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Database: UniProt
Entry: A0A3B3HM97_ORYLA
LinkDB: A0A3B3HM97_ORYLA
Original site: A0A3B3HM97_ORYLA 
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
//
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