ID PKP3_MOUSE Reviewed; 797 AA. AC Q9QY23; A4QPD8; Q0VGP3; Q3KQL7; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 2. DT 25-MAY-2022, entry version 141. DE RecName: Full=Plakophilin-3; GN Name=Pkp3; 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 [MRNA] (ISOFORM 1). RX PubMed=10381383; DOI=10.1242/jcs.112.14.2265; RA Bonne S., van Hengel J., Nollet F., Kools P., van Roy F.; RT "Plakophilin-3, a novel armadillo-like protein present in nuclei and RT desmosomes of epithelial cells."; RL J. Cell Sci. 112:2265-2276(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, and Eye; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-180 AND SER-331, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Kidney, Lung, and Pancreas; 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). RN [5] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-261, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: May play a role in junctional plaques. CC -!- SUBCELLULAR LOCATION: Nucleus. Cell junction, desmosome. Note=Nuclear CC and associated with desmosomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9QY23-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9QY23-2; Sequence=VSP_026139; 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; AF136719; AAD55892.1; -; mRNA. DR EMBL; BC090668; AAH90668.1; -; mRNA. DR EMBL; BC106141; AAI06142.1; -; mRNA. DR EMBL; BC139775; AAI39776.1; -; mRNA. DR CCDS; CCDS21999.1; -. [Q9QY23-1] DR CCDS; CCDS52437.1; -. [Q9QY23-2] DR RefSeq; NP_001156396.1; NM_001162924.1. [Q9QY23-2] DR RefSeq; NP_062736.2; NM_019762.2. [Q9QY23-1] DR AlphaFoldDB; Q9QY23; -. DR SMR; Q9QY23; -. DR BioGRID; 207999; 6. DR IntAct; Q9QY23; 2. DR STRING; 10090.ENSMUSP00000101654; -. DR iPTMnet; Q9QY23; -. DR PhosphoSitePlus; Q9QY23; -. DR MaxQB; Q9QY23; -. DR PaxDb; Q9QY23; -. DR PeptideAtlas; Q9QY23; -. DR PRIDE; Q9QY23; -. DR ProteomicsDB; 289754; -. [Q9QY23-1] DR ProteomicsDB; 289755; -. [Q9QY23-2] DR Antibodypedia; 4571; 287 antibodies from 33 providers. DR DNASU; 56460; -. DR Ensembl; ENSMUST00000066873; ENSMUSP00000069961; ENSMUSG00000054065. [Q9QY23-1] DR Ensembl; ENSMUST00000106039; ENSMUSP00000101654; ENSMUSG00000054065. [Q9QY23-2] DR GeneID; 56460; -. DR KEGG; mmu:56460; -. DR UCSC; uc009kjh.2; mouse. [Q9QY23-2] DR UCSC; uc009kji.2; mouse. [Q9QY23-1] DR CTD; 11187; -. DR MGI; MGI:1891830; Pkp3. DR VEuPathDB; HostDB:ENSMUSG00000054065; -. DR eggNOG; KOG1048; Eukaryota. DR GeneTree; ENSGT00940000159515; -. DR HOGENOM; CLU_009111_2_0_1; -. DR InParanoid; Q9QY23; -. DR OMA; LDWPEAS; -. DR OrthoDB; 233858at2759; -. DR PhylomeDB; Q9QY23; -. DR TreeFam; TF321877; -. DR Reactome; R-MMU-6805567; Keratinization. DR Reactome; R-MMU-6809371; Formation of the cornified envelope. DR BioGRID-ORCS; 56460; 0 hits in 73 CRISPR screens. DR ChiTaRS; Pkp3; mouse. DR PRO; PR:Q9QY23; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q9QY23; protein. DR Bgee; ENSMUSG00000054065; Expressed in lip and 210 other tissues. DR Genevisible; Q9QY23; MM. DR GO; GO:0005912; C:adherens junction; IBA:GO_Central. DR GO; GO:0030054; C:cell junction; ISO:MGI. DR GO; GO:0001533; C:cornified envelope; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030057; C:desmosome; IDA:MGI. DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0005914; C:spot adherens junction; ISS:MGI. DR GO; GO:0045294; F:alpha-catenin binding; ISO:MGI. