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Database: UniProt
Entry: A0A3P8VTB1_CYNSE
LinkDB: A0A3P8VTB1_CYNSE
Original site: A0A3P8VTB1_CYNSE 
ID   A0A3P8VTB1_CYNSE        Unreviewed;       887 AA.
AC   A0A3P8VTB1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Desmocollin-1-like {ECO:0000313|Ensembl:ENSCSEP00000017572.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000017572.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000017572.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000017572.1}
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|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC       ECO:0000256|RuleBase:RU003318}.
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DR   RefSeq; XP_008332597.1; XM_008334375.2.
DR   AlphaFoldDB; A0A3P8VTB1; -.
DR   STRING; 244447.ENSCSEP00000017572; -.
DR   Ensembl; ENSCSET00000017790.1; ENSCSEP00000017572.1; ENSCSEG00000011279.1.
DR   GeneID; 103396334; -.
DR   KEGG; csem:103396334; -.
DR   CTD; 560091; -.
DR   GeneTree; ENSGT01030000234624; -.
DR   InParanoid; A0A3P8VTB1; -.
DR   OMA; ITMRAVD; -.
DR   OrthoDB; 4539697at2759; -.
DR   Proteomes; UP000265120; Chromosome 20.
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:0060027; P:convergent extension involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0002159; P:desmosome assembly; IEA:Ensembl.
DR   GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
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; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF78; CADHERIN-LIKE PROTEIN 26; 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   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 6.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..887
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017995968"
FT   TRANSMEM        665..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          150..232
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          232..339
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          340..452
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          453..558
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          577..678
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   887 AA;  97537 MW;  D55A6EBDDB87DBDA CRC64;
     MANIFVFALS FMLSLLRVEP CFIPDSLYLL VPQQIQPDFE LTKVGTANCD SKTLRLTLSD
     ESFEFNNGRI VAVTDVYVGA GGRTFYVRAE DGSGPQSEME VHLIHSTLQK PKPKEGLLKR
     TKRRWSPPPF NILENDPGPY PKEIERIVSD SSATHDVYYT FSGPGFNEHP VGVFSLDKDS
     GMLKVHQTVD REMFPNFTLT TKVFDKHTMQ PTDSPLPIQI IVDDVNDNAP EFKSALQFSV
     LEHSKSGTSV GKVEATDRDQ EGTTHVKIKY SLLTGSDKFS INPVTGVITT LVGNLDREVK
     DKQLVTVEIK DMNGAPIGLS NTGTATITIG DINDNPPTFT KASYNANVKE NEQDKLILHI
     PVEDKDLINT PNWKSKFIIT KGNENGIFRI DTDPKTNEGL LYVVKPLNFE KNKNVKLEVM
     ARNEADLSNT DAKWQTVPVD ISVTDIDEGP EFSAPTVRFT VKENTPNGTL IGSYTATDPE
     TKSSDGIKYY KSTDPAAWIN VDKNTGELRV ANTIDKESHF VQNGIYNITM KAVDVTSKTG
     TGTVIIQVED VNDNVPTLPT GERVICEKDG ELGSVYVVAE DKDESPFSSP FSFNLPKDND
     GKWTMATYNA TTGILKQIKE LPRGIYQVPV DVTDLQGFGK TQTVTVRICQ CRNGICLAKD
     RSVTLGGLAV LAMLLPLLLL LLLCLLLAFI CVTKREKREI EDTGDSGGIL LQSNTEGKGD
     EVDASLIIVP TSGVDIDLTK GSVKDLNTGY IKGSMGTMGG HNIHESWRYK SNEIDSGQFD
     QNGKLGGHYG HLVNSGVSAD SRYVQDASFL HNWQTNGRYL HKKLDYFVSE EDGRYADDII
     HSYGFEGAGS AAGSVGCCSE FGDNENLDFL NALGPKFKTL ADVCKKT
//
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