DSG2_MOUSE
ID DSG2_MOUSE Reviewed; 1122 AA.
AC O55111; A2RRJ0; Q8K069; Q8R517;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Desmoglein-2;
DE Flags: Precursor;
GN Name=Dsg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Zhuxiang N., Garrod D.R.;
RT "Desmosomal cadherins mediate homophilic cell adhesion.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1042-1122, AND DEVELOPMENTAL STAGE.
RX PubMed=9404003; DOI=10.1046/j.1432-0436.1997.6220083.x;
RA King I.A., Angst B.D., Hunt D.M., Kruger M., Arnemann J., Buxton R.S.;
RT "Hierarchical expression of desmosomal cadherins during stratified
RT epithelial morphogenesis in the mouse.";
RL Differentiation 62:83-96(1997).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12787123; DOI=10.1046/j.1523-1747.2003.12257.x;
RA Whittock N.V.;
RT "Genomic sequence analysis of the mouse desmoglein cluster reveals evidence
RT for six distinct genes: characterization of mouse DSG4, DSG5, and DSG6.";
RL J. Invest. Dermatol. 120:970-980(2003).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-467.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q14126};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14126}.
CC Cell junction, desmosome {ECO:0000250|UniProtKB:Q14126}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermis, heart, brain, spleen, lung,
CC liver skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:12787123}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 to 17 dpc. Expressed
CC uniformly in all 12.5 dpc epithelia, gradually becoming confined to the
CC basal cell layers during. {ECO:0000269|PubMed:12787123,
CC ECO:0000269|PubMed:9404003}.
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:0000250|UniProtKB:Q14126}.
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DR EMBL; AB072269; BAB86843.1; -; mRNA.
DR EMBL; BC034056; AAH34056.1; -; mRNA.
DR EMBL; BC131653; AAI31654.1; -; mRNA.
DR EMBL; BC131654; AAI31655.1; -; mRNA.
DR EMBL; AJ000328; CAA03995.1; -; mRNA.
DR CCDS; CCDS29084.1; -.
DR RefSeq; NP_031909.2; NM_007883.3.
DR AlphaFoldDB; O55111; -.
DR SMR; O55111; -.
DR STRING; 10090.ENSMUSP00000057096; -.
DR GlyGen; O55111; 4 sites.
DR iPTMnet; O55111; -.
DR PhosphoSitePlus; O55111; -.
DR SwissPalm; O55111; -.
DR CPTAC; non-CPTAC-3572; -.
DR jPOST; O55111; -.
DR MaxQB; O55111; -.
DR PaxDb; O55111; -.
DR PeptideAtlas; O55111; -.
DR PRIDE; O55111; -.
DR ProteomicsDB; 279811; -.
DR Antibodypedia; 1349; 747 antibodies from 41 providers.
DR DNASU; 13511; -.
DR Ensembl; ENSMUST00000059787; ENSMUSP00000057096; ENSMUSG00000044393.
DR GeneID; 13511; -.
DR KEGG; mmu:13511; -.
DR UCSC; uc008ees.2; mouse.
DR CTD; 1829; -.
DR MGI; MGI:1196466; Dsg2.
DR VEuPathDB; HostDB:ENSMUSG00000044393; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_1_1; -.
DR InParanoid; O55111; -.
DR OMA; RDTANWI; -.
DR OrthoDB; 250139at2759; -.
DR PhylomeDB; O55111; -.
DR TreeFam; TF331809; -.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 13511; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dsg2; mouse.
DR PRO; PR:O55111; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O55111; protein.
DR Bgee; ENSMUSG00000044393; Expressed in left colon and 240 other tissues.
DR ExpressionAtlas; O55111; baseline and differential.
