ID   CAD20_RAT               Reviewed;         801 AA.
AC   Q5DWV1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Cadherin-20;
DE   Flags: Precursor;
GN   Name=Cdh20; Synonyms=Cad20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RA   Takahashi M., Osumi N.;
RT   "Expressions of rat cadherin-7 and 20 in the developing nervous system.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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; AB121033; BAD90596.1; -; mRNA.
DR   RefSeq; NP_001012766.1; NM_001012748.1.
DR   AlphaFoldDB; Q5DWV1; -.
DR   SMR; Q5DWV1; -.
DR   STRING; 10116.ENSRNOP00000019907; -.
DR   GlyGen; Q5DWV1; 4 sites.
DR   PaxDb; Q5DWV1; -.
DR   PRIDE; Q5DWV1; -.
DR   GeneID; 363948; -.
DR   KEGG; rno:363948; -.
DR   UCSC; RGD:1305438; rat.
DR   CTD; 28316; -.
DR   RGD; 1305438; Cdh20.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DWV1; -.
DR   PhylomeDB; Q5DWV1; -.
DR   PRO; PR:Q5DWV1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; 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; IPR039808; Cadherin.
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; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; SSF49313; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW   Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..59
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000320098"
FT   CHAIN           60..801
FT                   /note="Cadherin-20"
FT                   /id="PRO_0000320099"
FT   TOPO_DOM        60..619
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        620..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        641..801
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          61..165
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          166..274
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          275..389
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          390..494
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          494..610
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   801 AA;  89057 MW;  75622A6AC3F22062 CRC64;
     MWTTGRMSNA KSWLGLGTSL YFWALMDLAT TVLSSTPMPE VELDTLFSGK PQSHQRSRRS
     WVWNQFFVLE EYTGTDPLYV GKLHSDMDRG DGSIKYILSG EGAGIVFTID DTTGDIHAIQ
     RLDREERAQY TLRAQALDRR TGRPMEPESE FIIKIQDIND NEPKFLDGPY VATVPEMSPV
     GTSVIQVTAT DADDPTYGNS ARVVYSILQG QPYFSVDSKT GIIRTALMNM DREAKEYYEV
     IIQAKDMGGQ LGGLAGTTTV NITLSDVNDN PPRFPQKHYQ MSVLESAPVS STVGRVFAKD
     LDEGINAEMK YTIVDGDGAD AFDINTDPNF QVGIITVKKP LSFESKKSYT LKVEGSNPHV
     EMRFLNLGPF QDTTTVHIIV EDVDEPPVFE PRFYFVEVPE DVTIGTTIQI ISAKDPDMTN
     NSIRYSIDRG SDPGRFFYVD ITTGALMTAR PLDREEFSWH NITVLAMEMN NPSQVGSVAA
     TIKVLDVNDN APEFPRFYEA FICENAKAGQ LIQTVSAVDQ DDPHNGQHFY YSLAPEAANN
     PNFTVRDNQD NTARILTRRS GFRQQEQSVF YLPILIADSG QPVLSSTGTL TIQVCSCSDD
     GHVMSCSPEA YMLPVSLSRG ALIAILACVF VLLVLVLLIL SMRRHRKQPY IIDDDENIHE
     NIVRYDDEGG GEEDTEAFDI AAMWNPREAQ AGAAPKTRQD MLPEIESLSR YVPQTCAVSS
     TVHSYVLAKL YEADMDLWAP PFDSLQTYMF EGDGSVAGSL SSLQSATSDS EQSFDFLTDW
     GPRFRKLAEL YGASEGPSPL W