ID   DSG1_HUMAN              Reviewed;        1049 AA.
AC   Q02413; B7Z845;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   27-MAR-2024, entry version 220.
DE   RecName: Full=Desmoglein-1;
DE   AltName: Full=Cadherin family member 4;
DE   AltName: Full=Desmosomal glycoprotein 1;
DE            Short=DG1;
DE            Short=DGI;
DE   AltName: Full=Pemphigus foliaceus antigen;
DE   Flags: Precursor;
GN   Name=DSG1; Synonyms=CDHF4;
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] (ISOFORM 1), AND VARIANT VAL-11.
RC   TISSUE=Keratinocyte;
RX   PubMed=1711210; DOI=10.1073/pnas.88.11.4796;
RA   Wheeler G.N., Parker A.E., Thomas C.L., Ataliotis P., Poynter D.,
RA   Arnemann J., Rutman A.J., Pidsley S.C., Watt F.M., Rees D.A., Buxton R.S.,
RA   Magee A.I.;
RT   "Desmosomal glycoprotein DGI, a component of intercellular desmosome
RT   junctions, is related to the cadherin family of cell adhesion molecules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4796-4800(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-11.
RC   TISSUE=Foreskin;
RX   PubMed=1770008; DOI=10.1242/jcs.99.4.809;
RA   Nilles L.A., Parry D.A., Powers E.E., Angst B.D., Wagner R.M., Green K.J.;
RT   "Structural analysis and expression of human desmoglein: a cadherin-like
RT   component of the desmosome.";
RL   J. Cell Sci. 99:809-821(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [5]
RP   INVOLVEMENT IN PPKS1.
RX   PubMed=10332028; DOI=10.1093/hmg/8.6.971;
RA   Rickman L., Simrak D., Stevens H.P., Hunt D.M., King I.A., Bryant S.P.,
RA   Eady R.A.J., Leigh I.M., Arnemann J., Magee A.I., Kelsell D.P.,
RA   Buxton R.S.;
RT   "N-terminal deletion in a desmosomal cadherin causes the autosomal dominant
RT   skin disease striate palmoplantar keratoderma.";
RL   Hum. Mol. Genet. 8:971-976(1999).
RN   [6]
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   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [8]
RP   INTERACTION WITH JUP/PLAKOGLOBIN.
RX   PubMed=19759396; DOI=10.1074/jbc.m109.047928;
RA   Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
RT   "Interactions of plakoglobin and beta-catenin with desmosomal cadherins:
RT   basis of selective exclusion of alpha- and beta-catenin from desmosomes.";
RL   J. Biol. Chem. 284:31776-31788(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP   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   [10]
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   [11]
RP   INVOLVEMENT IN EPKHE.
RX   PubMed=23974871; DOI=10.1038/ng.2739;
RA   Samuelov L., Sarig O., Harmon R.M., Rapaport D., Ishida-Yamamoto A.,
RA   Isakov O., Koetsier J.L., Gat A., Goldberg I., Bergman R., Spiegel R.,
RA   Eytan O., Geller S., Peleg S., Shomron N., Goh C.S., Wilson N.J.,
RA   Smith F.J., Pohler E., Simpson M.A., McLean W.H., Irvine A.D., Horowitz M.,
RA   McGrath J.A., Green K.J., Sprecher E.;
RT   "Desmoglein 1 deficiency results in severe dermatitis, multiple allergies
RT   and metabolic wasting.";
RL   Nat. Genet. 45:1244-1248(2013).
RN   [12]
RP   INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SDRD (MICROBIAL INFECTION).
RX   PubMed=26924733; DOI=10.1038/srep22134;
RA   Askarian F., Ajayi C., Hanssen A.M., van Sorge N.M., Pettersen I.,
RA   Diep D.B., Sollid J.U., Johannessen M.;
RT   "The interaction between Staphylococcus aureus SdrD and desmoglein 1 is
RT   important for adhesion to host cells.";
RL   Sci. Rep. 6:22134-22134(2016).
RN   [13]
RP   SUBCELLULAR LOCATION, AND INDUCTION BY P.GINGIVALIS INFECTION.
