ID DSG2_HUMAN Reviewed; 1118 AA. AC Q14126; Q4KKU6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 212. DE RecName: Full=Desmoglein-2; DE AltName: Full=Cadherin family member 5; DE AltName: Full=HDGC; DE Flags: Precursor; GN Name=DSG2; Synonyms=CDHF5; 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]. RC TISSUE=Colon carcinoma; RX PubMed=8143788; DOI=10.1006/excr.1994.1103; RA Schaefer S., Koch P.J., Franke W.W.; RT "Identification of the ubiquitous human desmoglein, Dsg2, and the RT expression catalogue of the desmoglein subfamily of desmosomal cadherins."; RL Exp. Cell Res. 211:391-399(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 778-1118. RX PubMed=1935985; RA Koch P.J., Goldschmidt M.D., Walsh M.J., Zimbelmann R., Franke W.W.; RT "Complete amino acid sequence of the epidermal desmoglein precursor RT polypeptide and identification of a second type of desmoglein gene."; RL Eur. J. Cell Biol. 55:200-208(1991). RN [4] RP INTERACTION WITH PKP2. RX PubMed=11790773; DOI=10.1074/jbc.m108765200; RA Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J.; RT "Protein binding and functional characterization of plakophilin 2. Evidence RT for its diverse roles in desmosomes and beta -catenin signaling."; RL J. Biol. Chem. 277:10512-10522(2002). RN [5] RP GLYCOSYLATION AT ASN-112. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, 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-680, AND IDENTIFICATION BY RP 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112 AND ASN-182. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP GLYCOSYLATION AT ASN-462. RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., RA Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core fucosylated RT glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182 AND ASN-462. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, 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-680 AND SER-1118, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680 AND SER-703, AND RP IDENTIFICATION BY 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; SER-723 AND SER-726, AND RP 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 SER-680; SER-700; THR-804; RP SER-806; SER-810; SER-815 AND THR-922, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 PALMITOYLATION, AND SUBCELLULAR LOCATION. RX PubMed=31402609; DOI=10.15252/embr.201847472; RA Woodley K.T., Collins M.O.; RT "S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate RT cell adhesion."; RL EMBO Rep. 20:e47472-e47472(2019). RN [20] RP STRUCTURE BY NMR OF 47-162. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first cadherin domain from human desmoglein-2."; RL Submitted (OCT-2007) to the PDB data bank. RN [21] RP VARIANTS ARVD10 GLN-46; HIS-49; TYR-507 AND CYS-812. RX PubMed=16773573; DOI=10.1086/504393; RA Awad M.M., Dalal D., Cho E., Amat-Alarcon N., James C., Tichnell C., RA Tucker A., Russell S.D., Bluemke D.A., Dietz H.C., Calkins H., Judge D.P.; RT "DSG2 mutations contribute to arrhythmogenic right ventricular RT dysplasia/cardiomyopathy."; RL Am. J. Hum. Genet. 79:136-142(2006). RN [22] RP VARIANTS MET-56; GLY-158; VAL-293; LYS-713; LYS-773 AND GLY-920, AND RP INVOLVEMENT IN SUSCEPTIBILITY TO CMD1BB. RX PubMed=18678517; DOI=10.1016/j.ymgme.2008.06.005; RA Posch M.G., Posch M.J., Geier C., Erdmann B., Mueller W., Richter A., RA Ruppert V., Pankuweit S., Maisch B., Perrot A., Buttgereit J., Dietz R., RA Haverkamp W., Ozcelik C.; RT "A missense variant in desmoglein-2 predisposes to dilated RT cardiomyopathy."; RL Mol. Genet. Metab. 95:74-80(2008). RN [23] RP VARIANTS ARVD10 GLN-46; HIS-49; ALA-335; TYR-507 AND CYS-812, AND VARIANT RP MET-56. RX PubMed=20031617; DOI=10.1161/circgenetics.109.858217; RA den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., RA Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., RA Bluemke D.A., Calkins H., Dalal D., Judge D.P.; RT "Comprehensive desmosome mutation analysis in North Americans with RT arrhythmogenic right ventricular dysplasia/cardiomyopathy."; RL Circ. Cardiovasc. Genet. 