DSC1_BOVIN
ID DSC1_BOVIN Reviewed; 893 AA.
AC Q01107; Q28095;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Desmocollin-1;
DE AltName: Full=Desmosomal glycoprotein 2/3;
DE Short=DG2/DG3;
DE Flags: Precursor;
GN Name=DSC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1B), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Epidermis;
RX PubMed=2010468; DOI=10.1083/jcb.113.2.381;
RA Collins J.E., Legan P.K., Kenny T.P., Macgarvie J., Holton J.L.,
RA Garrod D.R.;
RT "Cloning and sequence analysis of desmosomal glycoproteins 2 and 3
RT (desmocollins): cadherin-like desmosomal adhesion molecules with
RT heterogeneous cytoplasmic domains.";
RL J. Cell Biol. 113:381-391(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1B), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2034686; DOI=10.1073/pnas.88.10.4476;
RA Mechanic S., Raynor K., Hill J.E., Cowin P.;
RT "Desmocollins form a distinct subset of the cadherin family of cell
RT adhesion molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4476-4480(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 133-893 (ISOFORM 1A), AND PROTEIN SEQUENCE OF
RP 296-308; 340-351; 493-507 AND 610-618.
RC TISSUE=Muzzle epithelium;
RX PubMed=1916068; DOI=10.1111/j.1432-0436.1991.tb00218.x;
RA Koch P.J., Goldschmidt M.D., Walsh M.J., Zimbelmann R., Schmelz M.,
RA Franke W.W.;
RT "Amino acid sequence of bovine muzzle epithelial desmocollin derived from
RT cloned cDNA: a novel subtype of desmosomal cadherins.";
RL Differentiation 47:29-36(1991).
RN [4]
RP PROTEIN SEQUENCE OF 133-155.
RX PubMed=2277091; DOI=10.1242/jcs.97.2.239;
RA Holton J.L., Kenny T.P., Legan P.K., Collins J.E., Keen J.N., Sharma R.,
RA Garrod D.R.;
RT "Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity
RT to calcium-dependent cell-cell adhesion molecules.";
RL J. Cell Sci. 97:239-246(1990).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=2120245; DOI=10.1242/jcs.96.2.239;
RA Parrish E.P., Marston J.E., Mattey D.L., Measures H.R., Venning R.,
RA Garrod D.R.;
RT "Size heterogeneity, phosphorylation and transmembrane organisation of
RT desmosomal glycoproteins 2 and 3 (desmocollins) in MDCK cells.";
RL J. Cell Sci. 96:239-248(1990).
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; Synonyms=DG2;
CC IsoId=Q01107-1; Sequence=Displayed;
CC Name=1B; Synonyms=DG3;
CC IsoId=Q01107-2; Sequence=VSP_000649, VSP_000650;
CC -!- TISSUE SPECIFICITY: Epidermis and weakly in tongue papillae.
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 -!- PTM: Isoform 1A is phosphorylated on a serine but isoform 1B is not.
CC {ECO:0000269|PubMed:2120245}.
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DR EMBL; X56966; CAA40286.1; -; mRNA.
DR EMBL; X56967; CAA40287.1; -; mRNA.
DR EMBL; X56968; CAA40289.1; -; Genomic_DNA.
DR EMBL; X56968; CAA40288.1; -; Genomic_DNA.
DR EMBL; M67489; AAA30492.1; -; mRNA.
DR EMBL; X58029; CAA41088.1; -; mRNA.
DR PIR; A43838; IJBODE.
DR PIR; B38456; IJBODF.
DR RefSeq; NP_776469.1; NM_174044.1. [Q01107-2]
DR AlphaFoldDB; Q01107; -.
DR SMR; Q01107; -.
DR STRING; 9913.ENSBTAP00000026482; -.
DR PaxDb; Q01107; -.
DR PeptideAtlas; Q01107; -.
DR PRIDE; Q01107; -.
DR GeneID; 281127; -.
DR KEGG; bta:281127; -.
DR CTD; 1823; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q01107; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:AgBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:AgBase.
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; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
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; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT PROPEP 30..132
FT /evidence="ECO:0000269|PubMed:2277091"
FT /id="PRO_0000003861"
FT CHAIN 133..893
FT /note="Desmocollin-1"
FT /id="PRO_0000003862"
FT TOPO_DOM 133..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..893
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 133..240
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 241..352
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..470
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 471..574
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 575..682
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08554"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 829..839
FT /note="KVYLCGQDEEH -> ESIRGHTLVKN (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:2034686"
FT /id="VSP_000649"
FT VAR_SEQ 840..893
FT /note="Missing (in isoform 1B)"
FT /evidence="ECO:0000303|PubMed:2034686"
FT /id="VSP_000650"
FT VARIANT 519
FT /note="I -> F"
FT VARIANT 788
FT /note="Y -> C"
FT CONFLICT 485
FT /note="T -> A (in Ref. 2; AAA30492 and 3; CAA41088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 99648 MW; A45A4D8B30951FC9 CRC64;
MAVASAAPGS IFWKQLLFSL LVLILFCDAC QKISLQVPSH LRAEALVGKV NLKECLQSAS
LILSSDPDFR ILEDGSIYTT HDLVLSSGKS FSILLSDSQG QGQKEIEIIL EAGGKKVPKR
HMKDAVLRRT KRRWAPIPCS LMENSLGPFP QHVQQVQSDA AQNYTIFYSI SGPGVDKEPF
NLFFIEKDTG DIFCTRSIDR EQYQEFPIYA YATTADGYAP EYPLPLVFKV EDDNDNAPYF
ENKLTVFTVP ENCRTGTSVG KVTAIDLDEP DTLHTRLKYK ILQQIPNNPR HFTVHPDTGV
ITTTTPLLDR EKCDTYKLIM EVRDMGGQPF GLFNTGTITI SLEDENDNAP YFTETSYTVE
VEENRIDVEI LRMAVHDHDL PNTPHSRAVY QILQGNENGT FKISTDPNTN EAVLCVVKPL
NYEVNRQVVL QIGVLNEAQF AKAVNSKTTT TMCTTVVTVK VKDHDEGPEC QPPVKVIQSE
DCLPTGTELL GYKAVDPERG TGEGLRYKKI QDEDNWFEIN EYTGDLKTVK VLDRESTFVK
NNQYNVSVIA FDADGRSCTG TLVVFLEDKN DHPPQIKQEE LTICRHDKDY VVLEPTDQDG
PDNGPPFQFI LDNSASKLWT VETRDGKTAI LRGRQDLDYD YYTVPIQIKD RHGASATHIL
PVRVCDCTIP SECRMPSKLS REAALANVFL GKWAILAMVL GSVLLLCILF TCFCVTVKKT
VKKCFPEDVA QQNLIVSNTE GPGEEVMDAN IRLPTQTSNV CDTSISVGTL GGQGVKTQQS
FEMVKGGYTL DANKGGGHQT LESVKGVTDT GRYTYSDWHN FTQPRLGEKV YLCGQDEEHK
LCEDYVRSYS YEGKGSVAGS VGCCSDRQEE EGLDFLDHLE PKFRTLAKTC VKK
