Full text data of DSC1
DSC1
(CDHF1)
[Confidence: low (only semi-automatic identification from reviews)]
Desmocollin-1 (Cadherin family member 1; Desmosomal glycoprotein 2/3; DG2/DG3; Flags: Precursor)
Desmocollin-1 (Cadherin family member 1; Desmosomal glycoprotein 2/3; DG2/DG3; Flags: Precursor)
UniProt
Q08554
ID DSC1_HUMAN Reviewed; 894 AA.
AC Q08554; Q9HB01;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Desmocollin-1;
DE AltName: Full=Cadherin family member 1;
DE AltName: Full=Desmosomal glycoprotein 2/3;
DE Short=DG2/DG3;
DE Flags: Precursor;
GN Name=DSC1; Synonyms=CDHF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND VARIANT PHE-848.
RC TISSUE=Foreskin;
RX PubMed=8507556;
RA Theis D.G., Koch P.J., Franke W.W.;
RT "Differential synthesis of type 1 and type 2 desmocollin mRNAs in
RT human stratified epithelia.";
RL Int. J. Dev. Biol. 37:101-110(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B).
RC TISSUE=Skin;
RX PubMed=8288219; DOI=10.1006/geno.1993.1453;
RA King I.A., Arnemann J., Spurr N.K., Buxton R.S.;
RT "Cloning of the cDNA (DSC1) coding for human type 1 desmocollin and
RT its assignment to chromosome 18.";
RL Genomics 18:185-194(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11027496; DOI=10.1006/bbrc.2000.3500;
RA Whittock N.V., Hunt D.M., Rickman L., Malhi S., Vogazianou A.P.,
RA Dawson L.F., Eady R.A.J., Buxton R.S., McGrath J.A.;
RT "Genomic organization and amplification of the human desmosomal
RT cadherin genes DSC1 and DSC3, encoding desmocollin types 1 and 3.";
RL Biochem. Biophys. Res. Commun. 276:454-460(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 135-151 AND 283-292.
RX PubMed=1713860; DOI=10.1016/0014-5793(91)80929-W;
RA King I.A., Magee A.I., Rees D.A., Buxton R.S.;
RT "Keratinization is associated with the expression of a new protein
RT related to the desmosomal cadherins DGII/III.";
RL FEBS Lett. 286:9-12(1991).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [7]
RP INTERACTION WITH JUP/PLAKOGLOBIN.
RX PubMed=19759396; DOI=10.1074/jbc.M109.047928;
RA Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
RT "Interactions of plakoglobin and beta-catenin with desmosomal
RT cadherins: basis of selective exclusion of alpha- and beta-catenin
RT from desmosomes.";
RL J. Biol. Chem. 284:31776-31788(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved
CC in the interaction of plaque proteins and intermediate filaments
CC mediating cell-cell adhesion. May contribute to epidermal cell
CC positioning (stratification) by mediating differential
CC adhesiveness between cells that express different isoforms. Linked
CC to the keratinization of epithelial tissues.
CC -!- SUBUNIT: Binds to JUP/plakoglobin.
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; Synonyms=DG2;
CC IsoId=Q08554-1; Sequence=Displayed;
CC Name=1B; Synonyms=DG3;
CC IsoId=Q08554-2; Sequence=VSP_000651, VSP_000652;
CC -!- TISSUE SPECIFICITY: Strongly expressed in epidermis, less in lymph
CC node and tongue.
CC -!- DOMAIN: Calcium may be bound by the cadherin-like repeats
CC (Potential).
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC each cadherin domain and rigidify the connections, imparting a
CC strong curvature to the full-length ectodomain (By similarity).
CC -!- SIMILARITY: Contains 5 cadherin domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z34522; CAA84279.1; -; mRNA.
DR EMBL; Z34522; CAA84278.1; -; mRNA.
DR EMBL; X72925; CAA51428.1; -; mRNA.
DR EMBL; X72925; CAA51429.1; -; mRNA.
DR EMBL; AF293358; AAG23424.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01252.1; -; Genomic_DNA.
DR PIR; A48910; A48910.
DR PIR; I37281; I37281.
DR PIR; I37282; I37282.
DR RefSeq; NP_004939.1; NM_004948.3.
DR RefSeq; NP_077739.1; NM_024421.2.
DR UniGene; Hs.567260; -.
DR ProteinModelPortal; Q08554; -.
