DSG2_HUMAN
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 03-AUG-2022, entry version 203.
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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31402609};
CC Single-pass type I membrane protein. Cell junction, desmosome.
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:0000250}.
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="http://atlasgeneticsoncology.org/Genes/DSG2ID40367ch18q12.html";
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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 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 AlphaFoldDB; Q14126; -.
DR SASBDB; Q14126; -.
DR SMR; Q14126; -.
DR BioGRID; 108163; 197.
DR DIP; DIP-46250N; -.
DR IntAct; Q14126; 69.
DR MINT; Q14126; -.
DR STRING; 9606.ENSP00000261590; -.
DR GlyConnect; 1172; 41 N-Linked glycans (5 sites).
DR GlyGen; Q14126; 11 sites, 40 N-linked glycans (5 sites), 1 O-linked glycan (2 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; Q14126; -.
DR PeptideAtlas; Q14126; -.
DR PRIDE; Q14126; -.
DR ProteomicsDB; 59829; -.
DR Antibodypedia; 1349; 747 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 CTD; 1829; -.
DR DisGeNET; 1829; -.
DR GeneCards; DSG2; -.
DR GeneReviews; DSG2; -.
DR HGNC; HGNC:3049; DSG2.
DR HPA; ENSG00000046604; Tissue enhanced (intestine, parathyroid gland).
DR MalaCards; DSG2; -.
DR MIM; 125671; gene.
DR MIM; 610193; phenotype.
DR MIM; 612877; phenotype.
DR neXtProt; NX_Q14126; -.
DR OpenTargets; ENSG00000046604; -.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
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; RDNWISV; -.
DR OrthoDB; 250139at2759; -.
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; 16 hits in 1080 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 160 other tissues.
DR ExpressionAtlas; Q14126; baseline and differential.
DR Genevisible; Q14126; HS.
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; IBA:GO_Central.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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: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 Gene3D; 4.10.900.10; -; 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; IPR009123; Desmoglein.
DR InterPro; IPR009122; Desmosomal_cadherin.
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; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 4.
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 (associated with CMD1BB and ARVD10 although
FT it may not be sufficient by itself to result in
FT cardiomyopathy; 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
