ID   DSG1A_MOUSE             Reviewed;        1057 AA.
AC   Q61495; A8WFQ4; Q8CE03;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Desmoglein-1-alpha;
DE            Short=Desmoglein-1;
DE            Short=Dsg1-alpha;
DE   AltName: Full=DG1;
DE   AltName: Full=DGI;
DE   AltName: Full=Desmosomal glycoprotein I;
DE   Flags: Precursor;
GN   Name=Dsg1a; Synonyms=Dsg1;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Keratinocyte;
RX   PubMed=11994138; DOI=10.1034/j.1600-0625.2002.110203.x;
RA   Mahoney M.G., Simpson A., Aho S., Uitto J., Pulkkinen L.;
RT   "Interspecies conservation and differential expression of mouse desmoglein
RT   gene family.";
RL   Exp. Dermatol. 11:115-125(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 734-1057.
RC   STRAIN=C57BL/6J; TISSUE=Head;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 748-974.
RX   PubMed=7959727; DOI=10.1006/geno.1994.1309;
RA   Buxton R.S., Wheeler G.N., Pidsley S.C., Marsden M.D., Adams M.J.,
RA   Jenkins N.A., Gilbert D.J., Copeland N.G.;
RT   "Mouse desmocollin (Dsc3) and desmoglein (Dsg1) genes are closely linked in
RT   the proximal region of chromosome 18.";
RL   Genomics 21:510-516(1994).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12631242; DOI=10.1034/j.1600-0625.2003.120102.x;
RA   Pulkkinen L., Choi Y.W., Kljuic A., Uitto J., Mahoney M.G.;
RT   "Novel member of the mouse desmoglein gene family: Dsg1-beta.";
RL   Exp. Dermatol. 12:11-19(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: Binds to JUP/plakoglobin (By similarity). Interacts with PKP2
CC       (By similarity). {ECO:0000250|UniProtKB:Q02413}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TSF1};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q7TSF1}.
CC       Cell junction, desmosome. Cytoplasm {ECO:0000250|UniProtKB:Q02413}.
CC       Nucleus {ECO:0000250|UniProtKB:Q02413}.
CC   -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12631242}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 17 dpc.
CC       {ECO:0000269|PubMed:12631242}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26378.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BC154410; AAI54411.1; -; mRNA.
DR   EMBL; AK029294; BAC26378.1; ALT_FRAME; mRNA.
DR   EMBL; X74335; CAA52382.1; -; mRNA.
DR   CCDS; CCDS50231.1; -.
DR   PIR; B54742; B54742.
DR   RefSeq; NP_034209.2; NM_010079.2.
DR   AlphaFoldDB; Q61495; -.
DR   SMR; Q61495; -.
DR   BioGRID; 199323; 11.
DR   IntAct; Q61495; 4.
DR   MINT; Q61495; -.
DR   STRING; 10090.ENSMUSP00000076393; -.
DR   GlyCosmos; Q61495; 2 sites, No reported glycans.
DR   GlyGen; Q61495; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61495; -.
DR   PhosphoSitePlus; Q61495; -.
DR   SwissPalm; Q61495; -.
DR   MaxQB; Q61495; -.
DR   PaxDb; 10090-ENSMUSP00000076393; -.
DR   ProteomicsDB; 277504; -.
DR   DNASU; 13510; -.
DR   Ensembl; ENSMUST00000077146.4; ENSMUSP00000076393.4; ENSMUSG00000069441.4.
DR   GeneID; 13510; -.
DR   KEGG; mmu:13510; -.
DR   UCSC; uc008eel.2; mouse.
DR   AGR; MGI:94930; -.
DR   CTD; 13510; -.
DR   MGI; MGI:94930; Dsg1a.
DR   VEuPathDB; HostDB:ENSMUSG00000069441; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT01030000234624; -.
DR   HOGENOM; CLU_005284_0_0_1; -.
DR   InParanoid; Q61495; -.
DR   OMA; LRKVCMH; -.
DR   OrthoDB; 5314152at2759; -.
DR   PhylomeDB; Q61495; -.
DR   TreeFam; TF331809; -.