2:428-435(2009). RN [24] RP VARIANT ARVD10 HIS-49, AND VARIANTS VAL-293; LYS-713; LYS-773 AND GLY-920. RX PubMed=19863551; DOI=10.1111/j.1399-0004.2009.01282.x; RA Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., RA Robb L., Talajic M., Brugada R.; RT "Role of genetic testing in arrhythmogenic right ventricular RT cardiomyopathy/dysplasia."; RL Clin. Genet. 77:37-48(2010). RN [25] RP VARIANT ARVD10 HIS-49. RX PubMed=21062920; DOI=10.1093/cvr/cvq353; RA Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., RA Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., RA Saffitz J.E., Protonotarios N., McKenna W.J.; RT "Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy RT caused by desmocollin-2 mutations."; RL Cardiovasc. Res. 90:77-87(2011). CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in CC the interaction of plaque proteins and intermediate filaments mediating CC cell-cell adhesion. CC -!- SUBUNIT: Interacts with PKP2. {ECO:0000269|PubMed:11790773}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31402609}; CC Single-pass type I membrane protein. Cell junction, desmosome CC {ECO:0000269|PubMed:31402609}. CC -!- TISSUE SPECIFICITY: All of the tissues tested and carcinomas. CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each CC cadherin domain and rigidify the connections, imparting a strong CC curvature to the full-length ectodomain. {ECO:0000305}. CC -!- PTM: Palmitoylated by ZDHHC5 at the plasma membrane. CC {ECO:0000269|PubMed:31402609}. CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 10 CC (ARVD10) [MIM:610193]: A congenital heart disease characterized by CC infiltration of adipose and fibrous tissue into the right ventricle and CC loss of myocardial cells, resulting in ventricular and supraventricular CC arrhythmias. {ECO:0000269|PubMed:16773573, ECO:0000269|PubMed:19863551, CC ECO:0000269|PubMed:20031617, ECO:0000269|PubMed:21062920}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cardiomyopathy, dilated, 1BB (CMD1BB) [MIM:612877]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:18678517}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40367/DSG2"; 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; Z26317; CAA81226.1; -; mRNA. DR EMBL; BC099655; AAH99655.1; -; mRNA. DR EMBL; BC099656; AAH99656.1; -; mRNA. DR EMBL; BC099657; AAH99657.1; -; mRNA. DR CCDS; CCDS42423.1; -. DR PIR; S38673; S38673. DR RefSeq; NP_001934.2; NM_001943.4. DR PDB; 2YQG; NMR; -; A=47-162. DR PDB; 5ERD; X-ray; 2.90 A; A/B=50-602. DR PDB; 5J5J; X-ray; 3.29 A; A=152-601. DR PDB; 6QNT; EM; 3.50 A; D=157-380. DR PDB; 6QNU; EM; 3.80 A; D/E=157-380. DR PDB; 6SIT; X-ray; 4.50 A; D=149-386. DR PDB; 7A7D; EM; 26.00 A; A/B/C/D/E/F/G=50-603. DR PDB; 7AGF; EM; 3.10 A; D/E/F=149-386. DR PDB; 7AGG; EM; 3.30 A; D/F=149-386. DR PDB; 8QJX; EM; 3.30 A; D/E=1-1118. DR PDB; 8QJY; EM; 3.50 A; D=1-1118. DR PDB; 8QK3; EM; 3.20 A; D=1-1118. DR PDBsum; 2YQG; -. DR PDBsum; 5ERD; -. DR PDBsum; 5J5J; -. DR PDBsum; 6QNT; -. DR PDBsum; 6QNU; -. DR PDBsum; 6SIT; -. DR PDBsum; 7A7D; -. DR PDBsum; 7AGF; -. DR PDBsum; 7AGG; -. DR PDBsum; 8QJX; -. DR PDBsum; 8QJY; -. DR PDBsum; 8QK3; -. DR AlphaFoldDB; Q14126; -. DR EMDB; EMD-11678; -. DR EMDB; EMD-11778; -. DR EMDB; EMD-11779; -. DR EMDB; EMD-18453; -. DR EMDB; EMD-18454; -. DR EMDB; EMD-18455; -. DR EMDB; EMD-4608; -. DR EMDB; EMD-4609; -. DR SASBDB; Q14126; -. DR SMR; Q14126; -. DR BioGRID; 108163; 269. DR DIP; DIP-46250N; -. DR IntAct; Q14126; 94. DR MINT; Q14126; -. DR STRING; 9606.ENSP00000261590; -. DR GlyConnect; 1172; 41 N-Linked glycans (5 sites). DR GlyCosmos; Q14126; 8 sites, 