DSG4_RAT
ID DSG4_RAT Reviewed; 1040 AA.
AC Q6W3B0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Desmoglein-4;
DE Flags: Precursor;
GN Name=Dsg4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LAH VAL-228.
RC STRAIN=BDIX;
RX PubMed=15081105; DOI=10.1016/j.ygeno.2003.11.015;
RA Jahoda C.A., Kljuic A., O'Shaughnessy R., Crossley N., Whitehouse C.J.,
RA Robinson M., Reynolds A.J., Demarchez M., Porter R.M., Shapiro L.,
RA Christiano A.M.;
RT "The lanceolate hair rat phenotype results from a missense mutation in a
RT calcium coordinating site of the desmoglein 4 gene.";
RL Genomics 83:747-756(2004).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome {ECO:0000250}.
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 rats 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 one month. Hair regrows again a few days later,
CC following a 29-day cycle of external growth and loss. Almost complete
CC pelage hair loss occurs by 18 month.
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DR EMBL; AY314982; AAQ88398.1; -; mRNA.
DR RefSeq; NP_955784.1; NM_199490.1.
DR AlphaFoldDB; Q6W3B0; -.
DR SMR; Q6W3B0; -.
DR STRING; 10116.ENSRNOP00000031941; -.
DR GlyGen; Q6W3B0; 2 sites.
DR PaxDb; Q6W3B0; -.
DR PRIDE; Q6W3B0; -.
DR GeneID; 291754; -.
DR KEGG; rno:291754; -.
DR CTD; 147409; -.
DR RGD; 735015; Dsg4.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; Q6W3B0; -.
DR OMA; PEPMIHG; -.
DR OrthoDB; 250139at2759; -.
DR Reactome; R-RNO-6805567; Keratinization.
DR Reactome; R-RNO-6809371; Formation of the cornified envelope.
DR PRO; PR:Q6W3B0; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
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_0000003859"
FT CHAIN 50..1040
FT /note="Desmoglein-4"
FT /id="PRO_0000003860"
FT TOPO_DOM 50..633
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..1040
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 883..909
FT /note="Desmoglein repeat 1"
FT REPEAT 910..940
FT /note="Desmoglein repeat 2"
FT REGION 1015..1040
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 228
FT /note="E -> V (in lah)"
FT /evidence="ECO:0000269|PubMed:15081105"
SQ SEQUENCE 1040 AA; 114367 MW; B543E3A1B2968677 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 LKLVKMLDYE QEPNIYLSIG VRNQAEFHHS
VASQFQMHST PVRIQVINVR EGPTFRPSSM TFSLRGGMRG DSLMNYVLGT YTAIDMDTGS
PATNVRYVIG HDAGSWLKVD SRTGEIQFSR EFDTKSKYIT DGMYAAEILA IDDGSGRTAT
GTICIEVPDA NDYCPVIYAE SRSVCTHASS VRIYVNDHSF GAPFTFCVVD ESPDTADIWD
IRSINGTSAI LMTEQTLSPG PYQIPILVKD SHNRACELPQ TVLLDACLCD DYHVCLHSST
TGIYTGDTIW VTDDMGTVTD DGLRQSNVGL GPAGIGMIIL GLLLLFLSPL LLLMCCCKRR
QPEGLGTRFA PVPEGGEGVM QPWRIEGAHP EDRDVSNICV PMTASNTQDR IDSSEIYTNT
YAGGGTVEGG VSGVELNTGV GTAAGIAAGG ATGTLRKRSS TIGTLREYQD TGMNMAFLDS
YFSEKAYAYA DEDEGRPAND CLLIYDHEGT GSPVGSIGCC SWIVDDLDES YMETLDPKFR
TLAEICLDTE IEPFPSHQAC IPISTDLPLL GPNYFVNESS GMTLSEAEFQ AEMAAASEPM
IHGDIIVTET YTATDPCVQP TTIVFDSQLP PNVVVTETVM APVYDVQGNI CVPAEIANTH
NVYYAERVVA SPGVPDMGNG NIGDTCIGPV MSGGILVGPE IQVTQMMSPD IHISQTTRST
SPMTSQHRVT RYSNIHYSRQ
