DSG1_PIG
ID DSG1_PIG Reviewed; 1045 AA.
AC Q3BDI7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Desmoglein-1;
DE AltName: Full=Desmosomal glycoprotein 1;
DE Short=DG1;
DE Short=DGI;
DE Flags: Precursor;
GN Name=DSG1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RX PubMed=16238811; DOI=10.1111/j.1365-3164.2005.00474.x;
RA Nishifuji K., Fudaba Y., Yamaguchi T., Iwasaki T., Sugai M., Amagai M.;
RT "Cloning of swine desmoglein 1 and its direct proteolysis by Staphylococcus
RT hyicus exfoliative toxins isolated from pigs with exudative epidermitis.";
RL Vet. Dermatol. 16:315-323(2005).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion (By similarity). {ECO:0000250}.
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 {ECO:0000250}.
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; AY677210; AAV84914.1; -; mRNA.
DR RefSeq; NP_001030612.1; NM_001035535.1.
DR AlphaFoldDB; Q3BDI7; -.
DR SMR; Q3BDI7; -.
DR STRING; 9823.ENSSSCP00000020931; -.
DR PaxDb; Q3BDI7; -.
DR PeptideAtlas; Q3BDI7; -.
DR PRIDE; Q3BDI7; -.
DR Ensembl; ENSSSCT00065068099; ENSSSCP00065029652; ENSSSCG00065049721.
DR GeneID; 641355; -.
DR KEGG; ssc:641355; -.
DR CTD; 1828; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q3BDI7; -.
DR OrthoDB; 250139at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IBA:GO_Central.
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; IBA:GO_Central.
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; 4.
DR SUPFAM; SSF49313; SSF49313; 4.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
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_0000289664"
FT CHAIN 50..1045
FT /note="Desmoglein-1"
FT /id="PRO_0000289665"
FT TOPO_DOM 50..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..1045
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..496
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 814..840
FT /note="Desmoglein repeat 1"
FT REPEAT 841..870
FT /note="Desmoglein repeat 2"
FT REPEAT 871..900
FT /note="Desmoglein repeat 3"
FT REPEAT 901..928
FT /note="Desmoglein repeat 4"
FT REPEAT 929..957
FT /note="Desmoglein repeat 5"
FT REGION 1019..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1045 AA; 113318 MW; E86391275E4C5209 CRC64;
MNWPFFRTAA VLFIFLVVLE VNSEFRIQVR DYNTKNGTIK WHSIRRQKRE WIKFAAACRE
GEDNSKRNPI AKIHSDCAAN QQVTYRISGV GIDQPPYGIF VINQKTGEIN ITSIVDREVT
PFFIIYCRAL NAQGQDLERP LELRVRVLDI NDNPPVFSMS TFLGQIEENS NANTLVMRLN
ATDADEPNNL NSKIAFKIIR QEPSDSPMFI INRYTGEIRT MNNFLDREQY SQYSLAVRGS
DRDGGADGMS AECECSIKIL DVNDNIPYME LPSNSLQIEE NSLNSNLLQI RVIDLDEEFS
ANWLAVIFFI SGNEGGWFDI EMNERTNVGT LKIVKPLDYE EVKNLQLSLG VRNKAEFHQS
IMSQYKLTAT AISVTVLNVI EGSVFRPGSK TYVVTSSMGQ NYKLGEFIAT DLDTGLPSTT
VRYVMGNNPT DLLAIDSKTG IITLRNKVTR EQYNLLGKKY QGTILSIDDA LQRTCTGTIN
IDLEGSGWED RQTDGAVTGG GTITSTNDFT PSYEYTTTNT EDVYSVTPTG NGVRVRHPLD
NVHFGPAGIG LLIMGFLVLG LVPFLLMYCD CGGAPGGGAG FEPVPECSDG AIHSWAVEGA
QPERADLTTI CVPQVPPDNA NIIECIDNSG VYTNEYCGRE MQELGGGERT TGFELIDGGK
ISGAPEICQE HSGTLRRNSM RECREGGLNM NFMESYFCQK AYAYADEDEG RPSNDCLLIY
DIEGEGSPAG SVGCCSFIGE DLDDSFLDTL GPKFKKLADI SLGKETEPYP DPDPSWPPQS
TDPICPPQGT EPIGSGHPPI SPHIGTTTVI SESTYPSGPG VHHPMPIPDP LSYGNVTMTE
SYTTSGILKP SVHVHDNRQA SNVVVTERVV GPISGANLHG MLEMPDLRDG SNVIVTERVI
APNSSLPTTL TIPDPRESSN VVVTERVIRP TSGIVGNLSM HPDISNTHNV IVTERVVSGS
GITGISGGSG MGSSGLVGST AGVGGDGLGL SSLGGGGLSS GIGGTATIGH LRGSSEHHFS
NTLGSASPTT TRSRITKYST VQYTK
