ID A0A3Q1B9M7_AMPOC Unreviewed; 239 AA.
AC A0A3Q1B9M7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000010957.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000010957.1}
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; A0A3Q1B9M7; -.
DR Ensembl; ENSAOCT00000018195.1; ENSAOCP00000010957.1; ENSAOCG00000015193.1.
DR GeneTree; ENSGT00940000155232; -.
DR Proteomes; UP000257160; 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:UP000257160};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..239
FT /note="Claudin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018767212"
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; 25440 MW; 3EDEC9FBB1B8000B CRC64;
MSGLQIVAFL SGVAGLGATI GATVSNEWRA TSRASSVITA TWVLQGLWNN CAGNAIGALH
CRPHHTIFQL AGYIQACRGL MIAAVCLGFF GSVFSLVGMK CTKIGGTDKN KARITCFAGV
DFILSGLCSL SACSLYAHRI TSEFFDPMFV AQKYELGAAL FIGWAGSVLC ILGGCMLCFS
IADSCTKSNS QVSYIYKGAA SHSRISSYPR GQAKSVNQRP PPDYSSSSRI QHFDKNAYV
//
