ID   CADH3_PIG               Reviewed;         145 AA.
AC   O18926;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Cadherin-3;
DE   AltName: Full=Placental cadherin;
DE            Short=P-cadherin;
DE   Flags: Fragment;
GN   Name=CDH3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retinal pigment epithelium;
RA   Lutz D.A., Zheng J.J.;
RT   "Expression of multiple cadherins in adult retinal pigment epithelial (RPE)
RT   cells.";
RL   Submitted (NOV-1997) 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.
CC   -!- SUBUNIT: Interacts with CDCP1 and CTNNB1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {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; AF033826; AAB87087.1; -; mRNA.
DR   AlphaFoldDB; O18926; -.
DR   SMR; O18926; -.
DR   STRING; 9823.ENSSSCP00000021843; -.
DR   PaxDb; O18926; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_095003_0_0_1; -.
DR   InParanoid; O18926; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; O18926; SS.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; 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:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 1.
DR   SUPFAM; SSF49313; SSF49313; 1.
DR   PROSITE; PS00232; CADHERIN_1; 1.
DR   PROSITE; PS50268; CADHERIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Transmembrane.
FT   CHAIN           <1..>145
FT                   /note="Cadherin-3"
FT                   /id="PRO_0000126643"
FT   TOPO_DOM        <1..>145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..39
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          40..>145
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         145
SQ   SEQUENCE   145 AA;  15617 MW;  8AA2C49E76EB40EC CRC64;
     KIAKYELFGH AVSENGASVE EPMNISIIVT DQNDHKPKFT QDVFRGSVLE GVLPGTSVMQ
     VTATDEDDAI NTYNGVVAYS ILSQEPKDPH DLMFTVHRST GAISVISSGL DRERVPEYTL
     TIQATDMDGD GSSTTATAIV EILDA