PLAK_MOUSE
ID PLAK_MOUSE Reviewed; 745 AA.
AC Q02257; Q8CGD3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Junction plakoglobin;
DE AltName: Full=Desmoplakin III;
DE AltName: Full=Desmoplakin-3;
GN Name=Jup;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-745.
RX PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA Butz S., Stappert J., Weissig H., Kemler R.;
RT "Plakoglobin and beta-catenin: distinct but closely related.";
RL Science 257:1142-1144(1992).
RN [4]
RP SEQUENCE REVISION TO 418 AND 420.
RA Butz S.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA Butz S., Kemler R.;
RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT adhesion.";
RL FEBS Lett. 355:195-200(1994).
RN [6]
RP RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT "Deconstructing the cadherin-catenin-actin complex.";
RL Cell 123:889-901(2005).
RN [7]
RP FUNCTION.
RX PubMed=19015309; DOI=10.1084/jem.20080406;
RA Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R.,
RA Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O.,
RA Bixel M.G., Butz S., Vestweber D.;
RT "VE-PTP maintains the endothelial barrier via plakoglobin and becomes
RT dissociated from VE-cadherin by leukocytes and by VEGF.";
RL J. Exp. Med. 205:2929-2945(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Common junctional plaque protein. The membrane-associated
CC plaques are architectural elements in an important strategic position
CC to influence the arrangement and function of both the cytoskeleton and
CC the cells within the tissue. The presence of plakoglobin in both the
CC desmosomes and in the intermediate junctions suggests that it plays a
CC central role in the structure and function of submembranous plaques.
CC Acts as a substrate for VE-PTP and is required by it to stimulate VE-
CC cadherin function in endothelial cells. Can replace beta-catenin in E-
CC cadherin/catenin adhesion complexes which are proposed to couple
CC cadherins to the actin cytoskeleton. {ECO:0000269|PubMed:19015309}.
CC -!- SUBUNIT: Homodimer. Component of an E-cadherin/catenin adhesion complex
CC composed of at least E-cadherin/CDH1 and gamma-catenin/JUP, and
CC possibly alpha-catenin/CTNNA1; the complex is located to adherens
CC junctions. The stable association of CTNNA1 is controversial as CTNNA1
CC was shown not to bind to F-actin when assembled in the complex.
CC Interacts with MUC1. Interacts with CAV1. Interacts with PTPRJ.
CC Interacts with DSG1. Interacts with DSC1 and DSC2. Interacts with PKP2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell junction,
CC desmosome. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane
CC protein. Note=Cytoplasmic in a soluble and membrane-associated form.
CC -!- DOMAIN: The entire ARM repeats region mediates binding to CDH1/E-
CC cadherin. The N-terminus and first three ARM repeats are sufficient for
CC binding to DSG1. The N-terminus and first ARM repeat are sufficient for
CC association with CTNNA1. DSC1 association requires both ends of the ARM
CC repeat region (By similarity). {ECO:0000250}.
CC -!- PTM: May be phosphorylated by FER. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AK170934; BAE42126.1; -; mRNA.
DR EMBL; BC040757; AAH40757.1; -; mRNA.
DR EMBL; BC094461; AAH94461.1; -; mRNA.
DR EMBL; M90365; AAB02885.1; -; mRNA.
DR CCDS; CCDS25420.1; -.
DR PIR; S35092; S35092.
DR RefSeq; NP_034723.1; NM_010593.2.
DR RefSeq; XP_006532378.1; XM_006532315.3.
DR RefSeq; XP_006532379.1; XM_006532316.1.
DR AlphaFoldDB; Q02257; -.
DR SMR; Q02257; -.
DR BioGRID; 200874; 67.
DR IntAct; Q02257; 53.
DR MINT; Q02257; -.
DR STRING; 10090.ENSMUSP00000001592; -.
DR GlyGen; Q02257; 1 site.
DR iPTMnet; Q02257; -.
DR PhosphoSitePlus; Q02257; -.
DR SwissPalm; Q02257; -.
DR CPTAC; non-CPTAC-3490; -.
DR EPD; Q02257; -.
DR jPOST; Q02257; -.
DR MaxQB; Q02257; -.
DR PaxDb; Q02257; -.
DR PeptideAtlas; Q02257; -.
DR PRIDE; Q02257; -.
DR ProteomicsDB; 289671; -.
DR Antibodypedia; 80391; 1297 antibodies from 46 providers.
DR DNASU; 16480; -.
DR Ensembl; ENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552.
DR Ensembl; ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
DR GeneID; 16480; -.
DR KEGG; mmu:16480; -.
DR UCSC; uc007lkz.2; mouse.
DR CTD; 3728; -.
DR MGI; MGI:96650; Jup.
DR VEuPathDB; HostDB:ENSMUSG00000001552; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000156395; -.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; Q02257; -.
DR OMA; PLDPMEM; -.
DR OrthoDB; 321213at2759; -.
DR PhylomeDB; Q02257; -.
DR TreeFam; TF317997; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 16480; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Jup; mouse.
DR PRO; PR:Q02257; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q02257; protein.
DR Bgee; ENSMUSG00000001552; Expressed in lip and 277 other tissues.
DR Genevisible; Q02257; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:MGI.
DR GO; GO:0016342; C:catenin complex; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030057; C:desmosome; IDA:MGI.
DR GO; GO:0005916; C:fascia adherens; ISO:MGI.
DR GO; GO:0071665; C:gamma-catenin-TCF7L2 complex; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
DR GO; GO:0002159; P:desmosome assembly; IMP:MGI.
DR GO; GO:0050982; P:detection of mechanical stimulus; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR InterPro; IPR030461; Plakoglobin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR PANTHER; PTHR45976:SF3; PTHR45976:SF3; 1.
DR Pfam; PF00514; Arm; 3.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..745
FT /note="Junction plakoglobin"
FT /id="PRO_0000064279"
FT REPEAT 132..171
FT /note="ARM 1"
FT REPEAT 172..215
FT /note="ARM 2"
FT REPEAT 216..255
FT /note="ARM 3"
FT REPEAT 258..297
FT /note="ARM 4"
FT REPEAT 298..341
FT /note="ARM 5"
FT REPEAT 342..381
FT /note="ARM 6"
FT REPEAT 383..420
FT /note="ARM 7"
FT REPEAT 423..464
FT /note="ARM 8"
FT REPEAT 470..510
FT /note="ARM 9"
FT REPEAT 512..551
FT /note="ARM 10"
FT REPEAT 574..613
FT /note="ARM 11"
FT REPEAT 615..661
FT /note="ARM 12"
FT REGION 132..297
FT /note="Interaction with DSC1 and DSG1"
FT /evidence="ECO:0000250"
FT REGION 574..661
FT /note="Interaction with DSC1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P14923"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14923"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14923"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14923"
FT CARBOHYD 14
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 745 AA; 81801 MW; 9609619D94052FC5 CRC64;
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG RQYTLKKTTT
YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQT TNLQRLAEPS
QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM
GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE
SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ
ESKLIILANG GPQGLVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH
LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC
NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY
GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR
HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI
QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY
RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLDMHMDL
DGDYPMDTYS DGLRPPYPTA DHMLA