DR SMR; Q08554; 136-667.
DR IntAct; Q08554; 5.
DR STRING; 9606.ENSP00000257198; -.
DR PhosphoSite; Q08554; -.
DR DMDM; 223590198; -.
DR PaxDb; Q08554; -.
DR PRIDE; Q08554; -.
DR DNASU; 1823; -.
DR Ensembl; ENST00000257197; ENSP00000257197; ENSG00000134765.
DR Ensembl; ENST00000257198; ENSP00000257198; ENSG00000134765.
DR GeneID; 1823; -.
DR KEGG; hsa:1823; -.
DR UCSC; uc002kwn.3; human.
DR CTD; 1823; -.
DR GeneCards; GC18M028732; -.
DR H-InvDB; HIX0039739; -.
DR HGNC; HGNC:3035; DSC1.
DR HPA; HPA012891; -.
DR MIM; 125643; gene.
DR neXtProt; NX_Q08554; -.
DR PharmGKB; PA27488; -.
DR eggNOG; NOG304955; -.
DR HOGENOM; HOG000231253; -.
DR HOVERGEN; HBG102801; -.
DR InParanoid; Q08554; -.
DR KO; K07600; -.
DR OMA; IKDRHGL; -.
DR OrthoDB; EOG74BJR7; -.
DR PhylomeDB; Q08554; -.
DR GeneWiki; DSC1; -.
DR GenomeRNAi; 1823; -.
DR NextBio; 7431; -.
DR PRO; PR:Q08554; -.
DR ArrayExpress; Q08554; -.
DR Bgee; Q08554; -.
DR CleanEx; HS_DSC1; -.
DR Genevestigator; Q08554; -.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; TAS:ProtInc.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.60; -; 6.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR009124; Cadherin/Desmocollin.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin_binding_dom.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR PANTHER; PTHR24025; PTHR24025; 1.
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 PRINTS; PR01820; DESMOCOLLIN.
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;
KW Cell membrane; Cleavage on pair of basic residues; Complete proteome;
KW Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT PROPEP 30 134 Potential.
FT /FTId=PRO_0000003863.
FT CHAIN 135 894 Desmocollin-1.
FT /FTId=PRO_0000003864.
FT TOPO_DOM 135 691 Extracellular (Potential).
FT TRANSMEM 692 714 Helical; (Potential).
FT TOPO_DOM 715 894 Cytoplasmic (Potential).
FT DOMAIN 135 242 Cadherin 1.
FT DOMAIN 243 354 Cadherin 2.
FT DOMAIN 355 471 Cadherin 3.
FT DOMAIN 472 575 Cadherin 4.
FT DOMAIN 576 682 Cadherin 5.
FT MOD_RES 385 385 Phosphothreonine.
FT CARBOHYD 165 165 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 546 546 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 830 840 KVYLCGQDEEH -> ESIRGHTLIKN (in isoform
FT 1B).
FT /FTId=VSP_000651.
FT VAR_SEQ 841 894 Missing (in isoform 1B).
FT /FTId=VSP_000652.
FT VARIANT 93 93 S -> F (in dbSNP:rs35338395).
FT /FTId=VAR_061059.
FT VARIANT 460 460 V -> I (in dbSNP:rs17800159).
FT /FTId=VAR_055579.
FT VARIANT 848 848 C -> F (in dbSNP:rs985861).
FT /FTId=VAR_055580.
FT CONFLICT 132 132 S -> T (in Ref. 1; CAA84278/CAA84279).
