DSC1_MOUSE
ID DSC1_MOUSE Reviewed; 886 AA.
AC P55849; E9QJX2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Desmocollin-1;
DE Flags: Precursor;
GN Name=Dsc1;
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] (ISOFORMS 1A AND 1B).
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=8823356; DOI=10.1111/1523-1747.ep12582790;
RA King I.A., O'Brien T.J., Buxton R.S.;
RT "Expression of the 'skin-type' desmosomal cadherin DSC1 is closely linked
RT to the keratinization of epithelial tissues during mouse development.";
RL J. Invest. Dermatol. 107:531-538(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
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. May contribute to epidermal cell positioning
CC (stratification) by mediating differential adhesiveness between cells
CC that express different isoforms. Linked to the keratinization of
CC epithelial tissues.
CC -!- SUBUNIT: Binds to JUP/plakoglobin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell junction, desmosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1A;
CC IsoId=P55849-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=P55849-2; Sequence=VSP_000653, VSP_000654;
CC -!- DOMAIN: Calcium may be bound by the cadherin-like repeats.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97986; CAA66628.1; -; mRNA.
DR EMBL; X97986; CAA66629.1; -; mRNA.
DR EMBL; AC132314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS89198.1; -. [P55849-1]
DR RefSeq; NP_001278733.1; NM_001291804.1. [P55849-1]
DR AlphaFoldDB; P55849; -.
DR SMR; P55849; -.
DR BioGRID; 199318; 8.
DR STRING; 10090.ENSMUSP00000042303; -.
DR GlyGen; P55849; 4 sites.
DR iPTMnet; P55849; -.
DR PhosphoSitePlus; P55849; -.
DR MaxQB; P55849; -.
DR PaxDb; P55849; -.
DR PeptideAtlas; P55849; -.
DR PRIDE; P55849; -.
DR ProteomicsDB; 275403; -. [P55849-1]
DR ProteomicsDB; 275404; -. [P55849-2]
DR Antibodypedia; 2439; 232 antibodies from 28 providers.
DR DNASU; 13505; -.
DR Ensembl; ENSMUST00000224432; ENSMUSP00000153639; ENSMUSG00000044322. [P55849-1]
DR GeneID; 13505; -.
DR KEGG; mmu:13505; -.
DR UCSC; uc008eeh.3; mouse. [P55849-1]
DR CTD; 1823; -.
DR MGI; MGI:109173; Dsc1.
DR VEuPathDB; HostDB:ENSMUSG00000044322; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR InParanoid; P55849; -.
DR OMA; QVTAIDH; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 13505; 2 hits in 71 CRISPR screens.
DR PRO; PR:P55849; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P55849; protein.
DR Bgee; ENSMUSG00000044322; Expressed in tail skin and 46 other tissues.
DR ExpressionAtlas; P55849; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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 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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
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; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..134
FT /evidence="ECO:0000255"
FT /id="PRO_0000003865"
FT CHAIN 135..886
FT /note="Desmocollin-1"
FT /id="PRO_0000003866"
FT TOPO_DOM 135..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..242
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..354
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 355..471
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 472..575
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 576..682
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08554"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 822..832
FT /note="KVYLCGQAEEH -> ESIRGHTLIKN (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:8823356"
FT /id="VSP_000653"
FT VAR_SEQ 840..886
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:8823356"
FT /id="VSP_000654"
FT CONFLICT 177
FT /note="V -> D (in Ref. 1; CAA66628/CAA66629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 98938 MW; C06C012644BCC59A CRC64;
MAVACAAPGS TFSKQLLFFL LVLVLFCDAC QKVSLHVPSH LKAETPVGKV NLEECLKSPS
LILSSDPAFR ILEDGTIYTT HDLLLSSEKR GFSILLSDGQ GQEQKKLEVV LSAREKKVFR
KRHTKEPVHN RSKRRWAPIP CSLMENSLGP FPQHIQQIQS DAAQNYTIFY SISGPGVDKE
PYNLFYIEKD TGDIYCTRSI DREQYDQFLV YGYATTADGY APDYPLPLLF KVEDDNDNAP
YFETKLTVFS VPENCRSGTS VGQVTAIDKD EPGTLHTRLK YKILQQIPDQ PKHFSIHPDT
GVITTTTPLL DREKCDTYKL VMEVRDMGGQ PFGLFTTGTI TISLEDENDN SPYFTQTSYT
TEVEENRIDV EILRMVVHDQ DLPNTPHSKA VYTILKGNEN GNFKITTDPN TNEGVLCVVK
PLNYEVSRQV TLQIGVLNEA QFTNAANAQP PTMCTTTVTV KIKDRDEGPE CQPPVKVIQS
KDGLPAGQEL LGYKAVDPET SSGEGLRYEM VGDEDNWFEI NKITGDLRTV KVLDRESKFV
KNNQYNISVV ATDTAGRSCT GTLVVLLEDF NDHPPQIDKE VTICQQEKDF AVLEPIDLDG
PDNGPPFQFL LDNSSSKLWT LESQDGKRAI LRQRHNLNYN YYSVPIQIQD RHGFSAKHVL
SVRVCDCTTP TECRMAVKEE RDAKPNIILG KWAILAMVLG SALLLCILFT CFCVTTTKRT
VKKCFPDDVA QQNLIVSNTE GPGEEVTEAN IRLPTQTANI CDTSMSVGTL GGQGIKTQQS
FEMVKGGHTL ESHKGGVLGA AEPGRYAYTD WQTFTQPRLG EKVYLCGQAE EHKHCEDYVR
PYNYEGKGSM AGSVGCCSDR QEEEGLEFLD QLEPKFRTLA KTCVKK