RX   PubMed=34368962; DOI=10.1111/jre.12918;
RA   Yu N., Zhang J., Phillips S.T., Offenbacher S., Zhang S.;
RT   "Impaired function of epithelial plakophilin-2 is associated with
RT   periodontal disease.";
RL   J. Periodont. Res. 56:1046-1057(2021).
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: Binds to JUP/plakoglobin (PubMed:19759396). Interacts with
CC       PKP2 (PubMed:11790773). {ECO:0000269|PubMed:11790773,
CC       ECO:0000269|PubMed:19759396}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       protein SdrD; this interaction increases S.aureus adherence to
CC       keratinocytes. {ECO:0000269|PubMed:26924733}.
CC   -!- INTERACTION:
CC       Q02413; Q08554: DSC1; NbExp=2; IntAct=EBI-1045757, EBI-2371346;
CC       Q02413; P15924: DSP; NbExp=2; IntAct=EBI-1045757, EBI-355041;
CC       Q02413; P14923: JUP; NbExp=2; IntAct=EBI-1045757, EBI-702484;
CC       Q02413; Q13835: PKP1; NbExp=2; IntAct=EBI-1045757, EBI-2513407;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TSF1};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q7TSF1}.
CC       Cell junction, desmosome {ECO:0000269|PubMed:34368962}. Cytoplasm
CC       {ECO:0000269|PubMed:34368962}. Nucleus {ECO:0000269|PubMed:34368962}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q02413-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q02413-2; Sequence=VSP_055930;
CC   -!- TISSUE SPECIFICITY: Epidermis, tongue, tonsil and esophagus.
CC   -!- INDUCTION: Protein abundance is reduced via proteasomal degradation in
CC       response to P.gingivalis infection of gingival epithelial cells.
CC       {ECO:0000269|PubMed:34368962}.
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   -!- DISEASE: Palmoplantar keratoderma 1, striate, focal, or diffuse (PPKS1)
CC       [MIM:148700]: A dermatological disorder characterized by thickening of
CC       the skin on the palms and soles, and longitudinal hyperkeratotic
CC       lesions on the palms, running the length of each finger.
CC       {ECO:0000269|PubMed:10332028}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Erythroderma, congenital, with palmoplantar keratoderma,
CC       hypotrichosis, and hyper IgE (EPKHE) [MIM:615508]: A syndrome
CC       characterized by severe dermatitis, multiple allergies and metabolic
CC       wasting. Clinical features include erythroderma, yellowish papules and
CC       plaques arranged at the periphery of the palms, along the fingers and
CC       over weight-bearing areas of the feet, skin erosions and scaling, and
CC       hypotrichosis. Additionally, patients manifest severe food allergies,
CC       elevated immunoglobulin E (IgE) levels and recurrent infections with
CC       marked metabolic wasting. {ECO:0000269|PubMed:23974871}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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DR   EMBL; X56654; CAA39976.1; -; mRNA.
DR   EMBL; AF097935; AAC83817.1; -; mRNA.
DR   EMBL; AK302888; BAH13831.1; -; mRNA.
DR   EMBL; AC009717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS11896.1; -. [Q02413-1]
DR   PIR; S16906; IJHUG1.
DR   RefSeq; NP_001933.2; NM_001942.3. [Q02413-1]
DR   AlphaFoldDB; Q02413; -.
DR   SMR; Q02413; -.
DR   BioGRID; 108162; 197.
DR   ELM; Q02413; -.
DR   IntAct; Q02413; 64.
DR   MINT; Q02413; -.
DR   STRING; 9606.ENSP00000257192; -.
DR   GlyCosmos; Q02413; 3 sites, No reported glycans.
DR   GlyGen; Q02413; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q02413; -.
DR   PhosphoSitePlus; Q02413; -.
DR   SwissPalm; Q02413; -.
DR   BioMuta; DSG1; -.
DR   DMDM; 292495005; -.
DR   EPD; Q02413; -.
DR   jPOST; Q02413; -.
DR   MassIVE; Q02413; -.
DR   MaxQB; Q02413; -.
