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Database: UniProt
Entry: H2MFA8_ORYLA
LinkDB: H2MFA8_ORYLA
Original site: H2MFA8_ORYLA 
ID   H2MFA8_ORYLA            Unreviewed;       796 AA.
AC   H2MFA8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Cadherin 18 {ECO:0000313|Ensembl:ENSORLP00000017280.1};
GN   Name=CDH18 {ECO:0000313|Ensembl:ENSORLP00000017280.1};
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:ENSORLP00000017280.1, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000017280.1, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017280.1,
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:ENSORLP00000017280.1}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000017280.1};
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   RefSeq; XP_004081245.1; XM_004081197.2.
DR   STRING; 8090.ENSORLP00000030444; -.
DR   Ensembl; ENSORLT00000017281.2; ENSORLP00000017280.1; ENSORLG00000013779.2.
DR   Ensembl; ENSORLT00000038412.1; ENSORLP00000030444.1; ENSORLG00000013779.2.
DR   Ensembl; ENSORLT00000044151.1; ENSORLP00000036182.1; ENSORLG00000013779.2.
DR   GeneID; 101174782; -.
DR   KEGG; ola:101174782; -.
DR   CTD; 1016; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000157512; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   OMA; RTMQDVY; -.
DR   OrthoDB; 3667774at2759; -.
DR   TreeFam; TF329887; -.
DR   Proteomes; UP000001038; Chromosome 20.
DR   Bgee; ENSORLG00000013779; Expressed in brain and 9 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: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; 4.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
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; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027:SF106; CADHERIN-18; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
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:UP000001038};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..796
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041197793"
FT   TRANSMEM        616..637
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..160
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          161..269
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          270..384
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          385..489
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          489..606
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   796 AA;  88150 MW;  2AB2BF9A498F7DCF CRC64;
     MRIPMTCCLC PFLVCLCFIQ RCYGASHHVP TKVPSKNQTK LANGETEVHH RPKRGWIWNQ
     FFVLEEHMGP DAQYVGKLHS NSDKGDGSVR YILSGEGAGT IFIIDEVTGD IHATKSLDRE
     RKAHYVLHAQ ALDRNTEEAL EPKSEFIIKV QDINDNAPKF PDGPFEATVP EMSEVGTSVL
     QVTATDSDDP TYGNSAKIVY SILQGQPYFS VDPKTGIIRT ALPNMDREAR EHYTVVIQAK
     DMAGQVGGLS GSTTINITLT DVNDNPPKFP QKNYQVLVLE SAEVGTPVGK LKANDDDLGT
     NADIKYTIIN SEGANMFSIA TNRDTKEGIV SLKKPLNYER KKTYTLHIEG LNTHADPRFT
     YLGPFKDTAT LKISVGDVDE APVFSMDYYI LDVYENSPSG TEVGTVTARD PDGDNKPVRY
     ELDSKEEEES YFRIDAKSGV IRTTQPLDRE DTPWHNITVV ASEVGNPVLF SHVPVTVQVL
     DTNDNPPEVA ADEEVIVCES SRPGQVIQTV RAVDKDDFAN GQRFSFALPS QLPVNPNFTL
     KDNEDSTASI IARRRRFSHL TQELYELPIV VWDGGEPSLT GTSTLTLRVC PCQRHGRIRM
     CQGEAFLSSA GLSTGALIAI LLCIIILLAI VVLFITLRRS KKEPLIISEE DIRENVVTYD
     DEGGGEEDTE AFDIVALRNP AAAEELKFRR DIRPEARSQC GFAHGQRSPS VELDEVDVHK
     FIKQRLVEAD MDASVPPYDS LQTYAYEGQG SPAGTISPLD SLGVQSEQEY NYLDDWGPEF
     QKLAELYGEA ESDVTT
//
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