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Database: UniProt
Entry: H2MEC2_ORYLA
LinkDB: H2MEC2_ORYLA
Original site: H2MEC2_ORYLA 
ID   H2MEC2_ORYLA            Unreviewed;       792 AA.
AC   H2MEC2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Cadherin-20 {ECO:0000256|ARBA:ARBA00040456};
GN   Name=CDH20 {ECO:0000313|Ensembl:ENSORLP00000016927.2};
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:ENSORLP00000016927.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000016927.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016927.2,
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:ENSORLP00000016927.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016927.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types. {ECO:0000256|ARBA:ARBA00037319}.
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}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; H2MEC2; -.
DR   STRING; 8090.ENSORLP00000016927; -.
DR   Ensembl; ENSORLT00000016928.2; ENSORLP00000016927.2; ENSORLG00000013497.2.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000158167; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   InParanoid; H2MEC2; -.
DR   TreeFam; TF329887; -.
DR   Proteomes; UP000001038; Chromosome 20.
DR   Bgee; ENSORLG00000013497; Expressed in gastrula and 3 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; 5.
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:SF84; CADHERIN-20; 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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..792
FT                   /note="Cadherin-20"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017396267"
FT   TRANSMEM        609..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..153
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          154..262
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          263..377
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          378..482
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          482..604
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   792 AA;  88091 MW;  3A2D3697311FE14A CRC64;
     MRTQLDLRLA VSRWVPLTLL MVLPHSFVAE PAEGDPGGSA LLQRVKRGWV WNQFFVLEEY
     TGLEPLYIGK LHSDMDKGDG SIRYILTGEG AGTTFTIDDS TGDIHAIQRL DREVKSQYVL
     RAQARNRLTD MPLEPESEFI VKIQDINDNE PKFLDGPYQA TVPEMSKVGT PVIQLTATDA
     DDPTYGNSAR VVYSILEGQP YFSVDAKTGM VRVSLADMDR ETRENYTVVI QAKDMGGQLG
     GLAGTTTINI TLSDVNDNAP VFDQRLYQMS VLESAPMGSV VGRIWAKDRD VGVNAEMKYR
     IIDGDGRDTF DISTDPTNRF GIIMVKKLLD FEKKPSYTLK VEGVNTHPDL TFQNPGPFKD
     VTIVHVSVED VDEPPLFDSA AYYMELPEDA EIGTVVRTVT ARDPDAANNT VRYSIEKTSD
     PDKFFYIELT SGSLMTVRSL DREEISWHNI TVLAMEMNNP SQISSVSVAV KVLDVNDNPP
     SLTHYLETYV CENAKAGQLV ETVTAVDPDE PPAGQHFHYS LAPEAANNPN FTLRDNQDNT
     AWILTRRSSW SQKDQTVFYL PIFISDDEQP VQTSTSTLTV RVCSCDHEGN AMSCNAEAYS
     LPASLSRGAL IAILACIFVL LVMILLMLSL RSHWKKPYLC DEEENIHENI VRYDDEGGGE
     EDTEAFDIAA MWNPREVHHR GKTRQDMLPE IESLSRYVPQ ACVVGGRGDG NVHGYVLAKL
     LEADGDPCAP PYDSLQTYAY EGDGSIAESL SSLQSGNSNA DHEYDYLNDW GPRFKKLAEM
     YGVVETSSPP VW
//
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