41 glycans. DR GlyGen; Q14126; 12 sites, 40 N-linked glycans (5 sites), 2 O-linked glycans (3 sites). DR iPTMnet; Q14126; -. DR PhosphoSitePlus; Q14126; -. DR SwissPalm; Q14126; -. DR BioMuta; DSG2; -. DR DMDM; 148876773; -. DR CPTAC; CPTAC-1307; -. DR EPD; Q14126; -. DR jPOST; Q14126; -. DR MassIVE; Q14126; -. DR MaxQB; Q14126; -. DR PaxDb; 9606-ENSP00000261590; -. DR PeptideAtlas; Q14126; -. DR ProteomicsDB; 59829; -. DR Antibodypedia; 1349; 831 antibodies from 41 providers. DR DNASU; 1829; -. DR Ensembl; ENST00000261590.13; ENSP00000261590.8; ENSG00000046604.14. DR GeneID; 1829; -. DR KEGG; hsa:1829; -. DR MANE-Select; ENST00000261590.13; ENSP00000261590.8; NM_001943.5; NP_001934.2. DR UCSC; uc002kwu.5; human. DR AGR; HGNC:3049; -. DR CTD; 1829; -. DR DisGeNET; 1829; -. DR GeneCards; DSG2; -. DR GeneReviews; DSG2; -. DR HGNC; HGNC:3049; DSG2. DR HPA; ENSG00000046604; Tissue enhanced (parathyroid). DR MalaCards; DSG2; -. DR MIM; 125671; gene. DR MIM; 610193; phenotype. DR MIM; 612877; phenotype. DR neXtProt; NX_Q14126; -. DR OpenTargets; ENSG00000046604; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 293888; Inherited isolated arrhythmogenic cardiomyopathy, dominant-left variant. DR Orphanet; 293910; Inherited isolated arrhythmogenic cardiomyopathy, dominant-right variant. DR Orphanet; 293899; Inherited isolated arrhythmogenic ventricular dysplasia, biventricular variant. DR PharmGKB; PA27502; -. DR VEuPathDB; HostDB:ENSG00000046604; -. DR eggNOG; KOG3594; Eukaryota. DR GeneTree; ENSGT01030000234624; -. DR HOGENOM; CLU_005284_0_1_1; -. DR InParanoid; Q14126; -. DR OMA; PAHARYV; -. DR OrthoDB; 5314152at2759; -. DR PhylomeDB; Q14126; -. DR TreeFam; TF331809; -. DR PathwayCommons; Q14126; -. DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR SignaLink; Q14126; -. DR BioGRID-ORCS; 1829; 18 hits in 1160 CRISPR screens. DR ChiTaRS; DSG2; human. DR EvolutionaryTrace; Q14126; -. DR GeneWiki; Desmoglein_2; -. DR GenomeRNAi; 1829; -. DR Pharos; Q14126; Tbio. DR PRO; PR:Q14126; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q14126; Protein. DR Bgee; ENSG00000046604; Expressed in mucosa of sigmoid colon and 162 other cell types or tissues. DR ExpressionAtlas; Q14126; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc. DR GO; GO:0001533; C:cornified envelope; TAS:Reactome. DR GO; GO:0030057; C:desmosome; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0086083; F:cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; IC:BHF-UCL. DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0002934; P:desmosome organization; IMP:BHF-UCL. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:BHF-UCL. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl. DR GO; GO:0003165; P:Purkinje myocyte development; IMP:BHF-UCL. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL. DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR CDD; cd11304; Cadherin_repeat; 3. DR Gene3D; 2.60.40.60; Cadherins; 5. DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR027397; Catenin-bd_sf. DR InterPro; IPR009122; Desmosomal_cadherin. DR PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1. DR PANTHER; PTHR24025:SF1; DESMOGLEIN-2; 1. DR Pfam; PF00028; Cadherin; 3. DR PRINTS; PR00205; CADHERIN. DR PRINTS; PR01818; DESMOCADHERN. DR PRINTS; PR01819; DESMOGLEIN. DR SMART; SM00112; CA; 4. DR SUPFAM; SSF49313; Cadherin-like; 5. DR PROSITE; PS00232; CADHERIN_1; 3. DR PROSITE; PS50268; CADHERIN_2; 4. DR Genevisible; Q14126; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cardiomyopathy; Cell adhesion; Cell junction; KW Cell membrane; Cleavage on pair of basic residues; Disease variant; KW Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate; KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT PROPEP 24..49 FT /evidence="ECO:0000255" FT /id="PRO_0000003845" FT CHAIN 50..1118 