /id="PRO_0000349117"
FT REPEAT 259..369
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 370..479
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 480..589
FT /note="3"
FT /evidence="ECO:0000255"
FT REGION 1..835
FT /note="N-terminal globular head"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 168..208
FT /note="Talin-interaction"
FT /evidence="ECO:0000250|UniProtKB:P12003"
FT REGION 259..589
FT /note="3 X 112 AA tandem repeats"
FT /evidence="ECO:0000255"
FT REGION 741..764
FT /note="Interaction with ACTN4"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 836..878
FT /note="Linker (Pro-rich)"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 857..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1066
FT /note="C-terminal tail"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 935..978
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT REGION 1052..1066
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 537
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 672
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1065
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P18206"
SQ SEQUENCE 1066 AA; 116615 MW; E0669F208E4E8A86 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVGKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE
LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GAANKSTVEG
IQASVKTARE LTPQVISAAR 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
