PKP4_HUMAN
ID PKP4_HUMAN Reviewed; 1192 AA.
AC Q99569; Q86W91;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Plakophilin-4;
DE AltName: Full=p0071;
GN Name=PKP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Frontal cortex;
RX PubMed=8937994; DOI=10.1242/jcs.109.11.2767;
RA Hatzfeld M., Nachtsheim C.;
RT "Cloning and characterization of a new armadillo family member, p0071,
RT associated with the junctional plaque: evidence for a subfamily of closely
RT related proteins.";
RL J. Cell Sci. 109:2767-2778(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-406 AND TYR-415, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP FUNCTION, INTERACTION WITH ECT2 AND RHOA, AND SUBCELLULAR LOCATION.
RX PubMed=17115030; DOI=10.1038/ncb1504;
RA Wolf A., Keil R., Gotzl O., Mun A., Schwarze K., Lederer M.,
RA Huttelmaier S., Hatzfeld M.;
RT "The armadillo protein p0071 regulates Rho signalling during cytokinesis.";
RL Nat. Cell Biol. 8:1432-1440(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-403 AND SER-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-281; SER-314 AND
RP SER-327, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP INTERACTION WITH FRMPD2.
RX PubMed=19706687; DOI=10.1242/jcs.046854;
RA Stenzel N., Fetzer C.P., Heumann R., Erdmann K.S.;
RT "PDZ-domain-directed basolateral targeting of the peripheral membrane
RT protein FRMPD2 in epithelial cells.";
RL J. Cell Sci. 122:3374-3384(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; SER-231 AND SER-776, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-106; SER-221;
RP SER-231; SER-236; SER-281; SER-314; SER-327; SER-337; SER-392; SER-406 AND
RP SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-221; SER-337; SER-392
RP AND SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH CCDC85B.
RX PubMed=25009281; DOI=10.1091/mbc.e13-08-0492;
RA Markham N.O., Doll C.A., Dohn M.R., Miller R.K., Yu H., Coffey R.J.,
RA McCrea P.D., Gamse J.T., Reynolds A.B.;
RT "DIPA-family coiled-coils bind conserved isoform-specific head domain of
RT p120-catenin family: potential roles in hydrocephalus and heterotopia.";
RL Mol. Biol. Cell 25:2592-2603(2014).
RN [20]
RP TISSUE SPECIFICITY.
RX PubMed=29034528; DOI=10.1111/ced.13214;
RA Abreu-Velez A.M., Valencia-Yepes C.A., Upegui-Zapata Y.A.,
RA Upegui-Quiceno E., Mesa-Herrera N.R., Velazquez-Velez J.E., Howard M.S.;
RT "Patients with a new variant of endemic pemphigus foliaceus have
RT autoantibodies against arrector pili muscle, colocalizing with MYZAP,
RT p0071, desmoplakins 1 and 2 and ARVCF.";
RL Clin. Exp. Dermatol. 42:874-880(2017).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=30479852; DOI=10.5826/dpc.0804a02;
RA Abreu-Velez A.M., Howard M.S., Padilla H.J.L., Tobon-Arroyave S.;
RT "Subclinical oral involvement in patients with endemic pemphigus
RT foliaceus.";
RL Dermatol. Pract. Concept. 8:252-261(2018).
CC -!- FUNCTION: Plays a role as a regulator of Rho activity during
CC cytokinesis. May play a role in junctional plaques.
CC {ECO:0000269|PubMed:17115030}.
CC -!- SUBUNIT: Interacts with PDZD2 (By similarity). Interacts (via the C-
CC terminus) with FRMPD2 (via the PDZ 2 domain). Interacts with RHOA; the
CC interaction is detected at the midbody. Interacts with ECT2; the
CC interaction is detected at the midbody. Interacts with CCDC85B
CC (PubMed:25009281). {ECO:0000250, ECO:0000269|PubMed:17115030,
CC ECO:0000269|PubMed:19706687, ECO:0000269|PubMed:25009281}.
CC -!- INTERACTION:
CC Q99569; Q8N5M1: ATPAF2; NbExp=4; IntAct=EBI-726447, EBI-1166928;
CC Q99569; Q12959: DLG1; NbExp=3; IntAct=EBI-726447, EBI-357481;
CC Q99569; Q96RT1: ERBIN; NbExp=4; IntAct=EBI-726447, EBI-993903;
CC Q99569; Q96RT1-2: ERBIN; NbExp=4; IntAct=EBI-726447, EBI-8449250;
CC Q99569; Q08379: GOLGA2; NbExp=3; IntAct=EBI-726447, EBI-618309;
CC Q99569; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-726447, EBI-741037;
CC Q99569; Q14160: SCRIB; NbExp=4; IntAct=EBI-726447, EBI-357345;
CC Q99569; P36406: TRIM23; NbExp=3; IntAct=EBI-726447, EBI-740098;
CC Q99569-2; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-4324902, EBI-1166928;
CC Q99569-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-4324902, EBI-618309;
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000269|PubMed:17115030}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:17115030}. Midbody {ECO:0000269|PubMed:17115030}.