SQ SEQUENCE 894 AA; 99987 MW; 2E0C835F6FE2E77F CRC64;
MALASAAPGS IFCKQLLFSL LVLTLLCDAC QKVYLRVPSH LQAETLVGKV NLEECLKSAS
LIRSSDPAFR ILEDGSIYTT HDLILSSERK SFSIFLSDGQ RREQQEIKVV LSARENKSPK
KRHTKDTALK RSKRRWAPIP ASLMENSLGP FPQHVQQIQS DAAQNYTIFY SISGPGVDKE
PFNLFYIEKD TGDIFCTRSI DREKYEQFAL YGYATTADGY APEYPLPLII KIEDDNDNAP
YFEHRVTIFT VPENCRSGTS VGKVTATDLD EPDTLHTRLK YKILQQIPDH PKHFSIHPDT
GVITTTTPFL DREKCDTYQL IMEVRDMGGQ PFGLFNTGTI TISLEDENDN PPSFTETSYV
TEVEENRIDV EILRMKVQDQ DLPNTPHSKA VYKILQGNEN GNFIISTDPN TNEGVLCVVK
PLNYEVNRQV ILQVGVINEA QFSKAASSQT PTMCTTTVTV KIIDSDEGPE CHPPVKVIQS
QDGFPAGQEL LGYKALDPEI SSGEGLRYQK LGDEDNWFEI NQHTGDLRTL KVLDRESKFV
KNNQYNISVV AVDAVGRSCT GTLVVHLDDY NDHAPQIDKE VTICQNNEDF AVLKPVDPDG
PENGPPFQFF LDNSASKNWN IEEKDGKTAI LRQRQNLDYN YYSVPIQIKD RHGLVATHML
TVRVCDCSTP SECRMKDKST RDVRPNVILG RWAILAMVLG SVLLLCILFT CFCVTAKRTV
KKCFPEDIAQ QNLIVSNTEG PGEEVTEANI RLPMQTSNIC DTSMSVGTVG GQGIKTQQSF
EMVKGGYTLD SNKGGGHQTL ESVKGVGQGD TGRYAYTDWQ SFTQPRLGEK VYLCGQDEEH
KHCEDYVCSY NYEGKGSLAG SVGCCSDRQE EEGLEFLDHL EPKFRTLAKT CIKK
//
ID DSC1_HUMAN Reviewed; 894 AA.
AC Q08554; Q9HB01;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-FEB-2009, sequence version 2.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=Desmocollin-1;
DE AltName: Full=Cadherin family member 1;
DE AltName: Full=Desmosomal glycoprotein 2/3;
DE Short=DG2/DG3;
DE Flags: Precursor;
GN Name=DSC1; Synonyms=CDHF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND VARIANT PHE-848.
RC TISSUE=Foreskin;
RX PubMed=8507556;
RA Theis D.G., Koch P.J., Franke W.W.;
RT "Differential synthesis of type 1 and type 2 desmocollin mRNAs in
RT human stratified epithelia.";
RL Int. J. Dev. Biol. 37:101-110(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B).
RC TISSUE=Skin;
RX PubMed=8288219; DOI=10.1006/geno.1993.1453;
RA King I.A., Arnemann J., Spurr N.K., Buxton R.S.;
RT "Cloning of the cDNA (DSC1) coding for human type 1 desmocollin and
RT its assignment to chromosome 18.";
RL Genomics 18:185-194(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11027496; DOI=10.1006/bbrc.2000.3500;
RA Whittock N.V., Hunt D.M., Rickman L., Malhi S., Vogazianou A.P.,
RA Dawson L.F., Eady R.A.J., Buxton R.S., McGrath J.A.;
RT "Genomic organization and amplification of the human desmosomal
RT cadherin genes DSC1 and DSC3, encoding desmocollin types 1 and 3.";
RL Biochem. Biophys. Res. Commun. 276:454-460(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 135-151 AND 283-292.
RX PubMed=1713860; DOI=10.1016/0014-5793(91)80929-W;
RA King I.A., Magee A.I., Rees D.A., Buxton R.S.;
RT "Keratinization is associated with the expression of a new protein
RT related to the desmosomal cadherins DGII/III.";
RL FEBS Lett. 286:9-12(1991).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385, AND MASS
RP SPECTROMETRY.
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [7]
RP INTERACTION WITH JUP/PLAKOGLOBIN.
RX PubMed=19759396; DOI=10.1074/jbc.M109.047928;
RA Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
RT "Interactions of plakoglobin and beta-catenin with desmosomal
RT cadherins: basis of selective exclusion of alpha- and beta-catenin
RT from desmosomes.";
RL J. Biol. Chem. 284:31776-31788(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved
CC in the interaction of plaque proteins and intermediate filaments
CC mediating cell-cell adhesion. May contribute to epidermal cell
CC positioning (stratification) by mediating differential
CC adhesiveness between cells that express different isoforms. Linked
CC to the keratinization of epithelial tissues.
CC -!- SUBUNIT: Binds to JUP/plakoglobin.
