DSC3_BOVIN
ID DSC3_BOVIN Reviewed; 896 AA.
AC Q28060; Q28061; Q28176;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Desmocollin-3;
DE Flags: Precursor;
GN Name=DSC3;
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 [MRNA].
RX PubMed=7673337; DOI=10.1242/jcs.108.6.2163;
RA Yue K.K.M., Holton J.L., Clarke J.P., Hyam J.L.M., Hashimoto T.,
RA Chidgey M.A.J., Garrod D.R.;
RT "Characterisation of a desmocollin isoform (bovine DSC3) exclusively
RT expressed in lower layers of stratified epithelia.";
RL J. Cell Sci. 108:2163-2173(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 686-814.
RC TISSUE=Epidermis;
RX PubMed=8034749; DOI=10.1083/jcb.126.2.507;
RA Legan P.K., Yue K.K.M., Chidgey M.A.J., Holton J.L., Wilkinson R.W.,
RA Garrod D.R.;
RT "The bovine desmocollin family: a new gene and expression patterns
RT reflecting epithelial cell proliferation and differentiation.";
RL J. Cell Biol. 126:507-518(1994).
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=3A;
CC IsoId=Q28060-1; Sequence=Displayed;
CC Name=3B;
CC IsoId=Q28060-2; Sequence=VSP_000661, VSP_000662;
CC -!- TISSUE SPECIFICITY: Stratified epithelia only (epidermis, tongue,
CC esophagus and rumen).
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; L33774; AAC41625.1; -; mRNA.
DR EMBL; L33774; AAC41626.1; -; mRNA.
DR EMBL; X75783; CAA53427.1; -; mRNA.
DR PIR; I45858; I45858.
DR PIR; S38589; S38589.
DR AlphaFoldDB; Q28060; -.
DR SMR; Q28060; -.
DR STRING; 9913.ENSBTAP00000020274; -.
DR PaxDb; Q28060; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q28060; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0045295; F:gamma-catenin binding; IBA:GO_Central.
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 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 2: Evidence at transcript 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..26
FT /evidence="ECO:0000255"
FT PROPEP 27..134
FT /evidence="ECO:0000255"
FT /id="PRO_0000003873"
FT CHAIN 135..896
FT /note="Desmocollin-3"
FT /id="PRO_0000003874"
FT TOPO_DOM 135..690
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..242
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..354
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 355..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..690
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
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 832..839
FT /note="KLHLCNQD -> ESIRGHTG (in isoform 3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000661"
FT VAR_SEQ 840..896
FT /note="Missing (in isoform 3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_000662"
FT CONFLICT 686..687
FT /note="VI -> EF (in Ref. 2; CAA53427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 99687 MW; 8CC0C30A63FB0BD4 CRC64;
MAAPGSGAPC AELCRQLLLT LVVFSFACEA CKKEIFNIPS KLEADKMIGR VNLKECLGSV
DRIQSSDPDF RVLEDGSVYT AHAVVLSDEK RSFTIWLSDT EKRTQKEILV LLEYQKKVLK
KRHTKETVLR RSKRRWAPIP CSMQENSLGP FPLFLQQVQS DAAQNYTIFY SISGRGVDKE
PLNLFFIERD TGNLYCTQPV DREEYDVFDL IAYASTADGY SADFPLPLPI RVEDENDNHP
IFTEAVYNFE VPESSRVGTT VGVVCATDRD EPDTMHTRLK YSILEQTPRS PGLFSVHPST
GVITTVSHYL DREVADKYSL IMKVQDMDGQ FFGLMSTATC IITVKDSNDN LPTFRQNAYE
ASVEENTVNV EILRIPVEDK DLINTANWRA NFTILKGNEN GHFKITTDKA TNEGVLSVVK
PLDYEESHQV VLEIGVANEA PFTRDVALRM TTMNRAVVTV HVKDQDEGPE CSPEVQYIRI
KENSAVGSKI SGYKAYDPET KSSSGLRYKI LHDPKEWITV NEGSGSLETY KTLDREVITP
KNDLYNITVL AIDQDGRSCT GTLAVSIEDV NDNPPEILQD YLVICKGNMD YVDISAIDHD
SSINGAPFYF SLANTSPEIN RLWTITRVND TAARLAYQKN AQFQEYFIPV AVKDRAGLSA
TKTLRVNLCD CTNPVQCRAA RRSADVILGK WAILAILLGI ALLFSILLTL VCGIVSARNK
KAFPDDLAQQ NLIISNTEAP GDDKVCSANG FMTQTVNNAN QGFCGTMGSG VKNGGQESIE
MVKGGQQTLE SCRGAGHHHT LDSCRGGTIE VENSRYTYSE WQNFTQPRLG EKLHLCNQDE
EHMPSQDYVL TYNYEGRGSP AGSVGCCSEK QEEDGLDFLN NLEAKFAALA KTCTKR