CC Cell membrane {ECO:0000269|PubMed:17115030}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17115030}. Note=Associated with the
CC pericentrosomal region in interphase and with spindle poles during
CC mitosis. In anaphase, during chromosome segregation, is recruited to
CC the central microtubule bundle, focussed at the spindle midzone and
CC ultimately localizes to the midbody at cytokinesis. Constituent of the
CC midbody cytoskeletal matrix. Colocalized with desmoplakin at desmosomal
CC junctional plaques in cultured epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q99569-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q99569-2; Sequence=VSP_006737;
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands (at protein level)
CC (PubMed:30479852). Expressed in arrector pili muscle (at protein level)
CC (PubMed:29034528). {ECO:0000269|PubMed:29034528,
CC ECO:0000269|PubMed:30479852}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA57478.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA57478.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X81889; CAA57478.1; ALT_SEQ; mRNA.
DR EMBL; AC005042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050308; AAH50308.1; -; mRNA.
DR CCDS; CCDS33305.1; -. [Q99569-1]
DR CCDS; CCDS33306.1; -. [Q99569-2]
DR RefSeq; NP_001005476.1; NM_001005476.2. [Q99569-2]
DR RefSeq; NP_001291898.1; NM_001304969.1.
DR RefSeq; NP_001291899.1; NM_001304970.1.
DR RefSeq; NP_003619.2; NM_003628.4. [Q99569-1]
DR RefSeq; XP_011510318.1; XM_011512016.1.
DR AlphaFoldDB; Q99569; -.
DR SMR; Q99569; -.
DR BioGRID; 114074; 152.
DR IntAct; Q99569; 60.
DR MINT; Q99569; -.
DR STRING; 9606.ENSP00000374409; -.
DR GlyGen; Q99569; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99569; -.
DR PhosphoSitePlus; Q99569; -.
DR SwissPalm; Q99569; -.
DR BioMuta; PKP4; -.
DR DMDM; 313104155; -.
DR EPD; Q99569; -.
DR jPOST; Q99569; -.
DR MassIVE; Q99569; -.
DR MaxQB; Q99569; -.
DR PaxDb; Q99569; -.
DR PeptideAtlas; Q99569; -.
DR PRIDE; Q99569; -.
DR ProteomicsDB; 78328; -. [Q99569-1]
DR ProteomicsDB; 78329; -. [Q99569-2]
DR Antibodypedia; 33712; 183 antibodies from 29 providers.
DR DNASU; 8502; -.
DR Ensembl; ENST00000389757.7; ENSP00000374407.3; ENSG00000144283.23. [Q99569-2]
DR Ensembl; ENST00000389759.8; ENSP00000374409.3; ENSG00000144283.23. [Q99569-1]
DR GeneID; 8502; -.
DR KEGG; hsa:8502; -.
DR MANE-Select; ENST00000389759.8; ENSP00000374409.3; NM_003628.6; NP_003619.2.
DR UCSC; uc002tzv.4; human. [Q99569-1]
DR CTD; 8502; -.
DR DisGeNET; 8502; -.
DR GeneCards; PKP4; -.
DR HGNC; HGNC:9026; PKP4.
DR HPA; ENSG00000144283; Tissue enhanced (brain, choroid plexus).
DR MIM; 604276; gene.
DR neXtProt; NX_Q99569; -.
DR OpenTargets; ENSG00000144283; -.
DR PharmGKB; PA33359; -.
DR VEuPathDB; HostDB:ENSG00000144283; -.
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000155773; -.
DR HOGENOM; CLU_007897_0_0_1; -.
DR InParanoid; Q99569; -.
DR OMA; KIEVCRL; -.
DR OrthoDB; 233858at2759; -.
DR PhylomeDB; Q99569; -.
DR TreeFam; TF321877; -.
DR PathwayCommons; Q99569; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q99569; -.
DR BioGRID-ORCS; 8502; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; PKP4; human.
DR GeneWiki; PKP4; -.
DR GenomeRNAi; 8502; -.
DR Pharos; Q99569; Tbio.