DR   PaxDb; 9606-ENSP00000257192; -.
DR   PeptideAtlas; Q02413; -.
DR   PRIDE; Q02413; -.
DR   ProteomicsDB; 58089; -. [Q02413-1]
DR   ABCD; Q02413; 45 sequenced antibodies.
DR   Antibodypedia; 3998; 878 antibodies from 42 providers.
DR   DNASU; 1828; -.
DR   Ensembl; ENST00000257192.5; ENSP00000257192.4; ENSG00000134760.6. [Q02413-1]
DR   GeneID; 1828; -.
DR   KEGG; hsa:1828; -.
DR   MANE-Select; ENST00000257192.5; ENSP00000257192.4; NM_001942.4; NP_001933.2.
DR   UCSC; uc002kwp.4; human. [Q02413-1]
DR   AGR; HGNC:3048; -.
DR   CTD; 1828; -.
DR   DisGeNET; 1828; -.
DR   GeneCards; DSG1; -.
DR   HGNC; HGNC:3048; DSG1.
DR   HPA; ENSG00000134760; Tissue enriched (skin).
DR   MalaCards; DSG1; -.
DR   MIM; 125670; gene.
DR   MIM; 148700; phenotype.
DR   MIM; 615508; phenotype.
DR   neXtProt; NX_Q02413; -.
DR   OpenTargets; ENSG00000134760; -.
DR   Orphanet; 369999; Diffuse palmoplantar keratoderma with painful fissures.
DR   Orphanet; 370002; Focal palmoplantar keratoderma with joint keratoses.
DR   Orphanet; 369992; Severe dermatitis-multiple allergies-metabolic wasting syndrome.
DR   Orphanet; 50942; Striate palmoplantar keratoderma.
DR   PharmGKB; PA27501; -.
DR   VEuPathDB; HostDB:ENSG00000134760; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT01030000234624; -.
DR   HOGENOM; CLU_005284_0_0_1; -.
DR   InParanoid; Q02413; -.
DR   OMA; LRKVCMH; -.
DR   OrthoDB; 5314152at2759; -.
DR   PhylomeDB; Q02413; -.
DR   TreeFam; TF331809; -.
DR   PathwayCommons; Q02413; -.
DR   Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
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   SignaLink; Q02413; -.
DR   BioGRID-ORCS; 1828; 7 hits in 1150 CRISPR screens.
DR   ChiTaRS; DSG1; human.
DR   GeneWiki; Desmoglein_1; -.
DR   GenomeRNAi; 1828; -.
DR   Pharos; Q02413; Tbio.
DR   PRO; PR:Q02413; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; Q02413; Protein.
DR   Bgee; ENSG00000134760; Expressed in upper arm skin and 101 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030057; C:desmosome; IDA:UniProtKB.
DR   GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR   GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; NAS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR   GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR   CDD; cd11304; Cadherin_repeat; 4.
DR   DisProt; DP01476; -.
DR   Gene3D; 2.60.40.60; Cadherins; 4.
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; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF9; DESMOGLEIN-1; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 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; 4.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 4.
