ID A0A3Q2CGG9_CYPVA Unreviewed; 902 AA.
AC A0A3Q2CGG9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cadherin-1 {ECO:0000256|ARBA:ARBA00023893};
DE AltName: Full=Epithelial cadherin {ECO:0000256|ARBA:ARBA00032684};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000004204.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000004204.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
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}.
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DR RefSeq; XP_015236863.1; XM_015381377.1.
DR AlphaFoldDB; A0A3Q2CGG9; -.
DR Ensembl; ENSCVAT00000008727.1; ENSCVAP00000004204.1; ENSCVAG00000005547.1.
DR GeneID; 107088912; -.
DR KEGG; cvg:107088912; -.
DR GeneTree; ENSGT00940000154848; -.
DR OrthoDB; 5306553at2759; -.
DR Proteomes; UP000265020; Unplaced.
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; 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: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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..902
FT /note="Cadherin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018704606"
FT TRANSMEM 726..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..286
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 287..398
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 399..510
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 511..617
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 616..729
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 902 AA; 99940 MW; 6B70CD3897AC9CDD CRC64;
MGTAWFAVCG VLIVALQVAA VEETSCVPGF ESELLIFKVT RKHLRQGTRL GKVGFTDCTD
RRRFLFSTDD SRFLVQPDGV LAVKRQVVLH EGHRDFFIHS WDSKGQKLTV PAMVMYDGHR
HGNNHPNTEH QHEGHKPNGQ LHDQTEMDAA AEQDAANREV PVLLFPKSSG GLKRRKRDWV
IPPISVSENQ RGPYPYRLNQ IRSSEDSKKT IHYSITGPGA DQPPIDLFTM DRNTGNLYVT
QELDREKQAE YRIWAHAVAE GSSGNAEDPM EIIIKVIDQN DNKPIFDQTT YVAEVPEATQ
KGTDVIQVTA TDADEDNNAN SEIAYRIEKQ SPEEPSLDMF TINPKTGAIR VNAARLDREK
HPEYTLEVSA ADMNGEGLAG STKVIIKVTD SNDHAPVFTE TSYKATIDEN RVDAEVVRML
VTDGDEPHSS AWNAKFKIVG GDPGNLFTVK TGSNKQEGII TTAKGLDFEK ISKHTLLVEV
LNEIPFAIQL PTYTATVEVT VNDVNEAPIF KPKDPTVTKS ESLKEGTNVV KLIAEDPDTA
RKQKVMFKMY IDPAGWLEVS DEGLVTVRSK MDRESAFVSE GKYMAVIHAY DDDQVPATGT
GTLTIILEDV NDNAPSIEQR EFRVCNKKPP PQILNVTDKD GPGNTSPYRV ILHDTAKVNW
TAKMDDTKTA IVLSLIRELE EGEYSVRMTV TDTGNQYQES TVKAHVCECT GEEVMCKGRA
AAGSNLPVIL GILGGILLLL MLVLLLLLFA RRKKPEKEPL LLQDDDIRDN IYYYDEEGGG
EDDQDFDLGV LHRGLDNRPE VFRNDVAPMF MTAPVYKPRP ANPDDIGNFI GDNLKAADND
PTAPPYDSLL VFDYEGGGSE AGSLSSLNSS SDGDQDYDCL ADWGPRFKKL ADMYGGGDDD
ML
//