DR PRO; PR:Q99569; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q99569; protein.
DR Bgee; ENSG00000144283; Expressed in C1 segment of cervical spinal cord and 191 other tissues.
DR ExpressionAtlas; Q99569; baseline and differential.
DR Genevisible; Q99569; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030057; C:desmosome; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028443; Plakophilin-4.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF8; PTHR10372:SF8; 1.
DR Pfam; PF00514; Arm; 3.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1192
FT /note="Plakophilin-4"
FT /id="PRO_0000064289"
FT REPEAT 415..455
FT /note="ARM 1"
FT REPEAT 518..557
FT /note="ARM 2"
FT REPEAT 560..599
FT /note="ARM 3"
FT REPEAT 604..644
FT /note="ARM 4"
FT REPEAT 660..702
FT /note="ARM 5"
FT REPEAT 706..751
FT /note="ARM 6"
FT REPEAT 815..855
FT /note="ARM 7"
FT REPEAT 862..901
FT /note="ARM 8"
FT REPEAT 950..993
FT /note="ARM 9"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..70
FT /evidence="ECO:0000255"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 270
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 415
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 478
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1013
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 1017
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FH0"
FT VAR_SEQ 1043..1085
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8937994"
FT /id="VSP_006737"
FT CONFLICT 41
FT /note="V -> M (in Ref. 3; AAH50308)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> Y (in Ref. 3; AAH50308)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="G -> W (in Ref. 3; AAH50308)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> V (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="S -> V (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="S -> V (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="V -> S (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="Q -> E (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="S -> T (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 766
FT /note="N -> D (in Ref. 3; AAH50308)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="G -> S (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="R -> G (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="V -> G (in Ref. 1; CAA57478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1192 AA; 131868 MW; 48EA1579E323E019 CRC64;
MPAPEQASLV EEGQPQTRQE AASTGPGMEP ETTATTILAS VKEQELQFQR LTRELEVERQ
IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNTGV SKPRVSDAVQ PNNYLIRTEP
EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN SYSDSGYQEA GSFHNSQNVS KADNRQQHSF
IGSTNNHVVR NSRAEGQTLV QPSVANRAMR RVSSVPSRAQ SPSYVISTGV SPSRGSLRTS
LGSGFGSPSV TDPRPLNPSA YSSTTLPAAR AASPYSQRPA SPTAIRRIGS VTSRQTSNPN
GPTPQYQTTA RVGSPLTLTD AQTRVASPSQ GQVGSSSPKR SGMTAVPQHL GPSLQRTVHD
MEQFGQQQYD IYERMVPPRP DSLTGLRSSY ASQHSQLGQD LRSAVSPDLH ITPIYEGRTY
YSPVYRSPNH GTVELQGSQT ALYRTGSVGI GNLQRTSSQR STLTYQRNNY ALNTTATYAE
PYRPIQYRVQ ECNYNRLQHA VPADDGTTRS PSIDSIQKDP REFAWRDPEL PEVIHMLQHQ
FPSVQANAAA YLQHLCFGDN KVKMEVCRLG GIKHLVDLLD HRVLEVQKNA CGALRNLVFG
KSTDENKIAM KNVGGIPALL RLLRKSIDAE VRELVTGVLW NLSSCDAVKM TIIRDALSTL
TNTVIVPHSG WNNSSFDDDH KIKFQTSLVL RNTTGCLRNL SSAGEEARKQ MRSCEGLVDS
LLYVIHTCVN TSDYDSKTVE NCVCTLRNLS YRLELEVPQA RLLGLNELDD LLGKESPSKD
SEPSCWGKKK KKKKRTPQED QWDGVGPIPG LSKSPKGVEM LWHPSVVKPY LTLLAESSNP
ATLEGSAGSL QNLSAGNWKF AAYIRAAVRK EKGLPILVEL LRMDNDRVVS SVATALRNMA
LDVRNKELIG KYAMRDLVNR LPGGNGPSVL SDETMAAICC ALHEVTSKNM ENAKALADSG
GIEKLVNITK GRGDRSSLKV VKAAAQVLNT LWQYRDLRSI YKKDGWNQNH FITPVSTLER
DRFKSHPSLS TTNQQMSPII QSVGSTSSSP ALLGIRDPRS EYDRTQPPMQ YYNSQGDATH
KGLYPGSSKP SPIYISSYSS PAREQNRRLQ HQQLYYSQDD SNRKNFDAYR LYLQSPHSYE
DPYFDDRVHF PASTDYSTQY GLKSTTNYVD FYSTKRPSYR AEQYPGSPDS WV
