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   27-MAR-2024, entry version 182.
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};
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; 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.ENSMUSP00000153261; -.
DR   GlyCosmos; P55850; 4 sites, No reported glycans.
DR   GlyGen; P55850; 4 sites.
DR   iPTMnet; P55850; -.
DR   PhosphoSitePlus; P55850; -.
DR   CPTAC; non-CPTAC-4029; -.
DR   PaxDb; 10090-ENSMUSP00000111514; -.
DR   PeptideAtlas; P55850; -.
DR   ProteomicsDB; 275405; -. [P55850-1]
DR   ProteomicsDB; 275406; -. [P55850-2]
DR   Antibodypedia; 7988; 277 antibodies from 33 providers.
DR   DNASU; 13507; -.
DR   Ensembl; ENSMUST00000115848.5; ENSMUSP00000111514.5; ENSMUSG00000059898.10. [P55850-2]
DR   Ensembl; ENSMUST00000225110.2; ENSMUSP00000153261.2; ENSMUSG00000059898.10. [P55850-1]
DR   GeneID; 13507; -.
DR   KEGG; mmu:13507; -.
DR   UCSC; uc008eea.2; mouse.
DR   AGR; MGI:1194993; -.
DR   CTD; 1825; -.
DR   MGI; MGI:1194993; Dsc3.
DR   VEuPathDB; HostDB:ENSMUSG00000059898; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT01030000234624; -.
DR   InParanoid; P55850; -.
DR   OMA; ITMRAVD; -.
DR   OrthoDB; 4539697at2759; -.
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 78 CRISPR screens.
DR   PRO; PR:P55850; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P55850; Protein.
DR   Bgee; ENSMUSG00000059898; Expressed in tail skin and 105 other cell types or tissues.
DR   ExpressionAtlas; P55850; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
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: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   CDD; cd11304; Cadherin_repeat; 3.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24027:SF80; CADHERIN-13; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01818; DESMOCADHERN.
DR   PRINTS; PR01820; DESMOCOLLIN.
DR   SMART; SM00112; CA; 5.
DR   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 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
//