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; Synonyms=DG2;
CC IsoId=Q08554-1; Sequence=Displayed;
CC Name=1B; Synonyms=DG3;
CC IsoId=Q08554-2; Sequence=VSP_000651, VSP_000652;
CC -!- TISSUE SPECIFICITY: Strongly expressed in epidermis, less in lymph
CC node and tongue.
CC -!- DOMAIN: Calcium may be bound by the cadherin-like repeats
CC (Potential).
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC each cadherin domain and rigidify the connections, imparting a
CC strong curvature to the full-length ectodomain (By similarity).
CC -!- SIMILARITY: Contains 5 cadherin domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z34522; CAA84279.1; -; mRNA.
DR EMBL; Z34522; CAA84278.1; -; mRNA.
DR EMBL; X72925; CAA51428.1; -; mRNA.
DR EMBL; X72925; CAA51429.1; -; mRNA.
DR EMBL; AF293358; AAG23424.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01252.1; -; Genomic_DNA.
DR PIR; A48910; A48910.
DR PIR; I37281; I37281.
DR PIR; I37282; I37282.
DR RefSeq; NP_004939.1; NM_004948.3.
DR RefSeq; NP_077739.1; NM_024421.2.
DR UniGene; Hs.567260; -.
DR ProteinModelPortal; Q08554; -.
DR SMR; Q08554; 136-667.
DR IntAct; Q08554; 5.
DR STRING; 9606.ENSP00000257198; -.
DR PhosphoSite; Q08554; -.
DR DMDM; 223590198; -.
DR PaxDb; Q08554; -.
DR PRIDE; Q08554; -.
DR DNASU; 1823; -.
DR Ensembl; ENST00000257197; ENSP00000257197; ENSG00000134765.
DR Ensembl; ENST00000257198; ENSP00000257198; ENSG00000134765.
DR GeneID; 1823; -.
DR KEGG; hsa:1823; -.
DR UCSC; uc002kwn.3; human.
DR CTD; 1823; -.
DR GeneCards; GC18M028732; -.
DR H-InvDB; HIX0039739; -.
DR HGNC; HGNC:3035; DSC1.
DR HPA; HPA012891; -.
DR MIM; 125643; gene.
DR neXtProt; NX_Q08554; -.
DR PharmGKB; PA27488; -.
DR eggNOG; NOG304955; -.
DR HOGENOM; HOG000231253; -.
DR HOVERGEN; HBG102801; -.
DR InParanoid; Q08554; -.
DR KO; K07600; -.
DR OMA; IKDRHGL; -.
DR OrthoDB; EOG74BJR7; -.
DR PhylomeDB; Q08554; -.
DR GeneWiki; DSC1; -.
DR GenomeRNAi; 1823; -.
DR NextBio; 7431; -.
DR PRO; PR:Q08554; -.
DR ArrayExpress; Q08554; -.
DR Bgee; Q08554; -.
DR CleanEx; HS_DSC1; -.
DR Genevestigator; Q08554; -.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; TAS:ProtInc.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.60; -; 6.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR009124; Cadherin/Desmocollin.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin_binding_dom.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR PANTHER; PTHR24025; PTHR24025; 1.
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 PRINTS; PR01820; DESMOCOLLIN.
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;
KW Cell membrane; Cleavage on pair of basic residues; Complete proteome;
KW Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT PROPEP 30 134 Potential.
FT /FTId=PRO_0000003863.
FT CHAIN 135 894 Desmocollin-1.
FT /FTId=PRO_0000003864.
FT TOPO_DOM 135 691 Extracellular (Potential).
FT TRANSMEM 692 714 Helical; (Potential).
FT TOPO_DOM 715 894 Cytoplasmic (Potential).
FT DOMAIN 135 242 Cadherin 1.
FT DOMAIN 243 354 Cadherin 2.
FT DOMAIN 355 471 Cadherin 3.
FT DOMAIN 472 575 Cadherin 4.
FT DOMAIN 576 682 Cadherin 5.
FT MOD_RES 385 385 Phosphothreonine.
FT CARBOHYD 165 165 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 546 546 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 830 840 KVYLCGQDEEH -> ESIRGHTLIKN (in isoform
FT 1B).
FT /FTId=VSP_000651.
FT VAR_SEQ 841 894 Missing (in isoform 1B).
FT /FTId=VSP_000652.
FT VARIANT 93 93 S -> F (in dbSNP:rs35338395).
FT /FTId=VAR_061059.
FT VARIANT 460 460 V -> I (in dbSNP:rs17800159).
