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Database: UniProt
Entry: H2MB77_ORYLA
LinkDB: H2MB77_ORYLA
Original site: H2MB77_ORYLA 
ID   H2MB77_ORYLA            Unreviewed;       792 AA.
AC   H2MB77;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
GN   Name=cdh19 {ECO:0000313|Ensembl:ENSORLP00000015798.1};
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:ENSORLP00000015798.1, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000015798.1, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015798.1,
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:ENSORLP00000015798.1}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015798.1};
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_011487369.1; XM_011489067.1.
DR   AlphaFoldDB; H2MB77; -.
DR   STRING; 8090.ENSORLP00000015798; -.
DR   Ensembl; ENSORLT00000015799.2; ENSORLP00000015798.1; ENSORLG00000012613.2.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000166818; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   InParanoid; H2MB77; -.
DR   OMA; YVCEGTQ; -.
DR   OrthoDB; 3667774at2759; -.
DR   TreeFam; TF329887; -.
DR   Proteomes; UP000001038; Chromosome 20.
DR   Bgee; ENSORLG00000012613; Expressed in muscle tissue and 6 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; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF421; CADHERIN-7-LIKE; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..792
FT                   /note="Cadherin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003565229"
FT   TRANSMEM        610..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          72..152
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          153..261
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          262..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..594
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   792 AA;  88179 MW;  66A62AC005B4BBB9 CRC64;
     MPTSRVLAIV TVFSMIPGGI LSDIKGSRGL ETQHLAQKST YPQRRLKRSW IWTQPFVPEE
     DPSLGVIGQI KSDSDRGDLS IKYILTGEGA GNIFEIDEYS GEIRKLKKLD REEKAFYVLQ
     AQAINRNTNE PEEPQSEFIV KVQDINDNVP QFQNEPYVSS IPEMSPAGTT VAQVTATDAD
     DPMFGNNAKL IYSILQGEPY FSVEPKTGIV VTSWPDLDRE TRDEYLVVIQ VQDMLGLSGG
     YSSSTTLTVI LTDVNDNGPT FQRQLYTFNV PENAAIGSTV GRIIADDGDI GINARMTYSL
     EDDLEESSTF IIKTDPVTQE GQLLLAKPLD YESKRRYKMA VEAINDHVDT RFLPLEEFKD
     STAIKIVVRD VDEPPAFVSP VYEWKVPENA AVGTVVGSIS ARDTDTHNSP IRYSIDKRSD
     ATKSFRIDAN NGTIAIVKAL DRETSSWHNF TIEAKEETQN HLSSSVAVFI KVLDINDNVP
     RLARDYQPYI CEGTQAGELI QLLSAVDVDN PEEGHHFYFS MVPEKHINPN FTIRDNQDNT
     AGIVTRRSTF TLKDRALYFL PVVVADSGTP TLSSTSTLTI SVCRCQPAGH CPTAGVERLL
     LSLDPGLQTV LGILVCLVTI SVLSVLMLLL RRHKRKQQEG LDVGLKELEL PDTVSQKVLH
     YGETGGRRVN FCQPAIPLHP QPRRRERRLR KEEVRASIRM SLGESHFIGP EDEVFRQFIL
     DRLAEADQDP YVPPFDCLQT YAYEGSGSPT GSLSSLDSLT GETELVQPLY NPRAHVVKLS
     PWCGSGEEDT TF
//
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