ID A0A3B3HM97_ORYLA Unreviewed; 873 AA.
AC A0A3B3HM97;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=LOC105358576 {ECO:0000313|Ensembl:ENSORLP00000032838.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000032838.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000032838.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000032838.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000032838.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000032838.1};
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 AlphaFoldDB; A0A3B3HM97; -.
DR STRING; 8090.ENSORLP00000032838; -.
DR Ensembl; ENSORLT00000044335.1; ENSORLP00000032838.1; ENSORLG00000023981.1.
DR GeneTree; ENSGT00940000154848; -.
DR InParanoid; A0A3B3HM97; -.
DR Proteomes; UP000001038; Chromosome 15.
DR Bgee; ENSORLG00000023981; Expressed in blastula and 10 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
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 PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
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 696..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..252
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 253..364
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 365..476
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 477..584
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 94..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 97209 MW; 04B157640B8AABA9 CRC64;
PCKPGFESDL IFKVNRKHLK PGARLGKVGF TDCTDRTRFL FSTDDSHFVF TTDGVLTVKR
AVVLHEGHLD FFVHSWDSQG NKMTVPVMVL RHGHHQSRDA ERHHGDHRHQ NHHNTEVDSA
NTKEVDLAVL YFPKSSNGLR RRKRDWVVPP INHPENHNGP FPYRMVQIRS NEDQVKKILY
SITGPGATED PVGLFTMDKD TGDLYVHRRL DREKQAHYTL FAHADSAGAS KAEDPMEIII
NIIDMNDNKP IFEQTSYVAE VAESSPKGTT VIQVKATDAD EPGNDNSIIR YTILSQEPKL
PSDSMFAINI FNGAIMVEGV GLDREKYPEY TLEIQAADTK GEGLTGKTAV VLKVTDSNDN
PPVFTASTYQ GLVDENAVGV QVVKMSVTDE DEPNTPAWNA KFKIIRGDPD KLFSIETGSN
KQEGIIKTAQ RLDFEKSRTH TLEVIVENDV PFAIPLTTST ATVVVTVKDV NEPPIFKEKE
MTVQKREDLP VYSVIFKSEA EDPDFARENT VKYKIIDDPE NWLKVDEDSG LVKVKSLMDR
ESPNVKENKY TVLLGAYDND PVPATGTGTL IIILEDVNDN APAIVERETQ ICKHQRTPAL
LSIVDKDEAA HSAPYSVAVH EKYSANWTAK MNESKTGIEL FLKSDIPEGK YKVVLTVSDR
GNLGQASSIN VEVCTCLENG ICSLARTGGK EEMSPYIWGI LGALLLLLVI AVLGLYAYNK
RQKKGEIGEP FEEDIIRDSL YHYAEEGGGE DDQNFDLSVL HYGLDNKPDV LRSDMMPLTM
SRPTYRTLPA NPDQIDNFIE DNLKAADEDP TAPPYDSLLV FDYEGGGSDA GSLSSLNSSN
SGDQDYNCLT EWGPRFKKLA DMYGGGEDDD DML
//