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Database: UniProt
Entry: A0A3B3BNN5_ORYME
LinkDB: A0A3B3BNN5_ORYME
Original site: A0A3B3BNN5_ORYME 
ID   A0A3B3BNN5_ORYME        Unreviewed;      1188 AA.
AC   A0A3B3BNN5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Desmoglein-2-like {ECO:0000313|Ensembl:ENSOMEP00000006593.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000006593.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000006593.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC       the interaction of plaque proteins and intermediate filaments mediating
CC       cell-cell adhesion. {ECO:0000256|RuleBase:RU004358}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC       {ECO:0000256|ARBA:ARBA00004568}. Cell membrane
CC       {ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC       {ECO:0000256|RuleBase:RU003318}.
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DR   AlphaFoldDB; A0A3B3BNN5; -.
DR   Ensembl; ENSOMET00000005540.1; ENSOMEP00000006593.1; ENSOMEG00000007667.1.
DR   GeneTree; ENSGT01030000234624; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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; 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   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF1; DESMOGLEIN-2; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01818; DESMOCADHERN.
DR   SMART; SM00112; CA; 4.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 2.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
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}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1188
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017400921"
FT   DOMAIN          61..142
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          142..251
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          252..339
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          449..560
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          362..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1135..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1188 AA;  126235 MW;  E72B45F233697E95 CRC64;
     MARLFQSVLV VLVLVQVAIV VRQTSGKNLV RKKREWILPP KPLKENKDYT KELSIAKIRS
     DFQQDQKVEY YLEGPGANQK PFNVFVVNHE TGDVRVTKIL DREEVDTYAL KGIAKYANGS
     EAERPIDLKI KVEDENDNDP VFPETLSVSV YELRPRGTFV VQVNATDADE PGNKNSELAY
     SLISQNPPHD MFSINKSGMI SVKNPNLDRE RCAQYSLTVQ AKDLYGEDGG RTATGVIIIN
     VLDVNDNLPT LEKLQYDGSI EENTHNVEVM RLKSNDDDLE GTDNWEAVYE IVKGNDAGYF
     NIVTDPKTNE GILMLVKPVD YEDVKDLDLG IIVKNKAPPF DPSAVINGAD VNIGGGAIGA
     SGASGASGAS GASGASGTNG ASGATGSGGA TGSGGPTGSG GPTGSGGATG ASGSSGGSTG
     TSGGSGSIKY TSYPVKINVK NKPEGPGFEP QVKNIPISEG LDPANLKKPI ATYTAIDKDT
     GKPAKNVRYL KGPDPGNWLS IDPETAEITL TKIPDRESPY LINGTYFANV LCISEDMPDK
     TATGTIAIKV EDTNDNCPTL TTNSKVICLP EDSFIVNGED KDSFPNGPPL HFVIVPEKTQ
     GDWKVEHLND SAVIVRAQKE LWPDSYTVEM VVSDQQGLSC KDPQKMEIVA CTCHDGVVCG
     ALGGQGQSRK DITLGPAAIG LMLLGLLLLL LIPLLLLSCM CGSVGNFQDI FSSIPYGTEE
     MLIKYHTEQN GENTEIPLLN TPGYLLVDSA KGHFAAAPAE LQQSFVAGNE LGTLRGYRET
     GTMFSDGQWQ MNQWGSGLLS ASEVQEFGQG GEGNLALPDS YLRDYYDQRT SINRSDAVKD
     SLLVFNNEGE GSLAGSLGSC SMLEQDGDLQ FLDDLEIKFK TLAEICGGKT VVSETKAVSI
     PPPVASVAMP KLSESTFESN MVTTQRVAPP PSLPPTTIRE ERTVVTDTTD HSKVLREDAA
     MLSEGMTSMA TGMGGQSQML VLQQQQQPVY YTAAPMLQPM QYVVQPQFQN AVILTEAPAA
     GLQDVVLLNG SDIGSNPGMI IQGQTMMHSG HAQGTGTMLL ENGSNLLHMG NLSGSQAMMV
     VDGTVAGSAT GVQGTLIQGG SLGSATGVQG TLIQGGSLSS GQHSGTQRVV RVEEATSGRG
     RAGKSGRSSL QRIVSTKGST QTSTSSTSLS TPTNTTQKVL IQETRQIR
//
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