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central. DR GO; GO:0002159; P:desmosome assembly; ISO:MGI. DR GO; GO:1902373; P:negative regulation of mRNA catabolic process; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; ISO: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; IPR028434; Plakophilin-3. DR InterPro; IPR028435; Plakophilin/d_Catenin. DR PANTHER; PTHR10372; PTHR10372; 1. DR PANTHER; PTHR10372:SF1; PTHR10372:SF1; 1. DR Pfam; PF00514; Arm; 2. DR SMART; SM00185; ARM; 4. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS50176; ARM_REPEAT; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell adhesion; Cell junction; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..797 FT /note="Plakophilin-3" FT /id="PRO_0000064288" FT REPEAT 305..348 FT /note="ARM 1" FT REPEAT 351..390 FT /note="ARM 2" FT REPEAT 393..432 FT /note="ARM 3" FT REPEAT 449..487 FT /note="ARM 4" FT REPEAT 491..536 FT /note="ARM 5" FT REPEAT 596..637 FT /note="ARM 6" FT REPEAT 645..684 FT /note="ARM 7" FT REPEAT 689..730 FT /note="ARM 8" FT REGION 58..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 253..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 81 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 250 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 261 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y446" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1..12 FT /note="MQEGNFLLSALQ -> MEPTAGSRTRMEPRRNCPTAGTSRMSQGASGGQTSG FT K (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_026139" FT CONFLICT 182 FT /note="R -> P (in Ref. 1; AAD55892)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="E -> K (in Ref. 1; AAD55892)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="A -> P (in Ref. 1; AAD55892)" FT /evidence="ECO:0000305" SQ SEQUENCE 797 AA; 87333 MW; C2ECF73BDE7323B1 CRC64; MQEGNFLLSA LQPETGVCSL ALPSDLQLDR RGAEGPEADR LRAARVQEQV RARLLQLGQQ SRHNGSAELD GSAESARGMP RGQYHTMQTG FSSRSQGMSG DKTSTFRPIA KPAYSPASWS SRSAVDLTCS RRLSSAHNGG SAFGAVGYGG TQPTPPMPTR PVSFHERGGA ASRADYDTLS LRSLRLGPGG LDDRYSVVSE QLEPAAASTY RAYAYERQAS SGSSRAGGLD WPEATEGPPS RTIRAPAMRT LQRFQSSHRS RGGTGSVSGA GLEPVARAPS VRSLSLSLAD SGHLPDVRGL DSYTGHRTLQ RLSSGFDDID LPSAVKYLMA SDPNLQVLGA AYIQHRCYSD AAAKKQARSL QAVPRLVKLF NHANQEVQRH ATGAMRNLIY DNVDNKLALV EENGIFELLR TLREQDDELR KNVTGILWNL SSSDHLKDRL ARDTLEQLTD LVLSPLSGAG GPPLIQQNAS EAEIFYNATG FLRNLSSASQ ATRQKMRECH GLVDALVTYI NHALDVGKCE DKSVENAVCV LRNLSYRLYD EMPPSALQRL EGRGRRDMAG APPGEMVGCF TPQSRRLREL PLTADALTFA EVSKDPKGLE WLWSPQIVGL YNRLLQRCEL NRHTTEAAAG ALQNITAGDR RWAGVLSRLA LEQERILNPL LDRVRTADHN QLRSLTGLIR NLSRNARNKD EMSTKVVSHL IEKLPGSVGE KCPPAEVLVN IIAVLNNLVV ASPIAARDLL YFDGLRKLVF IKKKRDSPDS EKSSRAASSL LANLWQYSKL HRDFRAKGYR KEDFLGP //