DR   Genevisible; Q02413; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cleavage on pair of basic residues; Cytoplasm; Glycoprotein; Hypotrichosis;
KW   Membrane; Metal-binding; Nucleus; Palmoplantar keratoderma; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..49
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003837"
FT   CHAIN           50..1049
FT                   /note="Desmoglein-1"
FT                   /id="PRO_0000003838"
FT   TOPO_DOM        50..548
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        570..1049
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          50..158
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          159..270
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          271..385
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          386..497
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REPEAT          813..839
FT                   /note="Desmoglein repeat 1"
FT   REPEAT          840..869
FT                   /note="Desmoglein repeat 2"
FT   REPEAT          870..899
FT                   /note="Desmoglein repeat 3"
FT   REPEAT          900..927
FT                   /note="Desmoglein repeat 4"
FT   REPEAT          928..956
FT                   /note="Desmoglein repeat 5"
FT   REGION          485..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..641
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055930"
FT   VARIANT         11
FT                   /note="M -> V (in dbSNP:rs1426310)"
FT                   /evidence="ECO:0000269|PubMed:1711210,
FT                   ECO:0000269|PubMed:1770008"
FT                   /id="VAR_060248"
FT   VARIANT         395
FT                   /note="T -> S (in dbSNP:rs16961655)"
FT                   /id="VAR_055573"
FT   VARIANT         493
FT                   /note="N -> T (in dbSNP:rs8091003)"
FT                   /id="VAR_024385"
FT   VARIANT         498
FT                   /note="T -> N (in dbSNP:rs8091117)"
FT                   /id="VAR_024386"
FT   VARIANT         528
FT                   /note="Y -> S (in dbSNP:rs16961689)"
FT                   /id="VAR_055574"
FT   VARIANT         538
FT                   /note="D -> N (in dbSNP:rs34302455)"
FT                   /id="VAR_055575"
FT   VARIANT         665
FT                   /note="M -> I (in dbSNP:rs35360042)"
FT                   /id="VAR_055576"
FT   VARIANT         821
FT                   /note="L -> Q (in dbSNP:rs16961692)"
FT                   /id="VAR_055577"
FT   VARIANT         828
FT                   /note="D -> N (in dbSNP:rs3752094)"
FT                   /id="VAR_060249"
FT   VARIANT         841
FT                   /note="Y -> F (in dbSNP:rs3752095)"
FT                   /id="VAR_020364"
SQ   SEQUENCE   1049 AA;  113748 MW;  FEA471244B9D67AE CRC64;
     MDWSFFRVVA MLFIFLVVVE VNSEFRIQVR DYNTKNGTIK WHSIRRQKRE WIKFAAACRE
     GEDNSKRNPI AKIHSDCAAN QQVTYRISGV GIDQPPYGIF VINQKTGEIN ITSIVDREVT
     PFFIIYCRAL NSMGQDLERP LELRVRVLDI NDNPPVFSMA TFAGQIEENS NANTLVMILN
     ATDADEPNNL NSKIAFKIIR QEPSDSPMFI INRNTGEIRT MNNFLDREQY GQYALAVRGS
     DRDGGADGMS AECECNIKIL DVNDNIPYME QSSYTIEIQE NTLNSNLLEI RVIDLDEEFS
     ANWMAVIFFI SGNEGNWFEI EMNERTNVGI LKVVKPLDYE AMQSLQLSIG VRNKAEFHHS
     IMSQYKLKAS AISVTVLNVI EGPVFRPGSK TYVVTGNMGS NDKVGDFVAT DLDTGRPSTT
     VRYVMGNNPA DLLAVDSRTG KLTLKNKVTK EQYNMLGGKY QGTILSIDDN LQRTCTGTIN
     INIQSFGNDD RTNTEPNTKI TTNTGRQEST SSTNYDTSTT STDSSQVYSS EPGNGAKDLL
     SDNVHFGPAG IGLLIMGFLV LGLVPFLMIC CDCGGAPRSA AGFEPVPECS DGAIHSWAVE
     GPQPEPRDIT TVIPQIPPDN ANIIECIDNS GVYTNEYGGR EMQDLGGGER MTGFELTEGV
     KTSGMPEICQ EYSGTLRRNS MRECREGGLN MNFMESYFCQ KAYAYADEDE GRPSNDCLLI
     YDIEGVGSPA GSVGCCSFIG EDLDDSFLDT LGPKFKKLAD ISLGKESYPD LDPSWPPQST
     EPVCLPQETE PVVSGHPPIS PHFGTTTVIS ESTYPSGPGV LHPKPILDPL GYGNVTVTES
     YTTSDTLKPS VHVHDNRPAS NVVVTERVVG PISGADLHGM LEMPDLRDGS NVIVTERVIA
     PSSSLPTSLT IHHPRESSNV VVTERVIQPT SGMIGSLSMH PELANAHNVI VTERVVSGAG
     VTGISGTTGI SGGIGSSGLV GTSMGAGSGA LSGAGISGGG IGLSSLGGTA SIGHMRSSSD
     HHFNQTIGSA SPSTARSRIT KYSTVQYSK
//