ID A0A452F333_CAPHI Unreviewed; 887 AA.
AC A0A452F333;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cadherin-1 {ECO:0000256|ARBA:ARBA00023893};
DE AltName: Full=Epithelial cadherin {ECO:0000256|ARBA:ARBA00032684};
GN Name=CDH1 {ECO:0000313|Ensembl:ENSCHIP00000018796.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000018796.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000018796.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000018796.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta
CC precursors. Has a strong inhibitory effect on APP C99 and C83
CC production. {ECO:0000256|ARBA:ARBA00025086}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}. Golgi
CC apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; LWLT01000020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452F333; -.
DR Ensembl; ENSCHIT00000026611.1; ENSCHIP00000018796.1; ENSCHIG00000018029.1.
DR GeneTree; ENSGT00940000157175; -.
DR OMA; LHEGHHD; -.
DR Proteomes; UP000291000; Chromosome 18.
DR Bgee; ENSCHIG00000018029; Expressed in descending colon and 15 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd00031; CA_like; 1.
DR CDD; cd11304; Cadherin_repeat; 3.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF435; CADHERIN-1; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 714..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..266
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 267..379
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 380..490
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 491..599
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 783..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 98224 MW; 009CD88C98D0E78C CRC64;
GLPWALGAAT SLRSCCCCRY VSSWLCQEPE PCVPGFGAES YTFTVPRRNL ERGRVLGRVS
FEGCAGLPRT VYVSDDTRFK VHTDGLVTVK RPVHLHRPEL SFLVHAWDST HRKLSTKVTL
TVSAHHHHHH RHHDSLSGTQ TEVLTFPGSH HGLRRQKRDW VIPPISCPEN EKGPFPKSLV
QIKSNKEKET QVFYSITGQG ADTPPVGVFI IERETGWLKV TQPLDREHIA KYILFSHAVS
SNGQAIEEPM EIVITVTDQN DNKPQFTQEV FKGSVLEGAL PGTSVMQVTA TDIDDDVNTH
NAAIGYKILA QEPMLPHNKM FTINKETGVI SVLTTGLDRE SFPTYTLMVQ AADLNGEGLS
TTATAVITVL DANDNAPRFD PTTYMGSVPE NEANVAITTL TVTDADVPNT PAWEAVYTVL
NDNEKQFIVI TDPVTNEGTL KTAKGLDFEA KQQYILYVAV TNVAPFEVTL PTSTATVTVD
VIDVNEAPIF VPPQKKVEVP EDFGVGLEIT SYTAREPDTF MEQKIMYRIW RDAANWLEIN
PETGAISTRA ELDREDVEHV KNSTYTALII ATDNGSPPAT GTGTLLLFLD DVNDNGPVPE
PRAMDFCQRN PEPHIINIMD PDLPPNTSPF TAELTHGASV NWTIEYNDQE RESLILKPKK
TLELGDHKIN LKLIDNQNKD QVTTLDVHVC DCDGIVSNCR KATPFAEAGL QVPAILGILG
GVLAFLILIL LLLLLVRRRR VVKEPLLPPE DDTRDNVYYY DEEGGGEEDQ DFDLSQLHRG
LDARPEVTRN DVAPTLMSVP QYRPRPANPD EIGNFIDENL KAADSDPTAP PYDSLLVFDY
EGSGSEAASL SSLNSSESDQ DQDYDYLNEW GNRFKKLADM YGGGEDD
//