ID A0A3Q4G846_NEOBR Unreviewed; 209 AA.
AC A0A3Q4G846;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000004990.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000004990.1}
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 RefSeq; XP_006786887.1; XM_006786824.1.
DR AlphaFoldDB; A0A3Q4G846; -.
DR STRING; 32507.ENSNBRP00000004990; -.
DR Ensembl; ENSNBRT00000005144.1; ENSNBRP00000004990.1; ENSNBRG00000003979.1.
DR GeneID; 102791209; -.
DR CTD; 9076; -.
DR GeneTree; ENSGT00940000155387; -.
DR OMA; RCTTCMA; -.
DR OrthoDB; 4040914at2759; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000003979; Expressed in zone of skin and 1 other cell type or tissue.
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:SF92; CLAUDIN-1; 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:UP000261580};
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 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 118..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 209 AA; 22059 MW; 8A5C52B24E9F3A6C CRC64;
MANAGVQLLG FILALIGSFG IIAATIMVQW KASSYVGDNI ITAQAMYEGL WQTCASQSTG
QVQCKVYDSL LQLPGNVQGT RGLMVSSIVL CFISILVAVM GLKCTTVMSD SPDLKDKVAL
SGGVIFILAG LLALAGASWF GSNIAKEFYN PFTPTNSRYE FGSALYVGWA SAILVIIGGA
FLCCHCPKQD AGPAQRYPQS HPAGGKNYV
//