FT /FTId=VAR_055579.
FT VARIANT 848 848 C -> F (in dbSNP:rs985861).
FT /FTId=VAR_055580.
FT CONFLICT 132 132 S -> T (in Ref. 1; CAA84278/CAA84279).
SQ SEQUENCE 894 AA; 99987 MW; 2E0C835F6FE2E77F CRC64;
MALASAAPGS IFCKQLLFSL LVLTLLCDAC QKVYLRVPSH LQAETLVGKV NLEECLKSAS
LIRSSDPAFR ILEDGSIYTT HDLILSSERK SFSIFLSDGQ RREQQEIKVV LSARENKSPK
KRHTKDTALK RSKRRWAPIP ASLMENSLGP FPQHVQQIQS DAAQNYTIFY SISGPGVDKE
PFNLFYIEKD TGDIFCTRSI DREKYEQFAL YGYATTADGY APEYPLPLII KIEDDNDNAP
YFEHRVTIFT VPENCRSGTS VGKVTATDLD EPDTLHTRLK YKILQQIPDH PKHFSIHPDT
GVITTTTPFL DREKCDTYQL IMEVRDMGGQ PFGLFNTGTI TISLEDENDN PPSFTETSYV
TEVEENRIDV EILRMKVQDQ DLPNTPHSKA VYKILQGNEN GNFIISTDPN TNEGVLCVVK
PLNYEVNRQV ILQVGVINEA QFSKAASSQT PTMCTTTVTV KIIDSDEGPE CHPPVKVIQS
QDGFPAGQEL LGYKALDPEI SSGEGLRYQK LGDEDNWFEI NQHTGDLRTL KVLDRESKFV
KNNQYNISVV AVDAVGRSCT GTLVVHLDDY NDHAPQIDKE VTICQNNEDF AVLKPVDPDG
PENGPPFQFF LDNSASKNWN IEEKDGKTAI LRQRQNLDYN YYSVPIQIKD RHGLVATHML
TVRVCDCSTP SECRMKDKST RDVRPNVILG RWAILAMVLG SVLLLCILFT CFCVTAKRTV
KKCFPEDIAQ QNLIVSNTEG PGEEVTEANI RLPMQTSNIC DTSMSVGTVG GQGIKTQQSF
EMVKGGYTLD SNKGGGHQTL ESVKGVGQGD TGRYAYTDWQ SFTQPRLGEK VYLCGQDEEH
KHCEDYVCSY NYEGKGSLAG SVGCCSDRQE EEGLEFLDHL EPKFRTLAKT CIKK
//
MIM
125643
*RECORD*
*FIELD* NO
125643
*FIELD* TI
*125643 DESMOCOLLIN 1; DSC1
*FIELD* TX
DESCRIPTION
The desmosome is a complex adhesive structure that plays a fundamental
read morerole in maintaining the strength and integrity of epithelial tissues.
Central to this role are transmembrane glycoproteins that mediate
cell-cell adhesion at the extracellular surface and interact with the
cytoskeleton (via components of the desmosomal plaque), thus linking the
intermediate filament networks of adjacent cells. Desmosomal
glycoproteins comprise 2 distinct groups, the desmogleins and the
desmocollins, both of which are members of the cadherin superfamily of
Ca(2+)-dependent cell adhesion molecules (summary by King et al., 1993).
CLONING
Using specific antibodies against the components of desmosomes, Cowin et
al. (1984) identified 2 glycoproteins bound to the cell surface. The
glycoproteins of 115 kD and 100 kD were named desmocollins to denote
that they are involved in the adhesive function of the desmosomes.
King et al. (1993) isolated a human DSC1 cDNA clone encoding
alternatively spliced desmocollin proteins of 760 (variant a) and 706
(variant b) residues. DSC1 shares 53% amino acid sequence identity with
the previously isolated type 3 desmocollin (DSC3; 600271); the N and C
termini of the mature proteins are more highly conserved. DSC1 is
expressed in the more differentiated layers of the epidermis, whereas
DSC3 is expressed in the basal layers of the epidermis.
Troyanovsky et al. (1993) stated that both DSC1 and DSC2 (125645) in the
human occur in 2 alternatively spliced forms (variants a and b) that
have different cytoplasmic domains reflecting different interactions
with components of the desmosomal plaque.
