PLAK_RAT
ID PLAK_RAT Reviewed; 745 AA.
AC Q6P0K8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Junction plakoglobin;
GN Name=Jup;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PROTEIN SEQUENCE OF 1-12; 58-81; 192-203 AND 262-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC Cell junction, desmosome {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Note=Cytoplasmic in a soluble and membrane-associated
CC form. {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC065580; AAH65580.1; -; mRNA.
DR RefSeq; NP_112309.2; NM_031047.2.
DR RefSeq; XP_006247491.1; XM_006247429.2.
DR RefSeq; XP_006247492.1; XM_006247430.3.
DR RefSeq; XP_017453037.1; XM_017597548.1.
DR AlphaFoldDB; Q6P0K8; -.
DR SMR; Q6P0K8; -.
DR BioGRID; 249576; 1.
DR IntAct; Q6P0K8; 3.
DR MINT; Q6P0K8; -.
DR STRING; 10116.ENSRNOP00000043950; -.
DR GlyGen; Q6P0K8; 1 site.
DR iPTMnet; Q6P0K8; -.
DR PhosphoSitePlus; Q6P0K8; -.
DR jPOST; Q6P0K8; -.
DR PaxDb; Q6P0K8; -.
DR PRIDE; Q6P0K8; -.
DR Ensembl; ENSRNOT00000040845; ENSRNOP00000043950; ENSRNOG00000015380.
DR GeneID; 81679; -.
DR KEGG; rno:81679; -.
DR UCSC; RGD:620412; rat.
DR CTD; 3728; -.
DR RGD; 620412; Jup.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000156395; -.
DR InParanoid; Q6P0K8; -.
DR OMA; PLDPMEM; -.
DR OrthoDB; 321213at2759; -.
DR PhylomeDB; Q6P0K8; -.
DR TreeFam; TF317997; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR PRO; PR:Q6P0K8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000015380; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q6P0K8; RN.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:RGD.
DR GO; GO:0016342; C:catenin complex; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030057; C:desmosome; IDA:RGD.
DR GO; GO:0005916; C:fascia adherens; IDA:RGD.
DR GO; GO:0071665; C:gamma-catenin-TCF7L2 complex; ISO:RGD.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:RGD.
DR GO; GO:0002159; P:desmosome assembly; ISO:RGD.
DR GO; GO:0050982; P:detection of mechanical stimulus; ISO:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
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:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
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 Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..745
FT /note="Junction plakoglobin"
FT /id="PRO_0000064281"
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:22673903"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; BF8673E1B797954D CRC64;
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GLLDEDDTCG RQYTLKKTTT
YTQGVPQSQG 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 NVLKILVNQL 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 LDPLDMHMDM
DGDYPMDTYS DGLRPPYPAA DHMLA
