ID G3PTZ3_GASAC Unreviewed; 210 AA.
AC G3PTZ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021080.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021080.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021080.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; G3PTZ3; -.
DR Ensembl; ENSGACT00000021120.1; ENSGACP00000021080.1; ENSGACG00000015972.1.
DR GeneTree; ENSGT00940000155387; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000015972; Expressed in zone of skin and 3 other cell types or tissues.
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:UP000007635};
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..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 22433 MW; 6383C7B75B7F9AF5 CRC64;
MANAGIQLLG FTLAFLGFIG SIASTVMVEW KASSFSGDNI ITAQAMFQGL WKSCVSQSTG
QVQCKVYDSL LQLPGIVQGT RGLMLSSILL CFISMMVCVV GMRCTTCMAD QPEQKDKVAL
AGGVVFIIAG LLALVGTSWY GHRIAQEFYD PFTPTNSRYE FGSALFVGWG AACLIIIGGG
FLCCNCSSQS SGKSPRYPPP RSTGKNADFR
//
