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Database: UniProt
Entry: A0A3Q3GTV4_9LABR
LinkDB: A0A3Q3GTV4_9LABR
Original site: A0A3Q3GTV4_9LABR 
ID   A0A3Q3GTV4_9LABR        Unreviewed;      1047 AA.
AC   A0A3Q3GTV4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Desmoglein-2-like {ECO:0000313|Ensembl:ENSLBEP00000037787.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000037787.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000037787.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3GTV4; -.
DR   STRING; 56723.ENSLBEP00000037787; -.
DR   Ensembl; ENSLBET00000039349.1; ENSLBEP00000037787.1; ENSLBEG00000028196.1.
DR   GeneTree; ENSGT01030000234624; -.
DR   InParanoid; A0A3Q3GTV4; -.
DR   Proteomes; UP000261660; 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; 3.
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; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01818; DESMOCADHERN.
DR   SMART; SM00112; CA; 3.
DR   SUPFAM; SSF49313; Cadherin-like; 4.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   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        630..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..151
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          229..270
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          271..343
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          412..511
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          346..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1033
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1047 AA;  113153 MW;  DF834BD9DB88BA18 CRC64;
     MFMIFAVNEQ PLSLVLQFQV VTVVTGKSGI HQARRKREWI LPPLPLMENE DYTKKEFIAK
     GALNENNNKR LRQSWRGIMG VILSATPDEN GLRVDRNPDL GWIRVTRILD REEFSVYNLL
     GVATAKNGSE PETRIGIKVE VKDKNDNTPI FSTENQGAVK ELSNPGKLFC FFMQLLQMCK
     LACDGKLNLH IVRDQLFFTS FNRTEMCLLT VVTLPFTPSL RLSNVFFIQK QNKYTLKVIG
     ADLDGRPGGN TGTGTVTINV LDVNDHLPTL EKEEYEGEIE ENTKDVAVMK LKASDLDLKG
     TENWEAVFDI VKGNEAGYFS IKKDPENNNE GILMLVKPVD YEKVKRGGGG GGGGGGGGGG
     GGGGSSGTGS TGSSWQSGTK FKSYPLKIKV KNAPEGPAFI PEVKAIPLLE GGSTVKVNDV
     IARYPAIDGD TLEPAKKVRY VKGSDPGNWL TIDPKTAEIK LNKLPDRESP YLVNGTYLAK
     VLCISEEMPF TTAVGTVAIQ VEDFNDNCPI VTSNHQTMCT TANHVIVIAK DEDVFPNGAP
     FVFNIIPEGT EGKWQVEPLN DTAAILRAQE EKWPGFYKVT FEVKDAQGEA CSEPQEVEVQ
     VCTCEDGVVC GKRGAQGQLG KGAGLGPGGI GLLFLGLLLL LLIPLLLLFC QCGGAAGTSG
     GFKEMPFDTK SHLINYRTEG QGENTEVPLL NLPTQMDGGL AMTNIQTTMA PMTSMGFQHS
     VASMDMINYG EGYQREGAWG TMNEHRGSGF YSEMESRESG LGGGLFDGMA LPDYVLADYY
     SQKLASGNEN LGVKDGILVY DYEGNGSPAG SVGSAGDLES DNGIQFLDDL GLKFKTLAEV
     CGGKKIQTEV KKVRAPAQTS VSSVITAQQL PPPPQVQPTI PQAERTVVRE TVKESTVREG
     MTKVNEGMTR VNEGMANQGQ MFMLQQQQPV YYTTTPMIQP MHYVVQPQVQ NTVLLAEAPS
     TNLQGSGVHT GGFSGTQRVM VVGGPTSSQG QLIQEAGGLS PTNLVPGSSR VRKGSTSARS
     HSSSTTTTVS TGPTIRKVVV KESKEIR
//
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