ID A0A665WQB5_ECHNA Unreviewed; 211 AA.
AC A0A665WQB5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN Name=LOC115053780 {ECO:0000313|Ensembl:ENSENLP00000046156.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000046156.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000046156.1}
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}.
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DR AlphaFoldDB; A0A665WQB5; -.
DR Ensembl; ENSENLT00000047288.1; ENSENLP00000046156.1; ENSENLG00000019589.1.
DR InParanoid; A0A665WQB5; -.
DR OMA; YNPMVPD; -.
DR Proteomes; UP000472264; 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:SF209; CLAUDIN-LIKE PROTEIN ZF-A89; 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:UP000472264};
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 TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 121..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 164..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 211 AA; 22439 MW; FF3AC2443B8E121E CRC64;
MASLGLQILG VGLAVLGWIG NILICMLPLW KVSAFIGNNI VVAQTIWEGL WMTCVVQSTG
QMQCKVYDSL LALPPDLQAA RAMVVIAILF SLFGLLLSVV GGKCTTCVGD KAAKARVAIS
AGIFFILSGA LCLVTVSLPA NTIIKDFYNP LVPDAQRREL GACLYVGWGA SGLLLIGGAL
LCCQCPTGRD RYNGPKYSSV AQSSYTRRDY V
//
