ID   PLAK_BOVIN              Reviewed;         745 AA.
AC   Q8SPJ1; Q17QY6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Junction plakoglobin;
DE   AltName: Full=Desmoplakin III;
DE   AltName: Full=Desmoplakin-3;
GN   Name=JUP {ECO:0000312|EMBL:AAM19329.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAM19329.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Simpson M.A., Crosby A.H.;
RT   "Role of plakoglobin in bovine cardiomyopathy with woolly haircoat
RT   syndrome.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAM19329.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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
CC       {ECO:0000250|UniProtKB:P14923}. Cell junction, desmosome
CC       {ECO:0000250|UniProtKB:P14923}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P14923}. Membrane
CC       {ECO:0000250|UniProtKB:P14923}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P14923}. Note=Cytoplasmic in a soluble and
CC       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}.
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; AF497524; AAM19329.1; -; Genomic_DNA.
DR   EMBL; AF497518; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; AF497519; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; AF497520; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; AF497521; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; AF497522; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; AF497523; AAM19329.1; JOINED; Genomic_DNA.
DR   EMBL; BC118114; AAI18115.1; -; mRNA.
DR   PIR; B32905; B32905.
DR   RefSeq; NP_001004024.1; NM_001004024.3.
DR   RefSeq; XP_005220741.1; XM_005220684.2.
DR   RefSeq; XP_010814523.1; XM_010816221.2.
DR   RefSeq; XP_010814524.1; XM_010816222.1.
DR   AlphaFoldDB; Q8SPJ1; -.
DR   SMR; Q8SPJ1; -.
DR   STRING; 9913.ENSBTAP00000023522; -.
DR   GlyCosmos; Q8SPJ1; 1 site, No reported glycans.
DR   iPTMnet; Q8SPJ1; -.
DR   PaxDb; 9913-ENSBTAP00000023522; -.
DR   PeptideAtlas; Q8SPJ1; -.
DR   Ensembl; ENSBTAT00000023522.6; ENSBTAP00000023522.5; ENSBTAG00000017685.6.
DR   Ensembl; ENSBTAT00000077921.1; ENSBTAP00000063220.1; ENSBTAG00000017685.6.
DR   GeneID; 445543; -.
DR   KEGG; bta:445543; -.
DR   CTD; 3728; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017685; -.
DR   VGNC; VGNC:30388; JUP.
DR   eggNOG; KOG4203; Eukaryota.
DR   GeneTree; ENSGT00940000156395; -.
DR   HOGENOM; CLU_008757_1_1_1; -.
DR   InParanoid; Q8SPJ1; -.
DR   OMA; SMIPIHE; -.
DR   OrthoDB; 50711at2759; -.
DR   TreeFam; TF317997; -.
DR   Reactome; R-BTA-418990; Adherens junctions interactions.
DR   Reactome; R-BTA-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-6805567; Keratinization.
DR   Reactome; R-BTA-6809371; Formation of the cornified envelope.
DR   Reactome; R-BTA-8980692; RHOA GTPase cycle.
DR   Reactome; R-BTA-9013106; RHOC GTPase cycle.
DR   Reactome; R-BTA-9013406; RHOQ GTPase cycle.
DR   Reactome; R-BTA-9013407; RHOH GTPase cycle.
DR   Reactome; R-BTA-9762292; Regulation of CDH11 function.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000017685; Expressed in esophagus and 103 other cell types or tissues.
DR   ExpressionAtlas; Q8SPJ1; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; ISS:AgBase.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0030057; C:desmosome; IDA:BHF-UCL.
DR   GO; GO:0071665; C:gamma-catenin-TCF7L2 complex; IEA:Ensembl.
DR   GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR   GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032993; C:protein-DNA complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005915; C:zonula adherens; IDA:BHF-UCL.
DR   GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IEA:Ensembl.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0071681; P:cellular response to indole-3-methanol; IEA:Ensembl.
DR   GO; GO:0002159; P:desmosome assembly; IEA:Ensembl.
DR   GO; GO:0050982; P:detection of mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR   GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR   GO; GO:0043588; P:skin development; IEA:Ensembl.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   PANTHER; PTHR45976; ARMADILLO SEGMENT POLARITY PROTEIN; 1.
DR   PANTHER; PTHR45976:SF3; JUNCTION PLAKOGLOBIN; 1.
DR   Pfam; PF00514; Arm; 3.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   2: Evidence at transcript 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_0000064277"
FT   REPEAT          132..171
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000255"
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:0000250|UniProtKB:P14923"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14923"
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"
FT   CONFLICT        92
FT                   /note="G -> S (in Ref. 2; AAI18115)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   745 AA;  81821 MW;  CCF44BAC1FEA469C CRC64;
     MEVMNLIEQP IKVTEWQQTY TYDSGIHSGA NTCVPSLSSK GLIEEDEACG RQYTLKKTTT
     YTQSVPPGQG DLEYQMSTTA RAKRVREAMC PGVTGEDSSL LLTTQVEGQT TNLQRLAEPS
     QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM
     GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE
     SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ
     ESKLIILANG GPQALVQIMR 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 EAAQSMIPMN EPYADDMDAT YRPMYSSDVP MDPLEMHMDM
     DGDYPIDTYS DGLRPPYATA DHMLA
//