DSG1_BOVIN
ID DSG1_BOVIN Reviewed; 1043 AA.
AC Q03763; Q9TS15;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Desmoglein-1;
DE AltName: Full=Desmosomal glycoprotein 1;
DE Short=DG1;
DE Short=DGI;
DE AltName: Full=Pemphigus foliaceus antigen;
DE Flags: Precursor;
GN Name=DSG1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muzzle epithelium;
RA Koch P.J., Goldschmidt M.D., Zimbelmann R., Franke W.W.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=8294446; DOI=10.1016/s0021-9258(17)42119-3;
RA Puttagunta S., Mathur M., Cowin P.;
RT "Structure of DSG1, the bovine desmosomal cadherin gene encoding the
RT pemphigus foliaceus antigen. Evidence of polymorphism.";
RL J. Biol. Chem. 269:1949-1955(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-1043.
RC TISSUE=Muzzle epithelium;
RX PubMed=1706270;
RA Koch P.J., Walsh M.J., Schmelz M., Goldschmidt M.D., Zimbelmann R.,
RA Franke W.W.;
RT "Identification of desmoglein, a constitutive desmosomal glycoprotein, as a
RT member of the cadherin family of cell adhesion molecules.";
RL Eur. J. Cell Biol. 53:1-12(1990).
RN [4]
RP PROTEIN SEQUENCE OF 101-123, AND SEQUENCE REVISION.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-493.
RX PubMed=1702628; DOI=10.1016/s0006-291x(05)80917-9;
RA Goodwin L., Hill J.E., Raynor K., Raszi L., Manabe M., Cowin P.;
RT "Desmoglein shows extensive homology to the cadherin family of cell
RT adhesion molecules.";
RL Biochem. Biophys. Res. Commun. 173:1224-1230(1990).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome.
CC -!- TISSUE SPECIFICITY: Epidermis, muzzle, tongue and esophagus.
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}.
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DR EMBL; X58466; CAA41380.1; -; mRNA.
DR EMBL; X57784; CAA40930.1; -; mRNA.
DR EMBL; M58165; AAA62709.1; -; mRNA.
DR PIR; S14603; IJBOG1.
DR RefSeq; NP_776470.1; NM_174045.1.
DR AlphaFoldDB; Q03763; -.
DR SMR; Q03763; -.
DR STRING; 9913.ENSBTAP00000018382; -.
DR iPTMnet; Q03763; -.
DR PaxDb; Q03763; -.
DR PRIDE; Q03763; -.
DR GeneID; 281131; -.
DR KEGG; bta:281131; -.
DR CTD; 1828; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q03763; -.
DR OrthoDB; 250139at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009123; Desmoglein.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR Pfam; PF00028; Cadherin; 3.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR PRINTS; PR01819; DESMOGLEIN.
DR SMART; SM00112; CA; 3.
DR SUPFAM; SSF49313; SSF49313; 4.
DR PROSITE; PS00232; CADHERIN_1; 2.
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; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..49
FT /evidence="ECO:0000255"
FT /id="PRO_0000003833"
FT CHAIN 50..1043
FT /note="Desmoglein-1"
FT /id="PRO_0000003834"
FT TOPO_DOM 50..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..1043
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..498
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 819..845
FT /note="Desmoglein repeat 1"
FT REPEAT 846..875
FT /note="Desmoglein repeat 2"
FT REPEAT 876..905
FT /note="Desmoglein repeat 3"
FT REPEAT 906..933
FT /note="Desmoglein repeat 4"
FT REPEAT 934..962
FT /note="Desmoglein repeat 5"
FT REGION 770..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1935985"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 124
FT /note="I -> V (in Ref. 2; no nucleotide entry and 5;
FT AAA62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="M -> N (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="M -> N (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1043 AA; 112243 MW; ADE46133F8B77C11 CRC64;
MNWPFFRAAV VLFIFLVVLE VNSDFRIQVR DYNTKNGTIK WHSLRRQKRE WIKFAAACRE
GEDNSKRNPI AKIHSDCAAN QQVTYRISGV GIDQPPYGIF VINQKTGEIN ITSIVDREVT
PFFIIYCRAL NSLGQDLEKP LELRVRVLDI NDNPPVFSMS TFVGEIEENS NANTLVMVLN
ATDADEPNNL NSKIAFKIIR QEPSDSPMFI INRYTGEIRT MNNFLDREQY GQYSLAVRGS
DRDGGADGMS AECECNIKIL DVNDNIPYME LPTQSISIEE NSLNSNLLQI RVIDLDEEFS
ANWMAVIFFI SGNEGNWFEI EMNERTNVGT LKVVKPLDFE AMNNLQLSLG VRNKAEFHQS
IMSQYKLTAT AISVTVLNVV EGSVFRPGSK TFVVNSNMGQ NYKIGEYVAW DLDANRPSTT
VRYVMGRNPT DLLAIDSKTA IITLRNKVTM EQYKILGGKY QGTILSIDDA LQRTCTGTIV
INLENGGWKT ERPNVNGSTT SAYGLTSGGV TTNGYTTGGG VGTVTFAVGT NGYGVGTGVY
QPLRDNVHFG PAGIGLLIMG FLVLGLVPFL LMCCDCGGAP GGGAAFEPVP ECSDGAIHSW
AVEGAQADPG VLANSAVPCI PVTNANVIEY VDNSGVYTNE YGAREMQDLG GGERTTGFEL
TDGVKMSGGP EICQEYPGTL RRNSMRECRE GGLNMNFMES YFCQKAYAYA DEDEGRPSND
CLLIYDIEGA GSPAGSVGCC SFIGEDLDDS FLDTLGPKFK KLADISLGKD VEPFPDSDPS
WPPKSTEPVC PPQGTEPTGG GHPPISPRFG TTTVISENTY PSGPGVQHPT PIPDPLGYGN
VTVTESYTSS GTLKPSVHIH DNRHASNVVV TERVVGPISG ADLQGMLEMP DLRDGSNVIV
TERVIAPSSS LPTTLTIPDP RQSSNVVVTE RVIQPTSGIV GNLSMHPELS NTHNVIVTER
VVSGSGITGS SSLLGSAGGG SGGGIGLGSL GGGGGLSSSL GGAATIGHLR GSAEHHFSNT
LGSASPTTTR SRITKYSTVQ YTK
