Q64727 (VINC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vinculin

Alternative name(s):
Metavinculin

Gene names

Name:

Vcl

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.1
Subunit structure	Exhibits self-association properties. Interacts with 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. Ref.6
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell junction › adherens junction By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junction 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 By similarity.
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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 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 Myristate Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	lamellipodium assembly Inferred from direct assay. Source: MGI regulation of cell migration Inferred from direct assay. Source: MGI
Cellular component	costamere Inferred from direct assay. Source: MGI fascia adherens Inferred from direct assay. Source: MGI focal adhesion Inferred from direct assay. Source: UniProtKB
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arhgef1	Q61210	3	EBI-432047,EBI-641821

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 1066	1065	Vinculin		PRO_0000064253
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
	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
	Region	1052 – 1066	15	Facilitates phospholipid membrane insertion
	Compositional bias	837 – 878	42	Pro-rich
Amino acid modifications
	Modified residue	100	1	Phosphotyrosine By similarity
	Modified residue	173	1	N6-acetyllysine By similarity
	Modified residue	290	1	Phosphoserine Ref.7 Ref.10 Ref.11
	Modified residue	324	1	Phosphothreonine Ref.9
	Modified residue	496	1	N6-acetyllysine By similarity
	Modified residue	508	1	Phosphothreonine By similarity
	Modified residue	537	1	Phosphotyrosine Potential
	Modified residue	604	1	Phosphothreonine By similarity
	Modified residue	692	1	Phosphotyrosine By similarity
	Modified residue	721	1	Phosphoserine Ref.10 Ref.11
	Modified residue	774	1	Phosphoserine Ref.9
	Modified residue	822	1	Phosphotyrosine Ref.8
	Modified residue	1065	1	Phosphotyrosine; by SRC-type Tyr-kinases By similarity
Experimental info
	Sequence conflict	16	1	V → E in AAB96843. Ref.1
	Sequence conflict	215	1	T → S in AAB96843. Ref.1
	Sequence conflict	363	1	L → V in AAB96843. Ref.1
	Sequence conflict	499	1	Q → K in BAC37033. Ref.3
	Sequence conflict	501	1	Q → R in AAB96843. Ref.1
	Sequence conflict	799	1	M → K in BAC37033. Ref.3
	Sequence conflict	812	1	G → D in AAB96843. Ref.1
	Sequence conflict	1044	1	A → T in BAC37033. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q64727 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 067F1B16A5285859	FASTA	1,066	116,717
	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 NFTVEKMSAE 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 LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS 610 620 630 640 650 660 DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GTANKSTVEG 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]	"Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion." Coll J.-L., Ben-Ze'ev A., Ezzell R.M., Rodriguez Fernandez J.L., Baribault H., Oshima R.G., Adamson E.D. Proc. Natl. Acad. Sci. U.S.A. 92:9161-9165(1995) [PubMed: 7568093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: 129/SvJ. Tissue: Embryo.
[2]	"Vinculin gene is non-essential in Drosophila melanogaster." Alatortsev V.E., Kramerova I.A., Frolov M.V., Lavrov S.A., Westphal E.D. FEBS Lett. 413:197-201(1997) [PubMed: 9280281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo and Forelimb.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 286-300; 656-666 AND 916-924, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[6]	"Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions." Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., Takai Y. J. Cell Biol. 144:1001-1017(1999) [PubMed: 10085297] [Abstract] Cited for: INTERACTION WITH SORBS1.
[7]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324 AND SER-774, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[12]	"Vinculin's C-terminal region facilitates phospholipid membrane insertion." Wirth V.F., List F., Diez G., Goldmann W.H. Biochem. Biophys. Res. Commun. 398:433-437(2010) [PubMed: 20599708] [Abstract] Cited for: REGION INVOLVED IN PHOSPHOLIPID MEMBRANE INSERTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13300, L13299 Genomic DNA. Translation: AAA40557.1. L18880 mRNA. Translation: AAB96843.1. AK035184 mRNA. Translation: BAC28973.1. AK077850 mRNA. Translation: BAC37033.1. BC008520 mRNA. Translation: AAH08520.1. BC008554 mRNA. Translation: AAH08554.1.
IPI	IPI00405227.
PIR	A60965. T10108.
RefSeq	NP_033528.3. NM_009502.4.
UniGene	Mm.279361.
3D structure databases
ProteinModelPortal	Q64727.
SMR	Q64727. Positions 1-258, 882-1063.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64727. 2 interactions.
MINT	MINT-1634466.
STRING	Q64727.
PTM databases
PhosphoSite	Q64727.
2D gel databases
REPRODUCTION-2DPAGE	Q64727.
Proteomic databases
PRIDE	Q64727.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
GeneID	22330.
KEGG	mmu:22330.
UCSC	uc007skz.1. mouse.
Organism-specific databases
CTD	7414.
MGI	MGI:98927. Vcl.
Phylogenomic databases
eggNOG	roNOG04310.
GeneTree	ENSGT00550000074411.
HOGENOM	HBG358349.
HOVERGEN	HBG079758.
InParanoid	Q64727.
OMA	ELTHQVH.
OrthoDB	EOG4P5K8C.
Gene expression databases
ArrayExpress	Q64727.
Bgee	Q64727.
CleanEx	MM_VCL.
Genevestigator	Q64727.
GermOnline	ENSMUSG00000021823. Mus musculus.
Family and domain databases
InterPro	IPR017997. Vinculin. IPR006077. Vinculin/catenin. IPR000633. Vinculin_CS. [Graphical view]
KO	K05700.
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	302571.
PMAP-CutDB	Q64727.
SOURCE	Search...

Entry information

Entry name

VINC_MOUSE

Accession

Primary (citable) accession number: Q64727
Secondary accession number(s): Q8BP32 , Q8BS46, Q922C5, Q922D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program