FT /note="Desmoglein-2" FT /id="PRO_0000003846" FT TOPO_DOM 50..609 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 610..634 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 635..1118 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 50..160 FT /note="Cadherin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 161..273 FT /note="Cadherin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 274..388 FT /note="Cadherin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT DOMAIN 389..503 FT /note="Cadherin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043" FT REPEAT 881..912 FT /note="Desmoglein repeat 1" FT REPEAT 913..942 FT /note="Desmoglein repeat 2" FT REPEAT 943..968 FT /note="Desmoglein repeat 3" FT REPEAT 969..992 FT /note="Desmoglein repeat 4" FT REPEAT 993..1021 FT /note="Desmoglein repeat 5" FT REPEAT 1022..1051 FT /note="Desmoglein repeat 6" FT REGION 1068..1118 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1092..1118 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 680 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 700 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 703 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 723 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 726 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 804 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 806 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 810 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 815 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 922 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1118 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT CARBOHYD 112 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973" FT CARBOHYD 309 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 462 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 514 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 46 FT /note="R -> Q (in ARVD10; dbSNP:rs121913008)" FT /evidence="ECO:0000269|PubMed:16773573, FT ECO:0000269|PubMed:20031617" FT /id="VAR_029365" FT VARIANT 49 FT /note="R -> H (in ARVD10; dbSNP:rs121913006)" FT /evidence="ECO:0000269|PubMed:16773573, FT ECO:0000269|PubMed:19863551, ECO:0000269|PubMed:20031617, FT ECO:0000269|PubMed:21062920" FT /id="VAR_029366" FT VARIANT 56 FT /note="V -> M (probable risk factor for CMD1BB and ARVD10; FT dbSNP:rs121913013)" FT /evidence="ECO:0000269|PubMed:18678517, FT ECO:0000269|PubMed:20031617" FT /id="VAR_062387" FT VARIANT 89 FT /note="Y -> C (in dbSNP:rs2230232)" FT /id="VAR_048508" FT VARIANT 158 FT /note="V -> G (in dbSNP:rs191143292)" FT /evidence="ECO:0000269|PubMed:18678517" FT /id="VAR_062388" FT VARIANT 293 FT /note="I -> V (in dbSNP:rs2230234)" FT /evidence="ECO:0000269|PubMed:18678517, FT ECO:0000269|PubMed:19863551" FT /id="VAR_048509" FT VARIANT 335 FT /note="T -> A (in ARVD10; dbSNP:rs191564916)" FT /evidence="ECO:0000269|PubMed:20031617" FT /id="VAR_065686" FT VARIANT 507 FT /note="C -> Y (in ARVD10; dbSNP:rs121913009)" FT /evidence="ECO:0000269|PubMed:16773573, FT ECO:0000269|PubMed:20031617" FT /id="VAR_029367" FT VARIANT 515 FT /note="V -> I (in dbSNP:rs2230235)" FT /id="VAR_048510" FT VARIANT 713 FT /note="E -> K (in dbSNP:rs79241126)" FT /evidence="ECO:0000269|PubMed:18678517, FT ECO:0000269|PubMed:19863551" FT /id="VAR_062389" FT VARIANT 773 FT /note="R -> K (in dbSNP:rs2278792)" FT /evidence="ECO:0000269|PubMed:18678517, FT ECO:0000269|PubMed:19863551" FT /id="VAR_048511" FT VARIANT 812 FT /note="G -> C (in ARVD10; dbSNP:rs121913010)" FT /evidence="ECO:0000269|PubMed:16773573, FT ECO:0000269|PubMed:20031617" FT /id="VAR_029368" FT VARIANT 863 FT /note="M -> L (in dbSNP:rs16962093)" FT /id="VAR_048512" FT VARIANT 903 FT /note="T -> I (in dbSNP:rs34065672)" FT /id="VAR_048513" FT VARIANT 920 FT /note="V -> G (in