DSG3_MOUSE
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 25-MAY-2022, entry version 145.
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 -!- 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 GlyGen; O35902; 4 sites.
DR iPTMnet; O35902; -.
DR PhosphoSitePlus; O35902; -.
DR MaxQB; O35902; -.
DR PaxDb; O35902; -.
DR PeptideAtlas; O35902; -.
DR PRIDE; O35902; -.
DR ProteomicsDB; 279812; -. [O35902-1]
DR ProteomicsDB; 279813; -. [O35902-2]
DR DNASU; 13512; -.
DR GeneID; 13512; -.
DR KEGG; mmu:13512; -.
DR CTD; 1830; -.
DR MGI; MGI:99499; Dsg3.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; O35902; -.
DR OrthoDB; 250139at2759; -.
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 74 CRISPR screens.
DR PRO; PR:O35902; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35902; protein.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of 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 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; 4.
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 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
