DSC2_MOUSE
ID DSC2_MOUSE Reviewed; 902 AA.
AC P55292; Q64734;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Desmocollin-2;
DE AltName: Full=Epithelial type 2 desmocollin;
DE Flags: Precursor;
GN Name=Dsc2; Synonyms=Dsc3;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=7711832; DOI=10.3109/09687689409160432;
RA Lorimer J.E., Hall L.S., Clarke J.P., Collins J.E., Fleming T.P.,
RA Garrod D.R.;
RT "Cloning, sequence analysis and expression pattern of mouse desmocollin 2
RT (DSC2), a cadherin-like adhesion molecule.";
RL Mol. Membr. Biol. 11:229-236(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 344-637.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=7959727; DOI=10.1006/geno.1994.1309;
RA Buxton R.S., Wheeler G.N., Pidsley S.C., Marsden M.D., Adams M.J.,
RA Jenkins N.A., Gilbert D.J., Copeland N.G.;
RT "Mouse desmocollin (Dsc3) and desmoglein (Dsg1) genes are closely linked in
RT the proximal region of chromosome 18.";
RL Genomics 21:510-516(1994).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
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=2A;
CC IsoId=P55292-1; Sequence=Displayed;
CC Name=2B;
CC IsoId=P55292-2; Sequence=VSP_000659, VSP_000660;
CC -!- TISSUE SPECIFICITY: In all epithelia tested and heart.
CC -!- DOMAIN: Calcium may be bound by the cadherin-like repeats.
CC {ECO:0000305}.
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; L33779; AAA79177.1; -; mRNA.
DR EMBL; L33779; AAA79176.1; -; mRNA.
DR EMBL; X73885; CAA52089.1; -; mRNA.
DR CCDS; CCDS29077.1; -. [P55292-2]
DR CCDS; CCDS84361.1; -. [P55292-1]
DR PIR; A54742; A54742.
DR RefSeq; NP_001304294.1; NM_001317365.1. [P55292-1]
DR RefSeq; NP_038533.1; NM_013505.4. [P55292-2]
DR AlphaFoldDB; P55292; -.
DR SMR; P55292; -.
DR BioGRID; 199319; 3.
DR STRING; 10090.ENSMUSP00000042905; -.
DR GlyGen; P55292; 4 sites.
DR iPTMnet; P55292; -.
DR PhosphoSitePlus; P55292; -.
DR MaxQB; P55292; -.
DR PaxDb; P55292; -.
DR PeptideAtlas; P55292; -.
DR PRIDE; P55292; -.
DR ProteomicsDB; 277407; -. [P55292-1]
DR ProteomicsDB; 277408; -. [P55292-2]
DR Antibodypedia; 2782; 347 antibodies from 32 providers.
DR DNASU; 13506; -.
DR Ensembl; ENSMUST00000039247; ENSMUSP00000042905; ENSMUSG00000024331. [P55292-2]
DR Ensembl; ENSMUST00000075214; ENSMUSP00000074702; ENSMUSG00000024331. [P55292-1]
DR GeneID; 13506; -.
DR KEGG; mmu:13506; -.
DR UCSC; uc008eec.1; mouse. [P55292-1]
DR CTD; 1824; -.
DR MGI; MGI:103221; Dsc2.
DR VEuPathDB; HostDB:ENSMUSG00000024331; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_2_1; -.
DR InParanoid; P55292; -.
DR OMA; LCNCITE; -.
DR PhylomeDB; P55292; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 13506; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dsc2; mouse.
DR PRO; PR:P55292; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P55292; protein.
DR Bgee; ENSMUSG00000024331; Expressed in conjunctival fornix and 189 other tissues.
DR ExpressionAtlas; P55292; baseline and differential.
DR Genevisible; P55292; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; 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:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; ISO:MGI.
DR GO; GO:0086042; P:cardiac muscle cell-cardiac muscle cell adhesion; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; 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; 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; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
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 Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..135
FT /evidence="ECO:0000255"
FT /id="PRO_0000003871"
FT CHAIN 136..902
FT /note="Desmocollin-2"
FT /id="PRO_0000003872"
FT TOPO_DOM 136..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 136..243
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..355
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 356..471
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 472..579
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 580..694
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 838..848
FT /note="KVQFCHTDDNQ -> ETIRGHTLIKN (in isoform 2B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000659"
FT VAR_SEQ 849..902
FT /note="Missing (in isoform 2B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000660"
SQ SEQUENCE 902 AA; 99961 MW; E233F8CB20ACCAB0 CRC64;
MAAVGSMRSG SPAFGLGHLL TLAILALASD ACKEVVLQVP SELPAEKFVG RVNLMDCLKS
ADIVHLSDPD FQVLEDGSVY TTSSVVLSSG QRSFTIWLFS TDSQEEREIS VHLEGPVEVL
NKRPHTEKVL SRAKRRWAPI PCSMLENSLG PFPLFLQQIQ SDTAQNYTIY YSIRGPGVDK
EPLNLFYVER DTGNLYCTGR VDREQYESFE LTAFATTPDG YTPEYPLPLL IKIEDENDNY
PIFTQKLYSF TVQENSRIGS IVGEVCATDL DEPDTMHTRL RYSILEQSPS PPMLFTMHPS
TGVITTTSAQ LDRELIDKYQ LLIKVQDMDG QYFGLHTTAK CIITIEDVND NLPTFTRTTY
VTSVEENTVN VEILRLTVQD KDLVNSPNWR ANYTILKGNE NGNFKIVTDP KTNEGILCVI
KPLDYEERQQ VTLQIGVVNE APYTREASSK SPMSTATVTV TVTNQDEGPE CIPPMQTVRI
QENVPVGTRN DGYKAYDPET RSSSGIRYRK LSDPRGWVTV NEDSGSITIF RALDREAETV
RNGIYNITVL ALDADGRSCT GTLGIILEDV NDNGPFIPKQ TVVICKATMS SAEIVAVDLD
DPVNGPPFDF SLESSDSEVQ RMWRLTRIND TAARLSYQND PSFGSYAVPI RVTDRLGLSS
VTTLNVLVCD CITESDCTLR SGERTGYADV RLGPWAILAI LLGIALLFCI LFTLVCSVSR
ASKQQKILPD DLAQQNLIVS NTEAPGDDKV YSTNGLTTQT MGASGQTAFT TMGTGVKSGG
QETIEMVKGG QQTLDSRRGA GYHHHTLDPC RGGHVEVDNY RHTYSEWYNF IQPRLGDKVQ
FCHTDDNQKL AQDYVLTYNY EGKGSAAGSV GCCSDLQEED GLEFLDHLEP KFRTLAEVCA
KR