dbSNP:rs142841727)" FT /evidence="ECO:0000269|PubMed:18678517, FT ECO:0000269|PubMed:19863551" FT /id="VAR_062390" FT CONFLICT 4..10 FT /note="SPGRAYA -> TRDRVR (in Ref. 1; CAA81226)" FT /evidence="ECO:0000305" FT CONFLICT 593 FT /note="C -> V (in Ref. 1; CAA81226)" FT /evidence="ECO:0000305" FT CONFLICT 643 FT /note="G -> A (in Ref. 1; CAA81226)" FT /evidence="ECO:0000305" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:5ERD" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 76..82 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 123..132 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:7AGF" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 197..205 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 233..242 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 278..282 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 289..296 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 304..306 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 307..315 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 321..326 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 327..330 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 342..345 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 350..358 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 362..366 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 373..380 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 391..400 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 418..420 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 426..431 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:5ERD" FT TURN 442..444 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 446..451 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 464..477 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 480..490 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 498..500 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 502..507 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 513..518 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 525..528 FT /evidence="ECO:0007829|PDB:5ERD" FT HELIX 540..543 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 544..549 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 551..560 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 564..570 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 575..577 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 584..591 FT /evidence="ECO:0007829|PDB:5ERD" FT STRAND 595..598 FT /evidence="ECO:0007829|PDB:5ERD" SQ SEQUENCE 1118 AA; 122294 MW; E1481AA1686DB80A CRC64; MARSPGRAYA LLLLLICFNV GSGLHLQVLS TRNENKLLPK HPHLVRQKRA WITAPVALRE GEDLSKKNPI AKIHSDLAEE RGLKITYKYT GKGITEPPFG IFVFNKDTGE LNVTSILDRE ETPFFLLTGY ALDARGNNVE KPLELRIKVL DINDNEPVFT QDVFVGSVEE LSAAHTLVMK INATDADEPN TLNSKISYRI VSLEPAYPPV FYLNKDTGEI YTTSVTLDRE EHSSYTLTVE ARDGNGEVTD KPVKQAQVQI RILDVNDNIP VVENKVLEGM VEENQVNVEV TRIKVFDADE IGSDNWLANF TFASGNEGGY FHIETDAQTN EGIVTLIKEV DYEEMKNLDF SVIVANKAAF HKSIRSKYKP TPIPIKVKVK NVKEGIHFKS SVISIYVSES MDRSSKGQII GNFQAFDEDT GLPAHARYVK LEDRDNWISV DSVTSEIKLA KLPDFESRYV QNGTYTVKIV AISEDYPRKT ITGTVLINVE DINDNCPTLI EPVQTICHDA EYVNVTAEDL DGHPNSGPFS FSVIDKPPGM AEKWKIARQE STSVLLQQSE KKLGRSEIQF LISDNQGFSC PEKQVLTLTV CECLHGSGCR EAQHDSYVGL GPAAIALMIL AFLLLLLVPL LLLMCHCGKG AKGFTPIPGT IEMLHPWNNE GAPPEDKVVP SFLPVDQGGS LVGRNGVGGM AKEATMKGSS SASIVKGQHE MSEMDGRWEE HRSLLSGRAT QFTGATGAIM TTETTKTARA TGASRDMAGA QAAAVALNEE FLRNYFTDKA ASYTEEDENH TAKDCLLVYS QEETESLNAS IGCCSFIEGE LDDRFLDDLG LKFKTLAEVC LGQKIDINKE IEQRQKPATE TSMNTASHSL CEQTMVNSEN TYSSGSSFPV PKSLQEANAE KVTQEIVTER SVSSRQAQKV ATPLPDPMAS RNVIATETSY VTGSTMPPTT VILGPSQPQS LIVTERVYAP ASTLVDQPYA NEGTVVVTER VIQPHGGGSN PLEGTQHLQD VPYVMVRERE SFLAPSSGVQ PTLAMPNIAV GQNVTVTERV LAPASTLQSS YQIPTENSMT ARNTTVSGAG VPGPLPDFGL EESGHSNSTI TTSSTRVTKH STVQHSYS //