DSG1A_MOUSE
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 03-AUG-2022, entry version 159.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome.
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 GlyGen; Q61495; 2 sites.
DR iPTMnet; Q61495; -.
DR PhosphoSitePlus; Q61495; -.
DR MaxQB; Q61495; -.
DR PaxDb; Q61495; -.
DR PRIDE; Q61495; -.
DR ProteomicsDB; 277504; -.
DR DNASU; 13510; -.
DR Ensembl; ENSMUST00000077146; ENSMUSP00000076393; ENSMUSG00000069441.
DR GeneID; 13510; -.
DR KEGG; mmu:13510; -.
DR UCSC; uc008eel.2; mouse.
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; MDWRFFR; -.
DR OrthoDB; 250139at2759; -.
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 76 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 tissues.
DR Genevisible; Q61495; MM.
DR GO; GO:0005911; C:cell-cell junction; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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_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
