Q02257 (PLAK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Junction plakoglobin

Alternative name(s):
Desmoplakin III
Desmoplakin-3

Gene names

Name:

Jup

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	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.7
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 By similarity.
Subcellular location	Cell junction › adherens junction. Cell junction › desmosome. Cytoplasm › cytoskeleton. Membrane; Peripheral membrane protein. Note: Cytoplasmic in a soluble and membrane-associated form.
Sequence similarities	Belongs to the beta-catenin family. Contains 9 ARM repeats.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cytoplasm Cytoskeleton Membrane
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	atrioventricular valve morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cell morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome cell-cell adhesion Inferred from mutant phenotype PubMed 8954745. Source: MGI cytoskeletal anchoring at plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome desmosome assembly Inferred from mutant phenotype PubMed 9847250PubMed 8954745PubMed 18496566. Source: MGI ectoderm development Inferred from Biological aspect of Ancestor. Source: RefGenome gastrulation Inferred from Biological aspect of Ancestor. Source: RefGenome morphogenesis of embryonic epithelium Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of Wnt receptor signaling pathway involved in heart development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of heart induction by canonical Wnt receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome nervous system development Inferred from Biological aspect of Ancestor. Source: RefGenome oocyte development Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome skin development Inferred from mutant phenotype PubMed 8954745. Source: MGI
Cellular component	Axin-APC-beta-catenin-GSK3B complex Inferred from Biological aspect of Ancestor. Source: RefGenome Z disc Inferred from direct assay PubMed 8821035. Source: MGI actin cytoskeleton Inferred from Biological aspect of Ancestor. Source: RefGenome basolateral plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome catenin complex Inferred from Biological aspect of Ancestor. Source: RefGenome desmosome Inferred from direct assay PubMed 15775979PubMed 14673151PubMed 10662781. Source: MGI fascia adherens Inferred from Biological aspect of Ancestor. Source: RefGenome internal side of plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome zonula adherens Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	RPTP-like protein binding Inferred from physical interaction PubMed 16973135. Source: MGI alpha-catenin binding Inferred from physical interaction PubMed 14579029. Source: MGI cadherin binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome structural molecule activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription coactivator activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	Junction plakoglobin		PRO_0000064279
Regions
	Repeat	132 – 171	40	ARM 1
	Repeat	216 – 255	40	ARM 2
	Repeat	258 – 297	40	ARM 3
	Repeat	342 – 381	40	ARM 4
	Repeat	383 – 420	38	ARM 5
	Repeat	423 – 464	42	ARM 6
	Repeat	470 – 510	41	ARM 7
	Repeat	512 – 551	40	ARM 8
	Repeat	574 – 613	40	ARM 9
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	20	1	Phosphotyrosine By similarity
	Modified residue	182	1	Phosphoserine By similarity
	Modified residue	660	1	Phosphotyrosine By similarity
	Modified residue	665	1	Phosphoserine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q02257 [UniParc]. Last modified December 6, 2005. Version 3. Checksum: 9609619D94052FC5	FASTA	745	81,801
	10 20 30 40 50 60 MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG RQYTLKKTTT 70 80 90 100 110 120 YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL 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 GPQGLVQIMR 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 AAVIPRLVQL LVKAHQDAQR 550 560 570 580 590 600 HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI 610 620 630 640 650 660 QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY 670 680 690 700 710 720 RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLDMHMDL 730 740 DGDYPMDTYS DGLRPPYPTA DHMLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NOD.
[2]	"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]. Strain: FVB/N. Tissue: Colon and Mammary tumor.
[3]	"Plakoglobin and beta-catenin: distinct but closely related." Butz S., Stappert J., Weissig H., Kemler R. Science 257:1142-1144(1992) [PubMed: 1509266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-745.
[4]	Butz S. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 418 AND 420.
[5]	"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion." Butz S., Kemler R. FEBS Lett. 355:195-200(1994) [PubMed: 7982500] [Abstract] Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[6]	"Deconstructing the cadherin-catenin-actin complex." Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J. Cell 123:889-901(2005) [PubMed: 16325582] [Abstract] Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[7]	"VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF." Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R., Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O., Bixel M.G., Butz S., Vestweber D. J. Exp. Med. 205:2929-2945(2008) [PubMed: 19015309] [Abstract] Cited for: FUNCTION.
[8]	"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-665, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK170934 mRNA. Translation: BAE42126.1. BC040757 mRNA. Translation: AAH40757.1. BC094461 mRNA. Translation: AAH94461.1. M90365 mRNA. Translation: AAB02885.1.
IPI	IPI00229475.
PIR	S35092.
RefSeq	NP_034723.1. NM_010593.2.
UniGene	Mm.299774.
3D structure databases
ProteinModelPortal	Q02257.
SMR	Q02257. Positions 111-673.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02257. 4 interactions.
STRING	Q02257.
PTM databases
PhosphoSite	Q02257.
Proteomic databases
PRIDE	Q02257.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552. ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
GeneID	16480.
KEGG	mmu:16480.
Organism-specific databases
CTD	3728.
MGI	MGI:96650. Jup.
Phylogenomic databases
eggNOG	NOG297695.
GeneTree	ENSGT00570000078959.
HOGENOM	HOG000230958.
HOVERGEN	HBG000919.
InParanoid	Q02257.
KO	K10056.
OMA	DDMDATY.
OrthoDB	EOG4FR0R3.
Gene expression databases
ArrayExpress	Q02257.
Bgee	Q02257.
CleanEx	MM_JUP.
Genevestigator	Q02257.
GermOnline	ENSMUSG00000001552. Mus musculus.
Family and domain databases
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000225. Armadillo. IPR013284. Beta-catenin. [Graphical view]
Pfam	PF00514. Arm. 3 hits. [Graphical view]
PRINTS	PR01869. BCATNINFAMLY.
SMART	SM00185. ARM. 12 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50176. ARM_REPEAT. 9 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	289775.
SOURCE	Search...

Entry information

Entry name

PLAK_MOUSE

Accession

Primary (citable) accession number: Q02257
Secondary accession number(s): Q8CGD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	December 6, 2005
Last modified:	May 16, 2012
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program