ID   CADH3_BOVIN             Reviewed;         491 AA.
AC   P19535;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Cadherin-3;
DE   AltName: Full=Placental cadherin;
DE            Short=P-cadherin;
DE   Flags: Fragment;
GN   Name=CDH3; Synonyms=CDHP;
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=2390969; DOI=10.1002/j.1460-2075.1990.tb07456.x;
RA   Liaw C.W., Cannon C., Power M.D., Kiboneka P.K., Rubin L.L.;
RT   "Identification and cloning of two species of cadherins in bovine
RT   endothelial cells.";
RL   EMBO J. 9:2701-2708(1990).
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; Single-pass type I membrane
CC       protein.
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; X53614; CAA37676.1; -; mRNA.
DR   PIR; S11694; IJBOCP.
DR   RefSeq; NP_001231534.1; NM_001244605.1.
DR   AlphaFoldDB; P19535; -.
DR   SMR; P19535; -.
DR   STRING; 9913.ENSBTAP00000042970; -.
DR   PaxDb; P19535; -.
DR   GeneID; 281063; -.
DR   KEGG; bta:281063; -.
DR   CTD; 1001; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   HOGENOM; CLU_005284_2_1_1; -.
DR   InParanoid; P19535; -.
DR   OrthoDB; 182239at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   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; 2.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; SSF49313; 3.
DR   PROSITE; PS00232; CADHERIN_1; 1.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..491
FT                   /note="Cadherin-3"
FT                   /id="PRO_0000126642"
FT   TOPO_DOM        <1..316
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..491
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..102
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          103..208
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          209..314
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   491 AA;  54208 MW;  6BEB0AE5918C4771 CRC64;
     ENTVSHEVQR LTVTDLDAPN SPAWRATYRI VGGDNGDHFT ITTDPESNQG ILTTQKGLDF
     EAKTQHTLYV EVINEVPFVV KLPTSTATVV VLVEDVNEPP VFVPPSKVIE IQEGISTGEP
     ICAYTARDPD KGSQKISYHI LRDPAGWLAM DPDSGQVTAA GVLDREDEQF VRNNIYEVMV
     LATDDGSPPT TGTGTLLLTL MDINDHGPVP EPRQITICNQ SPVPQVLNIT DKDLSPHTAP
     FQAQLTHDSD VYWTAEVNEK GDAVALSLKK FLKQGEYDVH LSLSDHGNKE QLTVIRATVC
     DCHGNMVTCR DPWTWGFLLP ILGAALALLL LLLVLLFLVR KKRKIKEPLL LPEDDTRDNV
     FYYGEEGGGE EDQDYDITQL HRGLEARPEV VLRNDVAPSF IPTPMYRPRP ANPDEIGNFI
     IENLKAANTD PTAPPYDSLL VFDYEGSGSD AASLSSLTSS TSDQDQDYNY LNEWGSRFKK
     LADMYGGGQD D