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Database: UniProt
Entry: A0A668ANR7_9TELE
LinkDB: A0A668ANR7_9TELE
Original site: A0A668ANR7_9TELE 
ID   A0A668ANR7_9TELE        Unreviewed;       239 AA.
AC   A0A668ANR7;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN   Name=CLDN10 {ECO:0000313|Ensembl:ENSMMDP00005052888.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005052888.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005052888.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a major role in tight junction-specific obliteration of
CC       the intercellular space, through calcium-independent cell-adhesion
CC       activity. {ECO:0000256|RuleBase:RU060637}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|RuleBase:RU060637}. Cell membrane
CC       {ECO:0000256|RuleBase:RU060637}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU060637}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC       {ECO:0000256|ARBA:ARBA00008295, ECO:0000256|RuleBase:RU060637}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU060637}.
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DR   AlphaFoldDB; A0A668ANR7; -.
DR   Ensembl; ENSMMDT00005053916.1; ENSMMDP00005052888.1; ENSMMDG00005023816.1.
DR   GeneTree; ENSGT00940000155232; -.
DR   InParanoid; A0A668ANR7; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF13; CLAUDIN-10; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW   ECO:0000256|RuleBase:RU060637};
KW   Cell membrane {ECO:0000256|RuleBase:RU060637};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU060637};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU060637};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU060637}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..239
FT                   /note="Claudin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025422728"
FT   TRANSMEM        80..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        114..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   TRANSMEM        157..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU060637"
FT   REGION          206..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  25284 MW;  888FFF67924DD853 CRC64;
     MSGVQIVALL GGLAGLGATI GATVSNEWRA TSRASSVITA TWVLQGLWNN CAGNAIGALH
     CRPHHTILKL EGYIQACRGL MIAAICLGFF GAIFALVGMK CTKIGGTDVN KARIACFAGV
     NFILSGLCSL SACSLYAHQI TTEFFDPMFI AQKYELGAAL FIGWGGSILC ILGGGLFCFS
     IAGSCTKSHS QAGYIYKGAT SHSHISSYPR GQAKSVNQRP PPEYSSSSRM QHFDKNVYV
//
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