CADH1_CHICK
ID CADH1_CHICK Reviewed; 887 AA.
AC P08641;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cadherin-1;
DE AltName: Full=Epithelial cadherin;
DE Short=E-cadherin;
DE AltName: Full=Liver cell adhesion molecule;
DE Short=L-CAM;
DE Flags: Precursor;
GN Name=CDH1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=3174655; DOI=10.1073/pnas.85.20.7617;
RA Sorkin B.C., Hemperly J.J., Edelman G.M., Cunningham B.A.;
RT "Structure of the gene for the liver cell adhesion molecule, L-CAM.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7617-7621(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-887, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3472238; DOI=10.1073/pnas.84.9.2808;
RA Gallin W.J., Sorkin B.C., Edelman G.M., Cunningham B.A.;
RT "Sequence analysis of a cDNA clone encoding the liver cell adhesion
RT molecule, L-CAM.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2808-2812(1987).
RN [3]
RP INTERACTION WITH CTNNA2.
RC TISSUE=Embryonic brain;
RX PubMed=1638632; DOI=10.1016/0092-8674(92)90103-j;
RA Hirano S., Kimoto N., Shimoyama Y., Hirohashi S., Takeichi M.;
RT "Identification of a neural alpha-catenin as a key regulator of cadherin
RT function and multicellular organization.";
RL Cell 70:293-301(1992).
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. E-cadherin is a ligand for integrin alpha-
CC E/beta-7.
CC -!- SUBUNIT: Homodimer. Interacts with CTNNA2.
CC {ECO:0000269|PubMed:1638632}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Non-neural epithelial tissues.
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; M22190; AAA82572.1; -; Genomic_DNA.
DR EMBL; M22180; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22181; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22182; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22186; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22183; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22194; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22184; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22185; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22189; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22193; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22187; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22192; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22191; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M22195; AAA82572.1; JOINED; Genomic_DNA.
DR EMBL; M16260; AAA82573.1; -; mRNA.
DR PIR; A30201; IJCHCL.
DR RefSeq; NP_001034347.2; NM_001039258.2.
DR AlphaFoldDB; P08641; -.
DR SMR; P08641; -.
DR IntAct; P08641; 2.
DR STRING; 9031.ENSGALP00000000855; -.
DR iPTMnet; P08641; -.
DR PRIDE; P08641; -.
DR GeneID; 415860; -.
DR KEGG; gga:415860; -.
DR CTD; 999; -.
DR VEuPathDB; HostDB:geneid_415860; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P08641; -.
DR OrthoDB; 182239at2759; -.
DR PhylomeDB; P08641; -.
DR PRO; PR:P08641; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016600; C:flotillin 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: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 GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030049; CDH1.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF319; PTHR24027:SF319; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..160
FT /id="PRO_0000003721"
FT CHAIN 161..887
FT /note="Cadherin-1"
FT /id="PRO_0000003722"
FT TOPO_DOM 161..714
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 161..268
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..381
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 382..493
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 494..599
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 600..704
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 745..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3472238"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3472238"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3472238"
FT CARBOHYD 643
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3472238"
FT CONFLICT 140
FT /note="T -> M (in Ref. 1; AAA82572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 97783 MW; F56A8A9779A94A40 CRC64;
MGRRWGSPAL QRFPVLVLLL LLQVCGRRCD EAAPCQPGFA AETFSFSVPQ DSVAAGRELG
RVSFAACSGR PWAVYVPTDT RFKVNGDGVV STKRPLTLYG RKISFTIYAQ DAMGKRHSAR
VTVGRHRHRR HHHNHHLQDT TPAVLTFPKH DPGFLRRQKR DWVIPPISCL ENHRGPYPMR
LVQIKSNKDK ESKVYYSITG QGADSPPVGI FIIERETGWL EVTEQLDREK IDRYTLLSHA
VSASGQPVED PMEIIITVMD QNDNKPVFIK EVFVGYIEEN AKPGTSVMTV NATDADDAVN
TDNGIVSYSI VSQQPPRPHP QMFTIDPAKG IISVLGTGLD RETTPNYTLI VQATDQEGKG
LSNTATAIIE VTDANDNIPI FNPTMYEGVV EENKPGTEVA RLTVTDQDAP GSPAWQAVYH
IKSGNLDGAF SIITDPSTNN GILKTAKGLD YETKSRYDLV VTVENKVPLS VPITLSTASV
LVTVLDVNEP PVFVPPIKRV GVPEDLPVGQ QVTSYTAQDP DRDMRQKITY RMGSDPAGWL
YIHPENGIVT ATQPLDRESV HAINSTYKAI ILAVDNGIPD TTGTGTLLLL LQDVNDNGPT
PEPRSFEICS RQPEKQILSI VDKDLPPHTY PFKAALEHGS SNNWTVEIRG QDELAMGLKK
ELEPGEYNIF VKLTDSQGKA QVTQVKAQVC ECEGTAKNCE RRSYIVGGLG VPAILGILGG
ILALLILLLL LLLFARRRKV EKEPLLPPED DMRDNVYNYD EEGGGEEDQD YDLSQLHRGL
DARPEVIRND VAPPLMAAPQ YRPRPANPDE IGNFIDENLK AADTDPTAPP YDSLLVFDYE
GGGSEATSLS SLNSSASDQD QDYDYLNEWG NRFKKLAELY GGGEDDE