DR Genevisible; O55111; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0002934; P:desmosome organization; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0003165; P:Purkinje myocyte development; ISO:MGI.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
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 Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..54
FT /evidence="ECO:0000255"
FT /id="PRO_0000003847"
FT CHAIN 55..1122
FT /note="Desmoglein-2"
FT /id="PRO_0000003848"
FT TOPO_DOM 55..618
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..1122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..164
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 165..277
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 278..398
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 397..504
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 885..916
FT /note="Desmoglein repeat 1"
FT REPEAT 917..945
FT /note="Desmoglein repeat 2"
FT REPEAT 946..971
FT /note="Desmoglein repeat 3"
FT REPEAT 972..995
FT /note="Desmoglein repeat 4"
FT REPEAT 996..1024
FT /note="Desmoglein repeat 5"
FT REPEAT 1025..1055
FT /note="Desmoglein repeat 6"
FT REGION 913..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14126"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 304
FT /note="D -> Y (in Ref. 1; BAB86843)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="I -> L (in Ref. 2; AAH34056)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="E -> D (in Ref. 2; AAH34056)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="V -> I (in Ref. 2; AAH34056)"
FT /evidence="ECO:0000305"
FT CONFLICT 863
FT /note="R -> T (in Ref. 1; BAB86843)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="H -> R (in Ref. 1; BAB86843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1122 AA; 122385 MW; 9EB9CD402632437A CRC64;
MARSPGDRCA LLLLVQLLAV VCLDFGNGLH LEVFSPRNEG KPFPKHTHLV RQKRAWITAP
VALREGEDLS RKNPIAKIHS DLAEEKGIKI TYKYTGKGIT EPPFGIFVFD RNTGELNITS
ILDREETPYF LLTGYALDSR GNNLEKPLEL RIKVLDINDN EPVFTQEVFV GSIEELSAAH
TLVMKITATD ADDPETLNAK VSYRIVSQEP ANSHMFYLNK DTGEIYTTSF TLDREEHSSY
SLTVEARDGN GQITDKPVQQ AQVQIRILDV NDNIPVVENK MYEGTVEENQ VNVEVMRIKV
TDADEVGSDN WLANFTFASG NEGGYFHIET DTQTNEGIVT LVKEVDYEEM KKLDLSIIVT
NKAAFHKSIL SKYKATPIPI TVKVKNVVEG IHFKSSVVSF RASEAMDRSS LSRSIGNFQV
FDEDTGQAAK VTYVKVQDTD NWVSVDSVTS EIKLVKIPDF ESRYVQNGTY TAKVVAISKE
HPQKTITGTI VITVEDVNDN CPVLVDSVRS VCEDEPYVNV TAEDLDGAQN SAPFSFSIID
QPPGTAQKWK ITHQESTSVL LQQSERKRGR SEIPFLISDS QGFSCPERQV LQLTVCECLK
GGGCVAAQYD NYVGLGPAAI ALMILALLLL LLVPLLLLIC HCGGGAKGFT PIPGTIEMLH
PWNNEGAPPE DKVVPSLLVA DHAESSAVRG GVGGAMLKEG MMKGSSSASV TKGQHELSEV
DGRWEEHRSL LTAGATHHVR TAGTIAANEA VRTRATGSSR DMSGARGAVA VNEEFLRSYF
TEKAASYNGE DDLHMAKDCL LVYSQEDTAS LRGSVGCCSF IEGELDDLFL DDLGLKFKTL
AEVCLGRKID LDVDIEQRQK PVREASVSAA SGSHYEQAVT SSESAYSSNT GFPAPKPLHE
VHTEKVTQEI VTESSVSSRQ SQKVVPPPDP VASGNIIVTE TSYAKGSAVP PSTVLLAPRQ
PQSLIVTERV YAPTSTLVDQ HYANEEKVLV TERVIQPNGG IPKPLEVTQH LKDAQYVMVR
ERESILAPSS GVQPTLAMPS VAAGGQNVTV TERILTPAST LQSSYQIPSE TSITARNTVL
SSVGSIGPLP NLDLEESDRP NSTITTSSTR VTKHSTMQHS YS
