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Protein

Vang-like protein 2

Gene

Vangl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process. Required for cell surface localization of FZD3 and FZD6 in the inner ear (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Vang-like protein 2
Alternative name(s):
Van Gogh-like protein 2
Gene namesi
Name:Vangl2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi1309442. Vangl2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 108108CytoplasmicSequence analysisAdd
BLAST
Transmembranei109 – 12921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini130 – 14718ExtracellularSequence analysisAdd
BLAST
Transmembranei148 – 16821Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini169 – 17810CytoplasmicSequence analysis
Transmembranei179 – 19921Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini200 – 21718ExtracellularSequence analysisAdd
BLAST
Transmembranei218 – 23821Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini239 – 521283CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Vang-like protein 2PRO_0000247591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei84 – 841PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP84889.
PRIDEiP84889.

PTM databases

PhosphoSiteiP84889.
SwissPalmiP84889.

Expressioni

Tissue specificityi

Asymmetrically localized to specific cell-cell boundaries in the developing inner ear.1 Publication

Developmental stagei

Expression does not persist beyond the early postnatal period in the sensory region of the inner ear.1 Publication

Gene expression databases

GenevisibleiP84889. RN.

Interactioni

Subunit structurei

Homodimer and heterodimer with VANGL1. Interacts through its C-terminal region with the N-terminal half of DVL1, DVL2 and DVL3. The PDZ domain of DVL1, DVL2 and DVL3 is required for the interaction. Also interacts with the PDZ domains of MAGI3, SCRIB/SCRB1 and FZD3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi252835. 4 interactions.
IntActiP84889. 4 interactions.
MINTiMINT-8416720.
STRINGi10116.ENSRNOP00000006849.

Structurei

3D structure databases

ProteinModelPortaliP84889.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Vang family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3814. Eukaryota.
ENOG410XPVT. LUCA.
GeneTreeiENSGT00390000012496.
HOGENOMiHOG000230590.
HOVERGENiHBG058215.
InParanoidiP84889.
KOiK04510.
OMAiGYHRERD.
OrthoDBiEOG7MSMNR.
PhylomeDBiP84889.
TreeFamiTF313467.

Family and domain databases

InterProiIPR009539. VANGL.
[Graphical view]
PANTHERiPTHR20886. PTHR20886. 1 hit.
PfamiPF06638. Strabismus. 1 hit.
[Graphical view]
PIRSFiPIRSF007991. Strabismus. 1 hit.

Sequencei

Sequence statusi: Complete.

P84889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTESQYSGY SYKSGHSRSS RKHRDRRDRH RSKSRDGSRG DKSVTIQAPG
60 70 80 90 100
EPLLDNESTR GDERDDNWGE TTTVVTGTSE HSISHDDLTR IAKDMEDSVP
110 120 130 140 150
LDCSRHLGVA AGAILALLSF LTPLAFLLLP PLLWREELEP CGTACEGLFI
160 170 180 190 200
SVAFKLLILL LGSWALFFRR PKASLPRVFV LRALLMVLVF LLVISYWLFY
210 220 230 240 250
GVRILDARER SYQGVVQFAV SLVDALLFVH YLAVVLLELR QLQPQFTLKV
260 270 280 290 300
VRSTDGASRF YNVGHLSIQR VAVWILEKYY HDFPVYNPAL LNLPKSVLAK
310 320 330 340 350
KVSGFKVYSL GEENSTNNST GQSRAVIAAA ARRRDNSHNE YYYEEAEHER
360 370 380 390 400
RVRKRRARLV VAVEEAFTHI KRLQEEEQKN PREVMDPREA AQAIFASMAR
410 420 430 440 450
AMQKYLRTTK QQPYHTMESI LQHLEFCITH DMTPKAFLER YLAAGPTIQY
460 470 480 490 500
HKERWLAKQW TLVSEEPVTN GLKDGIVFLL KRQDFSLVVS TKKVPFFKLS
510 520
EEFVDPKSHK FVMRLQSETS V
Length:521
Mass (Da):59,771
Last modified:July 25, 2006 - v1
Checksum:i94ECEF3EE63DF5BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03084676 Genomic DNA. No translation available.
RefSeqiNP_001099439.1. NM_001105969.1.
XP_006250338.1. XM_006250276.2.
XP_006250339.1. XM_006250277.2.
UniGeneiRn.198958.

Genome annotation databases

EnsembliENSRNOT00000006849; ENSRNOP00000006849; ENSRNOG00000004889.
ENSRNOT00000091710; ENSRNOP00000072619; ENSRNOG00000004889.
GeneIDi289229.
KEGGirno:289229.
UCSCiRGD:1309442. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03084676 Genomic DNA. No translation available.
RefSeqiNP_001099439.1. NM_001105969.1.
XP_006250338.1. XM_006250276.2.
XP_006250339.1. XM_006250277.2.
UniGeneiRn.198958.

3D structure databases

ProteinModelPortaliP84889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi252835. 4 interactions.
IntActiP84889. 4 interactions.
MINTiMINT-8416720.
STRINGi10116.ENSRNOP00000006849.

PTM databases

PhosphoSiteiP84889.
SwissPalmiP84889.

Proteomic databases

PaxDbiP84889.
PRIDEiP84889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000006849; ENSRNOP00000006849; ENSRNOG00000004889.
ENSRNOT00000091710; ENSRNOP00000072619; ENSRNOG00000004889.
GeneIDi289229.
KEGGirno:289229.
UCSCiRGD:1309442. rat.

Organism-specific databases

CTDi57216.
RGDi1309442. Vangl2.

Phylogenomic databases

eggNOGiKOG3814. Eukaryota.
ENOG410XPVT. LUCA.
GeneTreeiENSGT00390000012496.
HOGENOMiHOG000230590.
HOVERGENiHBG058215.
InParanoidiP84889.
KOiK04510.
OMAiGYHRERD.
OrthoDBiEOG7MSMNR.
PhylomeDBiP84889.
TreeFamiTF313467.

Miscellaneous databases

NextBioi629422.
PROiP84889.

Gene expression databases

GenevisibleiP84889. RN.

Family and domain databases

InterProiIPR009539. VANGL.
[Graphical view]
PANTHERiPTHR20886. PTHR20886. 1 hit.
PfamiPF06638. Strabismus. 1 hit.
[Graphical view]
PIRSFiPIRSF007991. Strabismus. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  2. "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals."
    Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A., Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J., Warchol M.E., Wenthold R.J., Kelley M.W.
    J. Neurosci. 26:5265-5275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiVANG2_RAT
AccessioniPrimary (citable) accession number: P84889
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: May 11, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.