CADHK_CHICK
ID CADHK_CHICK Reviewed; 732 AA.
AC P33145;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=B-cadherin;
DE AltName: Full=K-CAM protein;
DE Flags: Precursor; Fragment;
GN Name=K-CAM;
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].
RX PubMed=1763068; DOI=10.1073/pnas.88.24.11545;
RA Sorkin B.C., Gallin W.J., Edelman G.M., Cunningham B.A.;
RT "Genes for two calcium-dependent cell adhesion molecules have similar
RT structures and are arranged in tandem in the chicken genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11545-11549(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-732.
RC TISSUE=Embryonic brain;
RX PubMed=2026653; DOI=10.1083/jcb.113.4.893;
RA Napolitano E.W., Venstrom K., Wheeler E.F., Reichardt L.F.;
RT "Molecular cloning and characterization of B-cadherin, a novel chick
RT cadherin.";
RL J. Cell Biol. 113:893-905(1991).
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. B-cadherin may have important functions in
CC neurogenesis, in at least some epithelia, and in embryogenesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of 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; M81894; AAA48929.1; -; Genomic_DNA.
DR EMBL; X58518; CAA41408.1; -; mRNA.
DR PIR; A41634; IJCHCB.
DR AlphaFoldDB; P33145; -.
DR SMR; P33145; -.
DR STRING; 9031.ENSGALP00000000853; -.
DR VEuPathDB; HostDB:geneid_414845; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P33145; -.
DR PhylomeDB; P33145; -.
DR Proteomes; UP000000539; 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; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
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;
KW Transmembrane; Transmembrane helix.
FT PROPEP <1..6
FT /evidence="ECO:0000255"
FT /id="PRO_0000003831"
FT CHAIN 7..732
FT /note="B-cadherin"
FT /id="PRO_0000003832"
FT TOPO_DOM 6..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 6..114
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 115..227
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 228..339
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 340..443
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 444..554
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 414
FT /note="M -> V (in Ref. 2; CAA41408)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 732 AA; 80613 MW; 091D59A6A16CBD45 CRC64;
LRRQKRDWVI PPIKVPENER GPFPKNLVQI KSNRDREAKI FYSITGQGAD APPEGIFTIE
KETGWMKVTQ PLDREHINKY HLYSHAVSEN GKPVEEPMEI IVTVTDQNDN KPQFTQEVFR
GSVPEGALPG TSVMRVNATD ADDDVETYNG VIAYSILSQE PREPHPHMFT VNRATGTLSV
IASGLDRERV REYTLTMQAA DLDGQGLTTT ALAVIEITDV NDNAPEFDPK TYEAAVPENE
AELEVARLAT TDLDEPHTPA WRAVYSIVRG NEGGAFTITT DPASNEGVLR TAKGLDYEAK
RQFVLHVAVV NEAPFAIKLP TATATVMVSV EDVNEAPVFD PPLRLAQVPE DVPLGQPLAS
YTAQDPDRAQ QQRIKYVMGS DPAGWLAVHP ENGLITAREQ LDRESPFTKN STYMAVLLAV
DDGLPPATGT GTLLLTLLDV NDHGPEPEPR DIVICNRSPV PQVLTITDRD LPPNTGPFRA
ELSHGSGDSW AVEVGNGGDT VALWLTEPLE QNLYSVYLRL FDRQGKDQVT VIRAQVCDCQ
GRVESCAQKP RVDTGVPIVL AVLGAVLALL LVLLLLLLLV RRRKVVKEPL LLPEDDTRDN
IFYYGEEGGG EEDQDYDLSQ LHRGLDARPE VIRNDVAPPL MAAPQYRPRP ANPDEIGNFI
DENLKAADTD PTAPPYDSLL VFDYEGGGSE ATSLSSLNSS ASDQDQDYDY LNEWGNRFKK
LAELYGGGED EE
