ID   DSG3_MOUSE              Reviewed;         993 AA.
AC   O35902; Q8CB02; Q8CE48;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-NOV-2023, entry version 151.
DE   RecName: Full=Desmoglein-3;
DE   AltName: Full=130 kDa pemphigus vulgaris antigen homolog;
DE   Flags: Precursor;
GN   Name=Dsg3;
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] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ;
RX   PubMed=7894164; DOI=10.1007/bf00292018;
RA   Ishikawa H., Silos S.A., Tamai K., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Uitto J.;
RT   "cDNA cloning and chromosomal assignment of the mouse gene for desmoglein 3
RT   (Dsg3), the pemphigus vulgaris antigen.";
RL   Mamm. Genome 5:803-804(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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).
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: Interacts with PKP2. {ECO:0000250|UniProtKB:P32926}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35902-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35902-2; Sequence=VSP_012905, VSP_012906;
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis.
CC       {ECO:0000269|PubMed:12787123}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 to 17 dpc.
CC       {ECO:0000269|PubMed:12787123}.
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; U86016; AAB65091.1; -; mRNA.
DR   EMBL; AK029018; BAC26246.1; -; mRNA.
DR   EMBL; AK037142; BAC29718.1; -; mRNA.
DR   CCDS; CCDS29083.1; -. [O35902-1]
DR   RefSeq; NP_085099.2; NM_030596.4.
DR   AlphaFoldDB; O35902; -.
DR   SMR; O35902; -.
DR   STRING; 10090.ENSMUSP00000064718; -.
DR   GlyCosmos; O35902; 4 sites, No reported glycans.
DR   GlyGen; O35902; 4 sites.
DR   iPTMnet; O35902; -.
DR   PhosphoSitePlus; O35902; -.
DR   MaxQB; O35902; -.
DR   PaxDb; 10090-ENSMUSP00000064718; -.
DR   PeptideAtlas; O35902; -.
DR   ProteomicsDB; 279812; -. [O35902-1]
DR   ProteomicsDB; 279813; -. [O35902-2]
DR   DNASU; 13512; -.
DR   GeneID; 13512; -.
DR   KEGG; mmu:13512; -.
DR   AGR; MGI:99499; -.
DR   CTD; 1830; -.
DR   MGI; MGI:99499; Dsg3.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; O35902; -.
DR   OrthoDB; 5314152at2759; -.
DR   PhylomeDB; O35902; -.
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   BioGRID-ORCS; 13512; 1 hit in 79 CRISPR screens.
DR   PRO; PR:O35902; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O35902; Protein.
DR   GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0005914; C:spot adherens junction; TAS:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:MGI.
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   CDD; cd11304; Cadherin_repeat; 4.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
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; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF3; DESMOGLEIN-3; 1.
DR   Pfam; PF00028; Cadherin; 4.
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.
PE   2: Evidence at transcript level;
KW   Alternative splicing; 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:0000305"
FT   PROPEP          24..49
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000003853"
FT   CHAIN           50..993
FT                   /note="Desmoglein-3"
FT                   /id="PRO_0000003854"
FT   TOPO_DOM        50..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          50..157
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          158..267
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          268..388
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          384..495
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REPEAT          905..930
FT                   /note="Desmoglein repeat 1"
FT   REPEAT          931..961
FT                   /note="Desmoglein repeat 2"
FT   REGION          845..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        546
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         876..929
FT                   /note="YQTLPGSLEVTQTGSKICHTLSGNQETSVMSTSGSVHPAVAIPDPLQLGNYL
FT                   LT -> QYLFLLLPSNEEAGARIHRAPSTNPRLLLLCLVHSEQRSVHSQYGSDAQGMNT
FT                   L (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012905"
FT   VAR_SEQ         930..993
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012906"
FT   CONFLICT        816
FT                   /note="G -> A (in Ref. 2; BAC26246/BAC29718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        941
FT                   /note="P -> H (in Ref. 2; BAC29718)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   993 AA;  107889 MW;  DB6CC526ABFB179A CRC64;
     MTCLFPRALG SLALLMVVLL VQGELHVKPG GQHREDGTAL QLAKRRYKRE WVKFAKPCRE
     REDNSRRNPI AKITSDFQKN QKITYRISGV GIDQPPFGIF VVDPNNGDIN ITAIVDREET
     PSFLITCRAL NALGQDVERP LILTVKILDV NDNPPIFSQT IFKGEIEENS ASNSLVMILN
     ATDADEPNHM NSKIAFKIVS QEPAGMSMFL ISRNTGEVRT LTSSLDREQI SSYHLVVSGA
     DNDGTGLSTQ CECSIKIKDV NDNFPVLRES QYSARIEENT LNAELLRFQV TDWDEEYTDN
     WLAVYFFTSG NEGNWFEIET DPRTNEGILK VVKALDYEQV QSMQFSIAVR NKAEFHQSVI
     SQYRVQSTPV TIQVIDVREG ISFRPPSKTF TVQRGVSTNK LVGYILGTYQ ATDEDTGKAA
     SSVRYVLGRN DGGLLVIDSK TAQIKFVKNI DRDSTFIVNK TISAEVLAID ENTGKTSTGT
     IYVEVPSFNE NCPSVVLEKK DICTSSPSVT LSVRTLDRGK YTGPYTVSLE EQPLKLPVMW
     TITTLNATSA LLQAQQQVSP GVYNVPVIVK DNQDGLCDTP ESLTLTVCQC DDRSMCRAPI
     PSREPNTYGE SSWRLGPAAI GLILLGLLML LLAPLLLLTC DCGSGPIGGA ATGGFIPVPD
     GSEGTIHQWG IEGAQPEDKE ITNICVPPVT TNGADFMESS EVCTNTYAGG TMVEGASGME
     MITKLGGATG ATAALGPCSL GYSGTMRTRH STGGTLKDYA APVNMTFLGS YFSQKSLAYA
     EEEDEREVND CLLIYDDEGE DAAPHSPTLS SCSIFGDDLD DNFLDSLGPK FKKLAEICLG
     IDDEAKQAKP GPKDSGSGAD TCARSMEVPQ SGSNRYQTLP GSLEVTQTGS KICHTLSGNQ
     ETSVMSTSGS VHPAVAIPDP LQLGNYLLTE TYSTSGSFAQ PTTVTFDPHV TQNVTVTERV
     ICPLPSASSS IVAPTELRGS YNMLYTKETC SHL
//