ID A0A2K6KX96_RHIBE Unreviewed; 875 AA.
AC A0A2K6KX96;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Cadherin-1 {ECO:0000256|ARBA:ARBA00023893};
DE AltName: Full=Epithelial cadherin {ECO:0000256|ARBA:ARBA00032684};
GN Name=CDH1 {ECO:0000313|Ensembl:ENSRBIP00000015898.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000015898.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000015898.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000015898.1}
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 AlphaFoldDB; A0A2K6KX96; -.
DR Ensembl; ENSRBIT00000039742.1; ENSRBIP00000015898.1; ENSRBIG00000031940.1.
DR GeneTree; ENSGT00940000157175; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; 7.
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:SF319; CADHERIN-1; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
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; 5.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..875
FT /note="Cadherin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014384402"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 190..272
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 273..385
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 435..479
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 480..588
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 587..694
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 875 AA; 96695 MW; 1B36E5A13A7F984B CRC64;
MGPWSRSLSA LLLLLLQVSS WFCQEPEPCH PGFDAESYTF TVPRRHLERG RVLGRVSFED
CTGRQRTAYF SLDTRFKVGP DGVITVKRPL QFHNPQIHFL VYAWDSTYRK FSTKVTLNTV
GHHSRPPPLH ASVSGVQAEL LTFPNSSPGL RRRKRDWVIP PISCPENEKT ECWDPSLLIL
FLSFCFQIKS NKDKEGKVFY SITGQGADTP PVGVFIIERE TGWLKVTEPL DRENIATYTL
FSHAVSSNGN AVEDPMEILI TVTDQNDNKP VFTQEVFKGS VMEGALPGTS VMEVTATDAD
DDVNTYNAAI AYTILSQDPE LPDKNMFTIN KNTGVISVVT TGLDRESFPM YTLVVQAADL
QGEGLSTTAT AVITVTDTND NPPIFNPTTY KGQVPENEAN VVITTLKVTD ADAPNSPACR
NWHPRSCSCP CPLGLDFEAK QQYILHVAVT NVAPFEVSLT TSTATVTVDV LDVNEAPIFV
PPEKRVEVSE DFGVGQEITS YTAREPDTFM EQKITYRIWR DTANWLEINP DTGAISTRAE
LDREDSEHVK NSTYTALIIA TDNGSPVATG TGTLLLILSD VNDNAPIPEP RNIFLCERNP
KPQVINIIDA DLPPNTSPFT AELTHGASAN WTIEYNDPTQ ESIILKPKIA LEVGDYKINL
KLMDNQNKDQ VTTLEVSVCD CEGATGVCKK APLVEAGLQI PAILGILGGI LALLILILLL
LLFLRRRAVV KEPLLPPEDD TRDNVYYYDE EGGGEEDQDF DLSQLHRGLD ARPEVTRNDV
APTLLSVPRY LPRPANPDEI GNFIDENLKA ADSDPTAPPY DSLLVFDYEG SGSEAASLSS
LNSSESDKDQ DYDYLNEWGN RFKKLADMYG GGEDD
//
