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Q8WNW3 (PLAK_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Junction plakoglobin
Gene names
Name:Jup
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton By similarity.

Subunit structure

Homodimer. Component of an E-cadherin/catenin adhesion complex composed of at least E-cadherin/CDH1 and gamma-catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Interacts with MUC1. Interacts with CAV1. Interacts with PTPRJ. Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2 By similarity.

Subcellular location

Cell junctionadherens junction By similarity. Cell junctiondesmosome By similarity. Cytoplasmcytoskeleton By similarity. Membrane; Peripheral membrane protein By similarity. Note: Cytoplasmic in a soluble and membrane-associated form By similarity.

Domain

The entire ARM repeats region mediates binding to CDH1/E-cadherin. The N-terminus and first three ARM repeats are sufficient for binding to DSG1. The N-terminus and first ARM repeat are sufficient for association with CTNNA1. DSC1 association requires both ends of the ARM repeat region By similarity.

Post-translational modification

May be phosphorylated by FER By similarity.

Sequence similarities

Belongs to the beta-catenin family.

Contains 12 ARM repeats.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbundle of His cell to Purkinje myocyte communication

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to indole-3-methanol

Inferred from electronic annotation. Source: Ensembl

desmosome assembly

Inferred from electronic annotation. Source: Ensembl

detection of mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate by cardiac conduction

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell action potential

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

catenin complex

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

desmosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

gamma-catenin-TCF7L2 complex

Inferred from electronic annotation. Source: Ensembl

intercalated disc

Inferred from electronic annotation. Source: Ensembl

intermediate filament

Inferred from electronic annotation. Source: Ensembl

protein-DNA complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiontranscription coactivator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745Junction plakoglobin
PRO_0000064280

Regions

Repeat132 – 17140ARM 1
Repeat172 – 21544ARM 2
Repeat216 – 25540ARM 3
Repeat258 – 29740ARM 4
Repeat298 – 34144ARM 5
Repeat342 – 38140ARM 6
Repeat383 – 42038ARM 7
Repeat423 – 46442ARM 8
Repeat470 – 51041ARM 9
Repeat512 – 55140ARM 10
Repeat574 – 61340ARM 11
Repeat615 – 66147ARM 12
Region132 – 297166Interaction with DSC1 and DSG1 By similarity
Region574 – 66188Interaction with DSC1 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1821Phosphoserine By similarity
Modified residue6651Phosphoserine By similarity
Glycosylation141O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WNW3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 53F19D385AB19F60

FASTA74581,850
        10         20         30         40         50         60 
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GLMEEDEACG RQYTLKKTTT 

        70         80         90        100        110        120 
YTQAVPQSQG DLEYQMSTTA RAKRVREAMC PGVTGEDSSL LLATQVEGQT TNLQRLAEPS 

       130        140        150        160        170        180 
QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM 

       190        200        210        220        230        240 
GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE 

       250        260        270        280        290        300 
SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ 

       310        320        330        340        350        360 
ESKLIILANG GPQALVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH 

       370        380        390        400        410        420 
LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC 

       430        440        450        460        470        480 
NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY 

       490        500        510        520        530        540 
GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE ASVIPRLVQL LVKAHQDAQR 

       550        560        570        580        590        600 
HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 

       610        620        630        640        650        660 
QRVAAGVLCE LAQDKEAADA IDAEGASSPL MELLHSRNEG TATYAAAVLF RISEDKNPDY 

       670        680        690        700        710        720 
RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLEMHMDM 

       730        740 
DGDYPMDTYS DGLRPPYPAA DHMLA 

« Hide

References

[1]"Transcriptional upregulation of p27Kip1 during contact-induced growth arrest in endothelial cells."
Hirano M., Hirano K., Nishimura J., Kanaide H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Aortic endothelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046172 mRNA. Translation: BAB82985.1.
RefSeqNP_999488.1. NM_214323.1.
XP_005668876.1. XM_005668819.1.
XP_005668877.1. XM_005668820.1.
XP_005668878.1. XM_005668821.1.
XP_005668879.1. XM_005668822.1.
UniGeneSsc.42011.

3D structure databases

ProteinModelPortalQ8WNW3.
SMRQ8WNW3. Positions 118-672.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000018469.

Proteomic databases

PaxDbQ8WNW3.
PRIDEQ8WNW3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000018974; ENSSSCP00000018469; ENSSSCG00000017428.
GeneID397592.
KEGGssc:397592.

Organism-specific databases

CTD3728.

Phylogenomic databases

eggNOGNOG297695.
GeneTreeENSGT00730000110821.
HOGENOMHOG000230958.
HOVERGENHBG000919.
KOK10056.
OMAMNLIEQP.
OrthoDBEOG7X9G6B.
TreeFamTF317997.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR013284. Beta-catenin.
[Graphical view]
PfamPF00514. Arm. 3 hits.
[Graphical view]
PRINTSPR01869. BCATNINFAMLY.
SMARTSM00185. ARM. 12 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 9 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLAK_PIG
AccessionPrimary (citable) accession number: Q8WNW3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2002
Last modified: March 19, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families