ID   A0A3B5A475_9TELE        Unreviewed;      1314 AA.
AC   A0A3B5A475;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Desmoglein-2-like {ECO:0000313|Ensembl:ENSSPAP00000015495.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000015495.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000015495.1}
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   Ensembl; ENSSPAT00000015746.1; ENSSPAP00000015495.1; ENSSPAG00000011666.1.
DR   GeneTree; ENSGT01030000234624; -.
DR   Proteomes; UP000261400; 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:SF23; CADHERIN-4; 1.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 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|SAM:Phobius}; 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        55..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..196
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          204..305
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          306..389
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          488..598
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          415..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1278..1298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1314 AA;  140438 MW;  24256840F83F30AF CRC64;
     MGIYASTCVR SAPPPQPPPL TCSVSQSVFQ SVRNSFLRHQ DTIGLTVPDK DFSSVMIRVS
     SPVAVLLLFA VFLVVTANSG QKLVRKRREW ILPPKPLTEN VDYTKMESIA RIRSDFQSGT
     NVVYSLEGIG ANQNPFHVFV VDPNTGNVRV TKVLDREFID TYNLSGVATY RNGTQAEKKI
     DLRIKVEDQN DNAPVFGVVK PGAVNELSPK DTFVMKVSAT DADEPGNPNS MIAYSIIEQK
     PPGDMFYIDP TGNVYVKKLG LDRETIDQYV LTVKGQDLNG QRGGHSGTGT LTINVLDVND
     NPPTLEKEQY EGSIEENTEG VEVMRLKAED LDLKDTDNWE AVFDIVKGNE GGYFSIKTDP
     ETNEGILMLD KPVDYENIKD LDLGLVVRNK APLYDGFAPN GAGSIGFGGG AGGGGGSGTG
     SGTGSGTGSG TGGGGSGSGT GTGTGTGTGS GTGTSGTGAT SATGATTGFK TYPIKISVKN
     QPEGPRFDPK VKAIPISEGD SFDINKVIAS YPAIDGDTGK PAENVRYAKG SDPDNWFTID
     PKTAEIKLNK IPDRESPALV NGTYIAKVLC ITDDMPAKTA TGTIAIQVED FNDHCPTLTS
     DKRTMCTTSD AVIVNANDED AYPNGPPFDF VIIPEGTDGK WQVEHLNDTA AILKAQESLW
     PGFYEVEFVV RDRQGQACPD PQKVQIEVCT CADGVVCEQQ TVSGHSSKGV ELGPAAIGLL
     LLGLLLLLII PLLMLLCQCG GISGFPDLFA EMPFDTKTHL INYHTERLGE NTEVPLLNMP
     TQVDGNMVTM GAAKKTAMAP VAGLDFHQSI TSVNGMNGGT FQEGFLSTHR EGMWGMNQQD
     GSGFFSDFES RESGGGGEIY DLIALPDHLL EQYYNQATSG NDNLRFKDDL LMYDYEGKGS
     SADSVGCCSL LESENDLQFL DDLGPKFKTL AEVCGGTKIS TEVKQVCSPP PSSSIPSTQA
     SVSNLVMAQQ LPPSPKLQPT IPKTEQAVVR KTAEGSQLVM ESMATVREGM TTVKTLKERM
     ATDKTGLEGK TGMVNQMLLL QQQQQQPVYY TTTPVLQPMH YVVQPQVQNT MLVTEVPATN
     LPGMVLVDNN EIHGSCANLI HTGNFSGVHR SCANLIHTGN VSNVHGSCAS LIHTGNFSNV
     HGSCANLIHT GNFPDVHRSC ANLAHTGTFS DVSSCCANLI DTRNVSDVHR SCANLIYSGN
     LPGVHGSCAN LIHNGNFYGA QPMMVVEGKA PAGSMKVRKG SQTCLIQGGT LQCAELSGSQ
     RVKVVREPTS SRGKVVEQAG LSQKRSSAYK EFPPAREGHP LSVRAASMPF LPPA
//