P85972 (VINC_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vinculin

Alternative name(s):
Metavinculin

Gene names

Name:

Vcl

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1066 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion By similarity.
Subunit structure	Exhibits self-association properties. Interacts with APBB1IP, NRAP, SORBS1 and TLN1. Interacts with SYNM. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin By similarity. UniProtKB P18206
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › adherens junction By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction › focal adhesion By similarity. Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. Co-localizes with LIMD1 in the focal adhesions By similarity. Ref.2
Domain	Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion By similarity. The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly By similarity.
Post-translational modification	Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques By similarity. UniProtKB P12003 Acetylated; mainly by myristic acid but also by a small amount of palmitic acid By similarity.
Sequence similarities	Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Domain	Repeat
Ligand	Actin-binding
PTM	Acetylation Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction assembly Inferred from electronic annotation. Source: Compara apical junction assembly Inferred from electronic annotation. Source: Compara epithelial cell-cell adhesion Inferred from electronic annotation. Source: Compara lamellipodium assembly Inferred from electronic annotation. Source: Compara morphogenesis of an epithelium Inferred from electronic annotation. Source: Compara protein localization to cell surface Inferred from electronic annotation. Source: Compara regulation of cell migration Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from direct assay PubMed 1514597. Source: BHF-UCL actin cytoskeleton Inferred from electronic annotation. Source: InterPro costamere Inferred from electronic annotation. Source: Compara fascia adherens Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell intercalated disc Inferred from direct assay PubMed 1514597. Source: BHF-UCL protein complex Inferred from electronic annotation. Source: Compara sarcolemma Inferred from direct assay PubMed 1514597. Source: BHF-UCL
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity UniProtKB P18206
	Chain	2 – 1066	1065	Vinculin UniProtKB P18206		PRO_0000349117
Regions
	Repeat	259 – 369	111	1
	Repeat	370 – 479	110	2
	Repeat	480 – 589	110	3
	Region	2 – 835	834	N-terminal globular head By similarity
	Region	168 – 208	41	Talin-interaction By similarity UniProtKB P12003
	Region	259 – 589	331	3 X 112 AA tandem repeats
	Region	836 – 878	43	Linker (Pro-rich) By similarity
	Region	879 – 1066	188	C-terminal tail By similarity
	Region	935 – 978	44	Facilitates phospholipid membrane insertion By similarity
	Region	1052 – 1066	15	Facilitates phospholipid membrane insertion By similarity
	Compositional bias	837 – 878	42	Pro-rich
Amino acid modifications
	Modified residue	173	1	N6-acetyllysine By similarity
	Modified residue	290	1	Phosphoserine By similarity UniProtKB P18206
	Modified residue	324	1	Phosphothreonine By similarity UniProtKB Q64727
	Modified residue	346	1	Phosphoserine By similarity
	Modified residue	434	1	Phosphoserine By similarity
	Modified residue	496	1	N6-acetyllysine By similarity
	Modified residue	721	1	Phosphoserine By similarity UniProtKB P18206
	Modified residue	774	1	Phosphoserine By similarity UniProtKB Q64727
	Modified residue	822	1	Phosphotyrosine By similarity UniProtKB Q64727
	Modified residue	1065	1	Phosphotyrosine; by SRC-type Tyr-kinases By similarity UniProtKB P12003

Sequences

	Sequence		Length	Mass (Da)
	P85972 [UniParc]. Last modified September 2, 2008. Version 1. Checksum: E0669F208E4E8A86	FASTA	1,066	116,615
	10 20 30 40 50 60 MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE 70 80 90 100 110 120 TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS 130 140 150 160 170 180 DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 190 200 210 220 230 240 ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVGKMSAE 250 260 270 280 290 300 INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR 310 320 330 340 350 360 QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL 370 380 390 400 410 420 DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE 430 440 450 460 470 480 LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA 490 500 510 520 530 540 VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD 550 560 570 580 590 600 LLAKCDRVDQ LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS 610 620 630 640 650 660 DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GAANKSTVEG 670 680 690 700 710 720 IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 730 740 750 760 770 780 SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 790 800 810 820 830 840 EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 850 860 870 880 890 900 DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 910 920 930 940 950 960 AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE 970 980 990 1000 1010 1020 VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT 1030 1040 1050 1060 EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Proteome profile of the mature rat olfactory bulb." Maurya D.K., Sundaram C.S., Bhargava P. Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH474061 Genomic DNA. Translation: EDL86258.1.
IPI	IPI00365286.
RefSeq	NP_001100718.1. NM_001107248.1.
UniGene	Rn.164613.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6804299.
PTM databases
PhosphoSite	P85972.
2D gel databases
World-2DPAGE	0004:P85972.
Proteomic databases
PaxDb	P85972.
PRIDE	P85972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	305679.
KEGG	rno:305679.
UCSC	RGD:1311217. rat.
Organism-specific databases
CTD	7414.
RGD	1311217. Vcl.
Phylogenomic databases
eggNOG	NOG329927.
HOGENOM	HOG000007828.
HOVERGEN	HBG079758.
KO	K05700.
OMA	ELTHQVH.
OrthoDB	EOG4P5K8C.
Gene expression databases
ArrayExpress	P85972.
Genevestigator	P85972.
Family and domain databases
InterPro	IPR017997. Vinculin. IPR006077. Vinculin/catenin. IPR000633. Vinculin_CS. [Graphical view]
Pfam	PF01044. Vinculin. 2 hits. [Graphical view]
PRINTS	PR00806. VINCULIN.
SUPFAM	SSF47220. Vinculin/catenin. 7 hits.
PROSITE	PS00663. VINCULIN_1. 1 hit. PS00664. VINCULIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	654946.

Entry information

Entry name

VINC_RAT

Accession

Primary (citable) accession number: P85972
Secondary accession number(s): A6KKR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program