PLAK_PIG
ID PLAK_PIG Reviewed; 745 AA.
AC Q8WNW3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Junction plakoglobin;
GN Name=Jup;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RA Hirano M., Hirano K., Nishimura J., Kanaide H.;
RT "Transcriptional upregulation of p27Kip1 during contact-induced growth
RT arrest in endothelial cells.";
RL Submitted (JUL-2000) 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 {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}.
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DR EMBL; AB046172; BAB82985.1; -; mRNA.
DR RefSeq; NP_999488.1; NM_214323.1.
DR RefSeq; XP_005668876.1; XM_005668819.2.
DR RefSeq; XP_005668877.1; XM_005668820.2.
DR RefSeq; XP_005668878.1; XM_005668821.2.
DR RefSeq; XP_005668879.1; XM_005668822.2.
DR RefSeq; XP_013836408.1; XM_013980954.1.
DR RefSeq; XP_013836409.1; XM_013980955.1.
DR RefSeq; XP_013836410.1; XM_013980956.1.
DR AlphaFoldDB; Q8WNW3; -.
DR SMR; Q8WNW3; -.
DR STRING; 9823.ENSSSCP00000018469; -.
DR PaxDb; Q8WNW3; -.
DR PeptideAtlas; Q8WNW3; -.
DR PRIDE; Q8WNW3; -.
DR Ensembl; ENSSSCT00015058360; ENSSSCP00015023399; ENSSSCG00015043128.
DR Ensembl; ENSSSCT00015058494; ENSSSCP00015023451; ENSSSCG00015043128.
DR Ensembl; ENSSSCT00015058555; ENSSSCP00015023478; ENSSSCG00015043128.
DR Ensembl; ENSSSCT00015058643; ENSSSCP00015023519; ENSSSCG00015043128.
DR Ensembl; ENSSSCT00030090362; ENSSSCP00030041637; ENSSSCG00030064636.
DR Ensembl; ENSSSCT00035031200; ENSSSCP00035012212; ENSSSCG00035023778.
DR Ensembl; ENSSSCT00040036223; ENSSSCP00040015026; ENSSSCG00040026885.
DR Ensembl; ENSSSCT00040036325; ENSSSCP00040015063; ENSSSCG00040026885.
DR Ensembl; ENSSSCT00040036393; ENSSSCP00040015095; ENSSSCG00040026885.
DR Ensembl; ENSSSCT00040036477; ENSSSCP00040015137; ENSSSCG00040026885.
DR Ensembl; ENSSSCT00045064721; ENSSSCP00045045742; ENSSSCG00045037452.
DR Ensembl; ENSSSCT00050030549; ENSSSCP00050012734; ENSSSCG00050022624.
DR Ensembl; ENSSSCT00055023932; ENSSSCP00055018943; ENSSSCG00055012213.
DR Ensembl; ENSSSCT00060031590; ENSSSCP00060013537; ENSSSCG00060023262.
DR Ensembl; ENSSSCT00060031597; ENSSSCP00060013540; ENSSSCG00060023262.
DR Ensembl; ENSSSCT00060031599; ENSSSCP00060013542; ENSSSCG00060023262.
DR Ensembl; ENSSSCT00060031609; ENSSSCP00060013546; ENSSSCG00060023262.
DR Ensembl; ENSSSCT00065013724; ENSSSCP00065005606; ENSSSCG00065010328.
DR Ensembl; ENSSSCT00070029321; ENSSSCP00070024435; ENSSSCG00070014905.
DR GeneID; 397592; -.
DR KEGG; ssc:397592; -.
DR CTD; 3728; -.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_008757_1_1_1; -.
DR InParanoid; Q8WNW3; -.
DR OrthoDB; 321213at2759; -.
DR TreeFam; TF317997; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 12.
DR Genevisible; Q8WNW3; SS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0002159; P:desmosome assembly; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 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_0000064280"
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: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"
SQ SEQUENCE 745 AA; 81850 MW; 53F19D385AB19F60 CRC64;
MEVMNLIEQP IKVTEWQQTY TYDSGIHSGA NTCVPSVSSK GLMEEDEACG RQYTLKKTTT
YTQAVPQSQG DLEYQMSTTA RAKRVREAMC PGVTGEDSSL LLATQVEGQT 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 ASVIPRLVQL LVKAHQDAQR
HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI
QRVAAGVLCE LAQDKEAADA IDAEGASSPL MELLHSRNEG TATYAAAVLF RISEDKNPDY
RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLEMHMDM
DGDYPMDTYS DGLRPPYPAA DHMLA
