DSC2_BOVIN
ID DSC2_BOVIN Reviewed; 863 AA.
AC P33545;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Desmocollin-2;
DE AltName: Full=Epithelial type 2 desmocollin;
DE Flags: Precursor; Fragment;
GN Name=DSC2;
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] (ISOFORMS 2A AND 2B).
RC TISSUE=Muzzle epithelium;
RX PubMed=1729705; DOI=10.1073/pnas.89.1.353;
RA Koch P.J., Goldschmidt M.D., Zimbelmann R., Troyanovsky R., Franke W.W.;
RT "Complexity and expression patterns of the desmosomal cadherins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:353-357(1992).
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=2A;
CC IsoId=P33545-1; Sequence=Displayed;
CC Name=2B;
CC IsoId=P33545-2; Sequence=VSP_000655, VSP_000656;
CC -!- TISSUE SPECIFICITY: Esophagus and rumen. Weakly in epithelia and
CC cardiac muscle.
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; M81190; AAA30782.1; -; mRNA.
DR EMBL; M81190; AAA30783.1; -; mRNA.
DR PIR; A41799; IJBODC.
DR PIR; B41799; IJBODD.
DR AlphaFoldDB; P33545; -.
DR SMR; P33545; -.
DR STRING; 9913.ENSBTAP00000011306; -.
DR PaxDb; P33545; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P33545; -.
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: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 Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT PROPEP 1..89
FT /evidence="ECO:0000255"
FT /id="PRO_0000003867"
FT CHAIN 90..863
FT /note="Desmocollin-2"
FT /id="PRO_0000003868"
FT TOPO_DOM 90..644
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 90..197
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 198..309
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 310..423
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 424..528
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 529..644
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02487"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 799..809
FT /note="KVQQCDQDNTH -> ESIRGHTLVKN (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:1729705"
FT /id="VSP_000655"
FT VAR_SEQ 810..863
FT /note="Missing (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:1729705"
FT /id="VSP_000656"
FT VARIANT 264
FT /note="K -> Q"
FT VARIANT 333
FT /note="R -> Q"
FT NON_TER 1
SQ SEQUENCE 863 AA; 95875 MW; 603854CCA16727F2 CRC64;
KFIGRVNLKE CFKSATLIHS SDPDFQILED GSVYTTHAIL LSSEKSSFTI LLSNTETQEE
KEILVLLEHQ TKVLKKRHSQ EKVLRRAKRR WAPIPCSVPE NSLGPFPLFL QQIQSDTAQN
YTIYYSISGP GVDKEPRNLF YVERDTGNLF CTASIDRETY PLFELVAFAT TPDGYTPEYP
LTLVIRIEDE NDNAPIFTET SYSFEVFENS KVGTTVGQVC ATDQDEPDTL HTRLKYSIIE
QFPALPTLFS MHPTTGVITT SSSKLDRELI DKYQLKIKVQ DMDGQYFGLQ TTAICIINIE
DVNDNLPTFT RSSYVASVEE NRIDVEILRV AVRDKDLINT ANWRANYTIL KGNEDGNFKI
VTDSQTNEGV LCVVKPLNYE EKQQVTLEIG VVNEAPYTGT SRSTTNMATV TVNVQNQDEG
PECDPRVQTV RIKENVPVGT KTIGYKAYDP ETGSSSGIRY KKSSDPEGWV DVDKNSGVIT
ILKRLDREAR SGVYNISIIA SDKDGRTCNG VLGIVLEDVN DNGPVIPQRT VVICKTVMSS
AEIVAVDPDE PIHGPPFDFS LEGVSDSEVL RMWRLTKVND TAARLSYLND LRFGKYTVPV
RVTDRLGQSL VTQLVVILCD CVTPNDCSFR PVSRTGNREV ILGKWAILAI LLGIALLFCI
LFTLVCGATT GADKKPKVFP DDLAQQNLIV SNTEAPGDDK VYSTNDFTTH AVGGSAHGIG
GTLGSRVKNG GQETIEMVKG GHQTMESCQE TGHDHTLERC KEGGQHTLDS CRGGPVATDN
CKYTYSEWYT YTQPRLGEKV QQCDQDNTHM QAQDYVLTYN YEGRGSAAGS VGCCSERQEE
DGLEFLDHLG PKFRTLAETC MKR
