DSC3_MOUSE
ID DSC3_MOUSE Reviewed; 896 AA.
AC P55850; G5E8S6; O55110; O55122;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Desmocollin-3;
DE Flags: Precursor;
GN Name=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], AND TISSUE SPECIFICITY.
RX PubMed=9389456;
RX DOI=10.1002/(sici)1097-0177(199711)210:3<315::aid-aja11>3.0.co;2-9;
RA Chidgey M.A.J., Yue K.K.M., Gould S., Byrne C., Garrod D.R.;
RT "Changing pattern of desmocollin 3 expression accompanies epidermal
RT organisation during skin development.";
RL Dev. Dyn. 210:315-327(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 709-874, ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=9404003; DOI=10.1046/j.1432-0436.1997.6220083.x;
RA King I.A., Angst B.D., Hunt D.M., Kruger M., Arnemann J., Buxton R.S.;
RT "Hierarchical expression of desmosomal cadherins during stratified
RT epithelial morphogenesis in the mouse.";
RL Differentiation 62:83-96(1997).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-630.
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, desmosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3A;
CC IsoId=P55850-1; Sequence=Displayed;
CC Name=3B;
CC IsoId=P55850-2; Sequence=VSP_000665, VSP_000666;
CC -!- TISSUE SPECIFICITY: First expressed at 13.0 dpc in epithelium of
CC whisker pads and external nares, and in most mature vibrissa follicles.
CC 12 hours later, prominently expressed in whiskers and tactile follicles
CC above the eye. At 14.5 dpc, also expressed in developing nails and
CC teeth and, at low levels, in ventral and lateral skin. At 15.5 dpc,
CC highly expressed in general body epidermis and at 16.5 dpc, detected
CC over entire embryo. In the adult, highly expressed in basal layers of
CC stratified cells. {ECO:0000269|PubMed:9389456,
CC ECO:0000269|PubMed:9404003}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA72045.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y11169; CAA72045.1; ALT_FRAME; mRNA.
DR EMBL; AC105159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466557; EDK96937.1; -; Genomic_DNA.
DR EMBL; AJ000329; CAA03996.1; -; mRNA.
DR CCDS; CCDS37744.1; -. [P55850-1]
DR CCDS; CCDS89197.1; -. [P55850-2]
DR RefSeq; NP_001278738.1; NM_001291809.1. [P55850-2]
DR RefSeq; NP_031908.3; NM_007882.3. [P55850-1]
DR RefSeq; XP_006525656.1; XM_006525593.3. [P55850-1]
DR AlphaFoldDB; P55850; -.
DR SMR; P55850; -.
DR BioGRID; 199320; 1.
DR STRING; 10090.ENSMUSP00000111514; -.
DR GlyGen; P55850; 4 sites.
DR iPTMnet; P55850; -.
DR PhosphoSitePlus; P55850; -.
DR CPTAC; non-CPTAC-4029; -.
DR PaxDb; P55850; -.
DR PeptideAtlas; P55850; -.
DR PRIDE; P55850; -.
DR ProteomicsDB; 275405; -. [P55850-1]
DR ProteomicsDB; 275406; -. [P55850-2]
DR Antibodypedia; 7988; 240 antibodies from 33 providers.
DR DNASU; 13507; -.
DR Ensembl; ENSMUST00000115848; ENSMUSP00000111514; ENSMUSG00000059898. [P55850-2]
DR Ensembl; ENSMUST00000225110; ENSMUSP00000153261; ENSMUSG00000059898. [P55850-1]
DR GeneID; 13507; -.
DR KEGG; mmu:13507; -.
DR UCSC; uc008eea.2; mouse.
DR CTD; 1825; -.
DR MGI; MGI:1194993; Dsc3.
DR VEuPathDB; HostDB:ENSMUSG00000059898; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR InParanoid; P55850; -.
DR OMA; TLIMKVQ; -.
DR OrthoDB; 120970at2759; -.
DR PhylomeDB; P55850; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 13507; 2 hits in 73 CRISPR screens.
DR PRO; PR:P55850; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P55850; protein.
DR Bgee; ENSMUSG00000059898; Expressed in tail skin and 103 other tissues.
DR ExpressionAtlas; P55850; baseline and differential.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030057; C:desmosome; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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:0001701; P:in utero embryonic development; IMP:MGI.
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; 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 Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..135
FT /evidence="ECO:0000255"
FT /id="PRO_0000003877"
FT CHAIN 136..896
FT /note="Desmocollin-3"
FT /id="PRO_0000003878"
FT TOPO_DOM 136..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..896
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..472
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 473..580
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 581..691
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
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 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
FT VAR_SEQ 832..839
FT /note="KLHVCNQN -> DSIRGHTG (in isoform 3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000665"
FT VAR_SEQ 840..896
FT /note="Missing (in isoform 3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000666"
FT CONFLICT 45
FT /note="A -> V (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="I -> T (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="M -> I (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="L -> I (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="I -> Y (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="V -> I (in Ref. 4; CAA03996)"
FT /evidence="ECO:0000305"
FT CONFLICT 730..731
FT /note="QQ -> HE (in Ref. 1; CAA72045 and 4; CAA03996)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="D -> N (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="E -> K (in Ref. 1; CAA72045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 100203 MW; DC630F26CD00CB3D CRC64;
MVVPEFRSPQ CRALCTKLLL TLWVFSFVGE ACKKVTFHVP STLEADKIIG RVSLKECLSS
ADGIMPSDPD FRVLDDGSVY PTRAVVLSDE KRSFTIQLSD SKMQTQKEIP VILEHKKKVL
KKRHTKETVL RRSKRRWAPI PCSMQENSLG PFPLFLQQVQ SDAAQNYTVF YSISGRGADQ
EPLNWFFIER DTGNLYCTRP VDREEYDVFD LIAYASTADG YSADLPLPLP IKIEDENDNY
PLFTEAIYAF EVPEGSRLGT VVGTVCATDK DEPDTMHTRL KYSILEQTPP SPGLFSVHPD
TGVITTVSHY MDREVVDKYK LIMKVQDMNG QFFGLISTST CIITVQDSND NAPTFRQNTY
ETAVEENTYN VEILRIPVDD KDMINTANWK ANFTILKGNE NGWFKITTDP VTNEGVLCVV
KPLDYEENRQ VTLEIGVNNE APFIKDVANR IPTMNRAMVT VHVKDQNEGP ECKPPEQYVR
IKENSAVGSK INGYKAYDPE TKNSNGLRYK KLQDPKDWVS IEEVSGLLTI SKTLDREIMA
PRNDMYNITV MAIDQEGKSC TGTLAVNIED VNDNAPEIIQ DYIVICKPKM GYTDISAVDP
DEPIHGPPFQ FNLANTSPEV NRIWTLNQVN DTAARLSYQK TADVQIYNVP VTVKDRAGQS
ATKILRVNLC DCTHPSQCPL RSRSAGITLG KWAILAILLG IALLFSVLLT LVCGVVTARK
GKHFPEDLAQ QNLIISNTEA PGDDRVCSAN GFTTHTANNS SQGFCGTMGS GMRNGGQETI
EMMKGHQTLD SCRVAGHHHT LDSGRGGHMD TDNCRYTYSE WHSFTQPRLG EKLHVCNQNE
DHIPSQDYVL TYNYEGRGSP AGSVGCCSEK QEEEGLDFLN NLEPKFLTLA ETCTKR