DR   Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR   Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR   BioGRID-ORCS; 13510; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Dsg1a; mouse.
DR   PRO; PR:Q61495; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q61495; Protein.
DR   Bgee; ENSMUSG00000069441; Expressed in tail skin and 56 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0045295; F:gamma-catenin binding; ISO: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   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   CDD; cd11304; Cadherin_repeat; 4.
DR   Gene3D; 2.60.40.60; Cadherins; 4.
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; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF9; DESMOGLEIN-1; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 3.
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.
DR   Genevisible; Q61495; MM.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cleavage on pair of basic residues; Cytoplasm; Glycoprotein; Membrane;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..49
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003839"
FT   CHAIN           50..1057
FT                   /note="Desmoglein-1-alpha"
FT                   /id="PRO_0000003840"
FT   TOPO_DOM        50..564
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        586..1057
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..269
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          270..389
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          386..493
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REPEAT          832..858
FT                   /note="Desmoglein repeat 1"
FT   REPEAT          859..888
FT                   /note="Desmoglein repeat 2"
FT   REPEAT          889..918
FT                   /note="Desmoglein repeat 3"
FT   REPEAT          919..946
FT                   /note="Desmoglein repeat 4"
FT   REPEAT          947..975
FT                   /note="Desmoglein repeat 5"
FT   REGION          490..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..547
FT                   /note="Polar residues"
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   CONFLICT        749..750
FT                   /note="GS -> EG (in Ref. 4; CAA52382)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1057 AA;  114597 MW;  EEF6AF26E57051A0 CRC64;
     MDWHSFRIAA LLLTSLVVLE VNSEFQIQVR DHNAKNGTIK WHSIRRQKRE WIKFAAACRE
     GEDNSKRNPI AKIHSDCAAN QPVTYRISGV GIDQPPYGIF IINQKTGEIN ITSIVDREVT
     PFFIIYCRAL NAQGQDLENP LELRVRVMDI NDNPPVFSMT TFLGQIEENS NANTLVMKLN
     ATDADEPNNL NSMIAFKIIR QEPSDSPMFI INRKTGEIRT MNNFLDREQY SQYSLVVRGS
     DRDGGADGMS AESECSITIL DVNDNIPYLE QSSYDITIEE NALHSQLVQI RVIDLDEEFS
     DNWKAIIFFI SGNEGNWFEI EMNERTNVGT LKVVKPLDYE AMKNLQLSIG VRNVAEFHQS
     IISQYRLTAT MVTVTVLNVI EGSVFRPGSK TFVVDSRMEA NHRVGEFVAT DLDTGRASTN
     VRYEMGNNPE NLLVVDSRTG IITLRNRVTM EQYQRLNGEY KGTVLSIDDS LQRTCTGTIV
     IELSGTGWVT GSESGGSSSG SGDDRDRVTN GYQGTSSTEN PQRVTGSWGG SGIDGTRPNT
     NPFQGDPDET LETPLYGDNV HFGPAGIGLL IMGFLVLGLV PFLLICCDCG GAPGGGAGFE
     PVPECSDGAI HTWAVEGPQP EPHEGITTIC VPQMPPGNAN VIEYIDNSGV YTNEYCGREM
     QDLGGGERTT GFELMDGVKT SAAPEICQEY SGTLRRNSMR ECRDGGLNMN FMESYFCQKA
     YAYADEDEGR PSNDCLLIYD IEGVGSPAGS VGCCSFIGED LDESFLDTLG PKFKKLADIS
     LGKEIDSYPD SDPSWPPQST EPMCPQHTEP LGSGHPPISP HFGTTTVISE NAYHSGPGVQ
     HPVPIPDPLG YGNVTVRESY TTSGTLKPSV HFHDNQQASN VVVTERVVGP ISGADLHGML
     EIPDLRGGAN VIVTERVIAP GSSLPTSLTI PNPQETSNVV VTERVIQPTS GMIGNLSMTP
     ELSSAHNVIV TERVVSGAGM SEIAGTAGLG GVGGIGSSGL VSTTMGASGT GLNMGGTATI
     GHMRSSSDHH FSQTVGSASP SMARSRITKY NTVQYSK
//