MAPPING
Using a panel of somatic cell hybrids, King et al. (1993) assigned the
DSC1 gene to chromosome 18, where the DSC2 gene and the 3 desmoglein
genes (DSG1, 125670; DSG2, 125671; DSG3, 169615) had previously been
mapped.
*FIELD* RF
1. Cowin, P.; Mattey, D.; Garrod, D.: Identification of desmosomal
surface components (desmocollins) and inhibition of desmosome formation
by specific FAB-prime. J. Cell Sci. 70: 41-60, 1984.
2. King, I. A.; Arnemann, J.; Spurr, N. K.; Buxton, R. S.: Cloning
of the cDNA (DSC1) coding for human type 1 desmocollin and its assignment
to chromosome 18. Genomics 18: 185-194, 1993.
3. Troyanovsky, S. M.; Eshkind, L. G.; Troyanovsky, R. B.; Leube,
R. E.; Franke, W. W.: Contributions of cytoplasmic domains of desmosomal
cadherins to desmosome assembly and intermediate filament anchorage. Cell 72:
561-574, 1993.
*FIELD* CD
Victor A. McKusick: 11/29/1993
*FIELD* ED
terry: 01/19/2010
carol: 1/7/2010
alopez: 8/25/1998
dkim: 6/30/1998
carol: 12/22/1993
carol: 11/29/1993
*RECORD*
*FIELD* NO
125643
*FIELD* TI
*125643 DESMOCOLLIN 1; DSC1
*FIELD* TX
DESCRIPTION
The desmosome is a complex adhesive structure that plays a fundamental
read morerole in maintaining the strength and integrity of epithelial tissues.
Central to this role are transmembrane glycoproteins that mediate
cell-cell adhesion at the extracellular surface and interact with the
cytoskeleton (via components of the desmosomal plaque), thus linking the
intermediate filament networks of adjacent cells. Desmosomal
glycoproteins comprise 2 distinct groups, the desmogleins and the
desmocollins, both of which are members of the cadherin superfamily of
Ca(2+)-dependent cell adhesion molecules (summary by King et al., 1993).
CLONING
Using specific antibodies against the components of desmosomes, Cowin et
al. (1984) identified 2 glycoproteins bound to the cell surface. The
glycoproteins of 115 kD and 100 kD were named desmocollins to denote
that they are involved in the adhesive function of the desmosomes.
King et al. (1993) isolated a human DSC1 cDNA clone encoding
alternatively spliced desmocollin proteins of 760 (variant a) and 706
(variant b) residues. DSC1 shares 53% amino acid sequence identity with
the previously isolated type 3 desmocollin (DSC3; 600271); the N and C
termini of the mature proteins are more highly conserved. DSC1 is
expressed in the more differentiated layers of the epidermis, whereas
DSC3 is expressed in the basal layers of the epidermis.
Troyanovsky et al. (1993) stated that both DSC1 and DSC2 (125645) in the
human occur in 2 alternatively spliced forms (variants a and b) that
have different cytoplasmic domains reflecting different interactions
with components of the desmosomal plaque.
MAPPING
Using a panel of somatic cell hybrids, King et al. (1993) assigned the
DSC1 gene to chromosome 18, where the DSC2 gene and the 3 desmoglein
genes (DSG1, 125670; DSG2, 125671; DSG3, 169615) had previously been
mapped.
*FIELD* RF
1. Cowin, P.; Mattey, D.; Garrod, D.: Identification of desmosomal
surface components (desmocollins) and inhibition of desmosome formation
by specific FAB-prime. J. Cell Sci. 70: 41-60, 1984.
2. King, I. A.; Arnemann, J.; Spurr, N. K.; Buxton, R. S.: Cloning
of the cDNA (DSC1) coding for human type 1 desmocollin and its assignment
to chromosome 18. Genomics 18: 185-194, 1993.
3. Troyanovsky, S. M.; Eshkind, L. G.; Troyanovsky, R. B.; Leube,
R. E.; Franke, W. W.: Contributions of cytoplasmic domains of desmosomal
cadherins to desmosome assembly and intermediate filament anchorage. Cell 72:
561-574, 1993.
*FIELD* CD
Victor A. McKusick: 11/29/1993
*FIELD* ED
terry: 01/19/2010
carol: 1/7/2010
alopez: 8/25/1998
dkim: 6/30/1998
carol: 12/22/1993
carol: 11/29/1993