PLAK_XENLA
ID PLAK_XENLA Reviewed; 738 AA.
AC P30998; Q52L07;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Junction plakoglobin;
DE AltName: Full=Desmoplakin III;
DE AltName: Full=Desmoplakin-3;
GN Name=jup;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1459359; DOI=10.1111/j.1432-0436.1992.tb00695.x;
RA Fouquet B., Zimbelmann R., Franke W.W.;
RT "Identification of plakoglobin in oocytes and early embryos of Xenopus
RT laevis: maternal expression of a gene encoding a junctional plaque
RT protein.";
RL Differentiation 51:187-194(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 133-292.
RX PubMed=1397690; DOI=10.1016/0012-1606(92)90118-z;
RA de Marais A.A., Moon R.T.;
RT "The armadillo homologs beta-catenin and plakoglobin are differentially
RT expressed during early development of Xenopus laevis.";
RL Dev. Biol. 153:337-346(1992).
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 -!- SUBUNIT: Homodimer.
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 -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; M95593; AAA49931.1; -; mRNA.
DR EMBL; BC094116; AAH94116.1; -; mRNA.
DR EMBL; X67078; CAA47463.1; -; mRNA.
DR PIR; S35093; S35093.
DR RefSeq; NP_001084051.1; NM_001090582.1.
DR AlphaFoldDB; P30998; -.
DR SMR; P30998; -.
DR BioGRID; 100603; 1.
DR PRIDE; P30998; -.
DR DNASU; 399278; -.
DR GeneID; 399278; -.
DR KEGG; xla:399278; -.
DR CTD; 399278; -.
DR Xenbase; XB-GENE-6254182; jup.S.
DR OrthoDB; 321213at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 399278; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016342; C:catenin complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045294; F:alpha-catenin binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0002159; P:desmosome assembly; IEA:InterPro.
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 Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..738
FT /note="Junction plakoglobin"
FT /id="PRO_0000064282"
FT REPEAT 128..167
FT /note="ARM 1"
FT REPEAT 168..211
FT /note="ARM 2"
FT REPEAT 212..251
FT /note="ARM 3"
FT REPEAT 254..293
FT /note="ARM 4"
FT REPEAT 294..337
FT /note="ARM 5"
FT REPEAT 338..377
FT /note="ARM 6"
FT REPEAT 379..416
FT /note="ARM 7"
FT REPEAT 419..460
FT /note="ARM 8"
FT REPEAT 466..506
FT /note="ARM 9"
FT REPEAT 508..547
FT /note="ARM 10"
FT REPEAT 570..609
FT /note="ARM 11"
FT REPEAT 611..657
FT /note="ARM 12"
FT CONFLICT 185
FT /note="I -> V (in Ref. 3; CAA47463)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> T (in Ref. 3; CAA47463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 81711 MW; 569DBE69D08BBC58 CRC64;
MDLGDVVEMP MKVTEWQKTY TYDSGINSGI NTSVPSLNGK MVIEDDSLAY PNSYTTVKTT
TYTQQQNPDM ESHLNMTRAQ RVRAAMYPET VEDHSYLFST QIEGQQTNVQ KLAEPSQMLK
SAIMHLINYQ DDAELATRAI PELTKLLNDE DPMVVNKASM IVNQLSKKEA SRKALMQSPQ
IVAAIVRTMQ HTSDMDTARC TTSILHNLSH HREGLLSIFK SGGIPALVRM LSSPVESVLF
YAITTLHNLL LYQEGAKMAV RLADGLQKMV PLLNKNNPKF LAITTDCLQL LAYGNQESKL
IILGNGGPQG LVQIMRNYNY EKLLWTTSRV LKVLSVCPSN KPAIVEAGGM QALGKHLTSN
SPRLVQNCLW TLRNLSDVAT KQEGLDNVLK ILVNQLSSDD VNVLTCATGT LSNLTCNNGR
NKTLVTQSNG VESLIHTILR ASDKDDIAEP AVCAMRHLTS RHQDAEVAQN SVRLHYGIPA
IVKLLNPPYQ WPLVKATIGL IRNLALCPAN HAPLYDAGVI PRLVQLLVKS HQDAQRHAAS
GTQQPYTDGV KMEEIVEGCT GALHILARDP VNRMDIYKLN TIPLFVQLLY SPVENIQRVS
SGVLCELAQD KEAADTIDAE GASAPLMELL HSRNEGIATY AAAVLFRISE DKNADYRKRV
SVELTNAIFR QDPAAWEAAQ SMIPLNDPYS DEMENYRAMY PEDIPLEPMG GDMDVEYAMD
GYSDHPGRGH YADNHMMA
