DSG1B_MOUSE
ID DSG1B_MOUSE Reviewed; 1060 AA.
AC Q7TSF1; Q7TQ60;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Desmoglein-1-beta;
DE Short=Dsg1-beta;
DE AltName: Full=Desmoglein-5;
DE Flags: Precursor;
GN Name=Dsg1b; Synonyms=Dsg5;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Skin;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=PWK; TISSUE=Keratinocyte;
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
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
CC {ECO:0000269|PubMed:12631242}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermis.
CC {ECO:0000269|PubMed:12631242, ECO:0000269|PubMed:12787123}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 17 dpc.
CC {ECO:0000269|PubMed:12631242, 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; AY192158; AAP31152.1; -; mRNA.
DR EMBL; AY315940; AAP80571.1; -; mRNA.
DR CCDS; CCDS29081.1; -.
DR RefSeq; NP_859010.1; NM_181682.2.
DR AlphaFoldDB; Q7TSF1; -.
DR SMR; Q7TSF1; -.
DR BioGRID; 230374; 3.
DR IntAct; Q7TSF1; 4.
DR MINT; Q7TSF1; -.
DR STRING; 10090.ENSMUSP00000076026; -.
DR GlyGen; Q7TSF1; 2 sites.
DR iPTMnet; Q7TSF1; -.
DR PhosphoSitePlus; Q7TSF1; -.
DR MaxQB; Q7TSF1; -.
DR PaxDb; Q7TSF1; -.
DR PRIDE; Q7TSF1; -.
DR ProteomicsDB; 277412; -.
DR DNASU; 225256; -.
DR Ensembl; ENSMUST00000076737; ENSMUSP00000076026; ENSMUSG00000061928.
DR GeneID; 225256; -.
DR KEGG; mmu:225256; -.
DR UCSC; uc008eem.1; mouse.
DR CTD; 225256; -.
DR MGI; MGI:2664357; Dsg1b.
DR VEuPathDB; HostDB:ENSMUSG00000061928; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; Q7TSF1; -.
DR OMA; QCGASIN; -.
DR OrthoDB; 250139at2759; -.
DR PhylomeDB; Q7TSF1; -.
DR TreeFam; TF331809; -.
DR BioGRID-ORCS; 225256; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q7TSF1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSF1; protein.
DR Bgee; ENSMUSG00000061928; Expressed in esophagus and 13 other tissues.
DR ExpressionAtlas; Q7TSF1; baseline and differential.
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: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 1: Evidence at protein 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_0000003841"
FT CHAIN 50..1060
FT /note="Desmoglein-1-beta"
FT /id="PRO_0000003842"
FT TOPO_DOM 50..567
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..1060
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 835..861
FT /note="Desmoglein repeat 1"
FT REPEAT 862..891
FT /note="Desmoglein repeat 2"
FT REPEAT 892..921
FT /note="Desmoglein repeat 3"
FT REPEAT 922..949
FT /note="Desmoglein repeat 4"
FT REPEAT 950..978
FT /note="Desmoglein repeat 5"
FT REGION 490..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 929
FT /note="T -> N (in Ref. 2; AAP80571)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038
FT /note="I -> V (in Ref. 2; AAP80571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1060 AA; 114454 MW; 58873A358C52B9C8 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 QSSYDIEIEE NALHSQLVQI RVIDLDEEFS
DNWKAIIFFI SGNEGNWFEI EMNERTNVGT LKVVKPLDYE AMKNLQLSIG VRNVAEFHQS
IISQYRLTAT MVTVTVLNVI EGSVFRPGSK TFVVDSRMEA NHRVGEFVAT DLDTGRASTN
VRYEMGNNPE NLLVVDSRTG IITLRNRVTM EQYQRLNGEY KGTVLSIDDS LQRTCTGTIV
IELSGTGWVP GSDGGGSSSG SGGNRDPVTN GYQGTSTVGP QRVTGSGGVT SSGGGSGVNN
TPGRQNPLDE PEPEPFDITE DNVHFGPAGI GLLIMGFLVL GLVPFLLICC DCGGAPGGGA
GFEPVPECSD GAIHTWAIEG PQPEPHDGIT TICVPQMPPG NANVIEYIDN SGVYTNEYCG
REMQDLGGGE RTTGFELMDG VKTSAAPEIC QEYSGTLRRN SMRECRDGGL NMNFMESYFC
QKAYAYADED EGRPSNDCLL IYDIEGVGSP AGSVGCCSFI GEDLDESFLD TLGPKFKKLA
DISLGKEIDS YPDPDSSWPP QSTEPMCPQS TEPLGSGYPP ISPHFGTTTV ISENAYPSGP
GVQHPLPIPD PLGYGNVTVR ESYATSGTLK PSVHFHDNQQ ASNVVVTERV VGPVPGADLH
GMLEIPDLRD GTNVIVTERV IAPGSSLPTS LTIPNPRETS NVVVTERVIQ PTSGMIGNLS
MTPELSSAQN VIVTERVVSG AGMSGIAGTA GLGGVGGIGS SGLVSTTMGA AGTGLNMGGT
ATIGHMRSSS DHHFSQTIGS ASPNMARSRI TKYSTVQYSK
