DSG4_MOUSE
ID DSG4_MOUSE Reviewed; 1041 AA.
AC Q7TMD7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Desmoglein-4;
DE Flags: Precursor;
GN Name=Dsg4;
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], FUNCTION, AND VARIANT LAH SER-196.
RC STRAIN=PWK; TISSUE=Skin;
RX PubMed=12705872; DOI=10.1016/s0092-8674(03)00273-3;
RA Kljuic A., Bazzi H., Sundberg J.P., Martinez-Mir A., O'Shaughnessy R.,
RA Mahoney M.G., Levy M., Montagutelli X., Ahmad W., Aita V.M., Gordon D.,
RA Uitto J., Whiting D., Ott J., Fischer S., Gilliam T.C., Jahoda C.A.B.,
RA Morris R.J., Panteleyev A.A., Nguyen V.T., Christiano A.M.;
RT "Desmoglein 4 in hair follicle differentiation and epidermal adhesion.
RT Evidence from inherited hypotrichosis and acquired pemphigus vulgaris.";
RL Cell 113:249-260(2003).
RN [2]
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).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion. Coordinates the transition from proliferation to
CC differentiation in hair follicle keratinocytes.
CC {ECO:0000269|PubMed:12705872}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the skin; during the anagen
CC stage of hair follicles in the matrix, precortex and inner rooth
CC sheath. {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}.
CC -!- DISEASE: Note=Defects in Dsg4 are the cause of an autosomal recessive
CC phenotype lanceolate hair (lah). Lah mice pups develop only a few short
CC hairs on the head and neck which form a lance head at the tip and
CC disappear within a few month. They have thickened skin and do not
CC exhibit any growth retardation.
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DR EMBL; AY227349; AAP44999.1; -; mRNA.
DR EMBL; AY191584; AAO91793.1; -; mRNA.
DR CCDS; CCDS29082.1; -.
DR RefSeq; NP_853543.1; NM_181564.2.
DR AlphaFoldDB; Q7TMD7; -.
DR SMR; Q7TMD7; -.
DR BioGRID; 201094; 1.
DR IntAct; Q7TMD7; 1.
DR STRING; 10090.ENSMUSP00000019426; -.
DR GlyGen; Q7TMD7; 2 sites.
DR iPTMnet; Q7TMD7; -.
DR PhosphoSitePlus; Q7TMD7; -.
DR MaxQB; Q7TMD7; -.
DR PaxDb; Q7TMD7; -.
DR PRIDE; Q7TMD7; -.
DR ProteomicsDB; 277413; -.
DR Antibodypedia; 22155; 112 antibodies from 25 providers.
DR DNASU; 16769; -.
DR Ensembl; ENSMUST00000019426; ENSMUSP00000019426; ENSMUSG00000001804.
DR GeneID; 16769; -.
DR KEGG; mmu:16769; -.
DR UCSC; uc008een.1; mouse.
DR CTD; 147409; -.
DR MGI; MGI:2661061; Dsg4.
DR VEuPathDB; HostDB:ENSMUSG00000001804; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; Q7TMD7; -.
DR OMA; PEPMIHG; -.
DR OrthoDB; 250139at2759; -.
DR PhylomeDB; Q7TMD7; -.
DR TreeFam; TF331809; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 16769; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q7TMD7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TMD7; protein.
DR Bgee; ENSMUSG00000001804; Expressed in lip and 6 other tissues.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IMP:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP: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; Disease variant; Glycoprotein;
KW Membrane; Metal-binding; 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_0000003857"
FT CHAIN 50..1041
FT /note="Desmoglein-4"
FT /id="PRO_0000003858"
FT TOPO_DOM 50..634
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..1041
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..385
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 389..497
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 884..910
FT /note="Desmoglein repeat 1"
FT REPEAT 911..941
FT /note="Desmoglein repeat 2"
FT REGION 1014..1041
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 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 196
FT /note="Y -> S (in lah)"
FT /evidence="ECO:0000269|PubMed:12705872"
SQ SEQUENCE 1041 AA; 114449 MW; 230ECC0553048B2B CRC64;
MDWLLFRNIC LLILFMVVLG VNSEFIVEVK ELDIENGTTT WQTVRRQKRE WIKFAAACRE
GEDNSKRNPI ARIRSDCEVS QRITYRISGA GIDRPPYGVF TINPRTGEIN ITSVVDREIT
PLFLIHCRAL NSRGEDLERP LELRVKVMDV NDNPPVFTQN VYTANIEENS DANALVVKLS
ATDADEDNHL NSKIAYKIIS QEPAGAPMFM VNRYTGEVRT MSNFLDREQH SMYNLLVRGS
DRDGATDGLS SECDCRIKIL DVNDNFPILE KTSYSASIEE NCLSSELIRL QAIDLDEEGT
DNWLAQYSIL SGNDGNWFEI QTDPKTNEGI LKVVKMLDYE QEPNIYLSIG VRNQAEFHHS
VASQFQMHST PVRIQVVNVR EGPTFSPSSM TFSLRGGMRG ASLMNYVLGT YTAIDMDTGN
PATNVRYVIG HDAGSWLKVD SRTGEIQFSR EFDMKSKYIT DGIYAAQILA IDDGSGRTAT
GTICIEIPDA NDYCPVIYAE SRSVCTHASS VRIYVNDHSF GSPFTFCVVD ESPDIANIWD
IRSINGTSAI LMTEQTLSPG PYQIPILVKD SHNRACELPQ TVLLDACFCD DHHVCLHSST
TGIYTGDITW VTDDMYGTVT DDGVRQSNVG LGPAGIGMII LGLLLLLLSP LLLLMCCCKR
RQPEGLGTRF APVPEGGEGV MQPWRIEGAH PEDRDVSNIC VPMTASNTQD RIDSSEIYTN
TYAGGGTVEG GVSGVELNTG VGTATGMVAA GATGTLRKRS STIGTLREYQ DTGMNMAFLD
SYFSEKAYAY ADEDEGRPAN DCLLIYDHEG AGSPVGSIGC CSWIVDDLDE SYIETLDPKF
RTLAEICLDT EIEPFPSHQA CIPISTDLPL LGPNYFVNES SGMTLSEAEF QAEMAAASEP
MIHGDIIVTE TYTTSDPCVQ PTTIVFDSQI PPNVVVTETV MAPVYDVQGN ICVPAEIANT
HNVYYAERVV ASPGIPDMGN SNISDACIGP VMSGGILVGP EIQVTQMMSP DIHISQTTGS
TSPMTSQHRV TRYSNMHYSR Q
