DSG1C_MOUSE
ID DSG1C_MOUSE Reviewed; 911 AA.
AC Q7TSF0; Q7TQ61;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Desmoglein-1-gamma;
DE Short=Dsg1-gamma;
DE AltName: Full=Desmoglein-6;
DE Flags: Precursor;
GN Name=Dsg1c; Synonyms=Dsg6;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=PWK; TISSUE=Skin;
RX PubMed=12631243; DOI=10.1034/j.1600-0625.2003.120103.x;
RA Kljuic A., Christiano A.M.;
RT "A novel mouse desmosomal cadherin family member, desmoglein 1 gamma.";
RL Exp. Dermatol. 12:20-29(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP 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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TSF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSF0-2; Sequence=VSP_012903, VSP_012904;
CC -!- TISSUE SPECIFICITY: Expressed in epidermis, brain, liver, skeletal,
CC muscle and testis. {ECO:0000269|PubMed:12631243,
CC ECO:0000269|PubMed:12787123}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 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; AY314983; AAP79926.1; -; mRNA.
DR EMBL; AY192159; AAP31153.1; -; mRNA.
DR CCDS; CCDS29079.1; -. [Q7TSF0-1]
DR RefSeq; NP_859008.1; NM_181680.2. [Q7TSF0-1]
DR AlphaFoldDB; Q7TSF0; -.
DR SMR; Q7TSF0; -.
DR BioGRID; 229273; 2.
DR STRING; 10090.ENSMUSP00000054799; -.
DR GlyGen; Q7TSF0; 3 sites.
DR iPTMnet; Q7TSF0; -.
DR PhosphoSitePlus; Q7TSF0; -.
DR MaxQB; Q7TSF0; -.
DR PaxDb; Q7TSF0; -.
DR PeptideAtlas; Q7TSF0; -.
DR PRIDE; Q7TSF0; -.
DR DNASU; 211924; -.
DR Ensembl; ENSMUST00000054128; ENSMUSP00000054799; ENSMUSG00000034774. [Q7TSF0-1]
DR GeneID; 211924; -.
DR KEGG; mmu:211924; -.
DR UCSC; uc008eej.1; mouse. [Q7TSF0-2]
DR UCSC; uc008eek.1; mouse. [Q7TSF0-1]
DR CTD; 211924; -.
DR MGI; MGI:2664358; Dsg1c.
DR VEuPathDB; HostDB:ENSMUSG00000034774; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_2_1; -.
DR InParanoid; Q7TSF0; -.
DR OrthoDB; 250139at2759; -.
DR PhylomeDB; Q7TSF0; -.
DR TreeFam; TF331809; -.
DR BioGRID-ORCS; 211924; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q7TSF0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSF0; protein.
DR Bgee; ENSMUSG00000034774; Expressed in liver and 6 other tissues.
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 Pfam; PF00028; Cadherin; 3.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01819; DESMOGLEIN.
DR SMART; SM00112; CA; 3.
DR SUPFAM; SSF49313; SSF49313; 4.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 3.
PE 1: Evidence at protein 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:0000255"
FT PROPEP 24..49
FT /evidence="ECO:0000255"
FT /id="PRO_0000003843"
FT CHAIN 50..911
FT /note="Desmoglein-1-gamma"
FT /id="PRO_0000003844"
FT TOPO_DOM 50..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..911
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 REPEAT 783..809
FT /note="Desmoglein repeat 1"
FT REPEAT 810..839
FT /note="Desmoglein repeat 2"
FT REPEAT 840..869
FT /note="Desmoglein repeat 3"
FT REPEAT 870..897
FT /note="Desmoglein repeat 4"
FT REPEAT 898..911
FT /note="Desmoglein repeat 5; truncated"
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 CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 427..429
FT /note="RYV -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12631243"
FT /id="VSP_012903"
FT VAR_SEQ 430..911
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12631243"
FT /id="VSP_012904"
FT CONFLICT 442
FT /note="S -> SRT (in Ref. 1; AAP79926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 100516 MW; 2864E998106CFB6F CRC64;
MDWHSFRIAA LLLTSLVVLE VNSEFQIQVR DHNAKNGTIK WHSIRRQKRE WIKFAAACRE
GEDNSKRNPI AKIHSDCAAN QPVTYRISGV GIDQPPYGIF IINQKTGEIN ITSIVDREVT
PFFIIYCRAL NAQGQDLENP LELRVRVMDI NDNPPVFSMT TFLGQIEENS NANTLVMKLN
ATDADEPNNL NSMIAFKIIR QEPSDSPMFT INRKTGEIRT MNNFLDREQY SQYSLVVRGS
DRDGGADGMS AESECSITIL DVNDNIPYLE QSSYDITIEE NTLHSQLLQI RVIDLDEEFS
DNWKAIIFFI SGNEGNWFEI EMNERTNVGT LKVVKPLDYE AVKNLQLCIG VRNVAEFHQS
IISQYRLTVT LITVTVLNVV KGCVFQPGSK TFIVDSRMEA NHTVGEFLAT DCETGQATNK
FKNVRYRYVM GNNPENLLVV DSGIITLRNR VTMEQYERLN KRYEGTVLSI HDSLQRTCTG
TIIMVLCGFW TTTEHPTTST EKPVTLSITP NVDNVHFGPA GIGLLIMGFL VLGLVPFLLI
SCDCGGAPGG GAGFEPVPEC SDGAIHTWAV EGPQPGGITT ICVPQMPPGN ANVIEYIDNS
GVYTNEYCGR EMQDLGGGER TTGFELMDGV KTSAAPEICQ EYSGTLRRNS MRECRDGGLN
MNFMESYFCQ KAYAYADEDE GRPSNDCLLI YDIEGVGSPA GSVGCCSFIE DLDESFLDTL
GPKFKKLADI SLGKEIDSYP DPDPSWPPQS TEPICPQHME QLASGHPSIS PHFGKTTVIS
ENAYPSGPGV QHPMLIPDPL GYGNITVRES YTTSGTLKPS VHFHDNQQAS NVVVTERVVG
PISGADLHGM LEIPALRDGT NVIVTERVIA PGSSLPNSLT IPNPRETSNV VVTERVIQPT
SGMIGNLSIP P
