DSG3_CANLF
ID DSG3_CANLF Reviewed; 993 AA.
AC Q7YRU7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Desmoglein-3;
DE Flags: Precursor;
GN Name=DSG3;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oral mucosa;
RX PubMed=14507443; DOI=10.1016/s0923-1811(03)00095-1;
RA Nishifuji K., Amagai M., Ota T., Nishikawa T., Iwasaki T.;
RT "Cloning of canine desmoglein 3 and immunoreactivity of serum antibodies in
RT human and canine pemphigus vulgaris with its extracellular domains.";
RL J. Dermatol. Sci. 32:181-191(2003).
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF394784; AAP80592.1; -; mRNA.
DR RefSeq; NP_001002983.1; NM_001002983.1.
DR AlphaFoldDB; Q7YRU7; -.
DR SMR; Q7YRU7; -.
DR STRING; 9612.ENSCAFP00000026686; -.
DR PaxDb; Q7YRU7; -.
DR Ensembl; ENSCAFT00030002158; ENSCAFP00030001907; ENSCAFG00030001202.
DR GeneID; 403470; -.
DR KEGG; cfa:403470; -.
DR CTD; 1830; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; Q7YRU7; -.
DR OMA; KYVMGRN; -.
DR OrthoDB; 250139at2759; -.
DR TreeFam; TF331809; -.
DR Reactome; R-CFA-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-CFA-6805567; Keratinization.
DR Reactome; R-CFA-6809371; Formation of the cornified envelope.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000018051; Expressed in keratinocyte and 43 other tissues.
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: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; 4.
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..48
FT /evidence="ECO:0000255"
FT /id="PRO_0000003849"
FT CHAIN 49..993
FT /note="Desmoglein-3"
FT /id="PRO_0000003850"
FT TOPO_DOM 49..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..993
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..156
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 157..266
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 267..386
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..494
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 903..929
FT /note="Desmoglein repeat 1"
FT REPEAT 930..960
FT /note="Desmoglein repeat 2"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 993 AA; 107551 MW; B1EE9C6DE9666D5D CRC64;
MTWLLFRTSG ALAILMVLIL VHGELRIETK GQHGEDETAI QGRRRYKREW VKFAKPCRER
EDNSRRNPIA KITSDFQATQ KITYRISGMG IDQPPFGIFV VDKNTGEINI TAIVDREETP
SFQITCHALN VLGQDVEKPL ILTVKILDVN DNAPVFSQSI FMGEIEENSA SNSLVMILNA
TDADEPNHLN SKIAFKIVSQ EPAGTPMFLL SRHTGEVRTL TNSLDREQVS SYRLVVSGAD
KDGEGLSTQC ECSIKVKDVN DNFPMFKESQ YSAHIKENTL TSELLRFQVI DWDEEFTDNW
LAVYFFTSGN EGNWFEIQTD PRTNEGILKV VKALDYEQLQ SVQFSIAVKN KAEFHQSVIS
QYQVKSTPVT IQVVNVKEGI AFHPASKTFT VRKGISSKKL VNYVLGTYQA IDEDTNKAAS
YVKYVMGRND GGLLFIDPKT AQIKFVRNID RDSTFIVNKT ITAEVLAIDE NTGKTATGTI
YVEVPGFNEN CPTVVLEKKA ICSSLRSVVV SARVPDNKYT GPYTFSLEEQ SLKLPVVWSI
TTLNATSALL NAQQQLSPGE YTISLTVTDS QDRQCETPES LTLEVCQCDN RDICRSSNGN
KDYERLDGKR PSGRLGSAAI GLLLLGLLLL LLAPLLLLTC DYGVGPIGGV TGGFIPVPDG
SEGTIHQWGI EGAQPEDKEI TNICVPPITT SGADFMENSE VCTNTYAGGT VVEGASGMEL
TTKLGAATGS GAAAGFGATA GFGAATGLGI GSAGQSGTMR TRHSTGGTNK DYGEGAISMN
FLDSYFSQKA FACAEEDDVQ EANDCLLIYD NEGMGAPSSP VGSLGCCSFI ADELDDSFLD
SLGPKFKKLA EISLGIDDEA KQSQPLSKAS LSGMESCGYS LEVQQPESVR GQTLLGSQGA
SALSASSSVL QSATSIPNPV QHGSYMVTET YSASGSLVQP TTTVLEPLLT QNVTVTERVI
CPISNVSGNL QTPMELRGSR NMICTEDPCS RLI
