ID A0A1S3L2H0_SALSA Unreviewed; 185 AA.
AC A0A1S3L2H0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN Name=LOC106563813 {ECO:0000313|RefSeq:XP_013985153.1,
GN ECO:0000313|RefSeq:XP_013985154.1, ECO:0000313|RefSeq:XP_013985155.1,
GN ECO:0000313|RefSeq:XP_013985156.1, ECO:0000313|RefSeq:XP_013985157.1,
GN ECO:0000313|RefSeq:XP_013985158.1, ECO:0000313|RefSeq:XP_013985159.1,
GN ECO:0000313|RefSeq:XP_013985161.1, ECO:0000313|RefSeq:XP_013985162.1,
GN ECO:0000313|RefSeq:XP_013985163.1, ECO:0000313|RefSeq:XP_013985164.1,
GN ECO:0000313|RefSeq:XP_013985165.1, ECO:0000313|RefSeq:XP_013985166.1,
GN ECO:0000313|RefSeq:XP_013985167.1, ECO:0000313|RefSeq:XP_013985168.1,
GN ECO:0000313|RefSeq:XP_013985169.1, ECO:0000313|RefSeq:XP_013985170.1,
GN ECO:0000313|RefSeq:XP_013985172.1, ECO:0000313|RefSeq:XP_013985173.1,
GN ECO:0000313|RefSeq:XP_013985174.1, ECO:0000313|RefSeq:XP_013985175.1,
GN ECO:0000313|RefSeq:XP_013985176.1, ECO:0000313|RefSeq:XP_013985177.1,
GN ECO:0000313|RefSeq:XP_013985178.1, ECO:0000313|RefSeq:XP_013985179.1,
GN ECO:0000313|RefSeq:XP_013985180.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013985157.1};
RN [1] {ECO:0000313|RefSeq:XP_013985153.1, ECO:0000313|RefSeq:XP_013985154.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013985153.1,
RC ECO:0000313|RefSeq:XP_013985154.1};
RG RefSeq;
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}.
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DR RefSeq; XP_013985153.1; XM_014129678.1.
DR RefSeq; XP_013985154.1; XM_014129679.1.
DR RefSeq; XP_013985155.1; XM_014129680.1.
DR RefSeq; XP_013985156.1; XM_014129681.1.
DR RefSeq; XP_013985157.1; XM_014129682.1.
DR RefSeq; XP_013985158.1; XM_014129683.1.
DR RefSeq; XP_013985159.1; XM_014129684.1.
DR RefSeq; XP_013985161.1; XM_014129686.1.
DR RefSeq; XP_013985162.1; XM_014129687.1.
DR RefSeq; XP_013985163.1; XM_014129688.1.
DR RefSeq; XP_013985164.1; XM_014129689.1.
DR RefSeq; XP_013985165.1; XM_014129690.1.
DR RefSeq; XP_013985166.1; XM_014129691.1.
DR RefSeq; XP_013985167.1; XM_014129692.1.
DR RefSeq; XP_013985168.1; XM_014129693.1.
DR RefSeq; XP_013985169.1; XM_014129694.1.
DR RefSeq; XP_013985170.1; XM_014129695.1.
DR RefSeq; XP_013985172.1; XM_014129697.1.
DR RefSeq; XP_013985173.1; XM_014129698.1.
DR RefSeq; XP_013985174.1; XM_014129699.1.
DR RefSeq; XP_013985175.1; XM_014129700.1.
DR RefSeq; XP_013985176.1; XM_014129701.1.
DR RefSeq; XP_013985177.1; XM_014129702.1.
DR RefSeq; XP_013985178.1; XM_014129703.1.
DR RefSeq; XP_013985179.1; XM_014129704.1.
DR RefSeq; XP_013985180.1; XM_014129705.1.
DR KEGG; sasa:106563813; -.
DR OrthoDB; 4040914at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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:SF192; CLAUDIN-RELATED; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01077; CLAUDIN.
DR PRINTS; PR01385; CLAUDIN14.
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:UP000087266};
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 5..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 117..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 185 AA; 19751 MW; 9244860955ADF8A9 CRC64;
MSRQILAFVL AFIGFMGTIV ICALPMWKVT AFVGANIVTA QVFWEGLWMN CVIQSTGHMQ
CKAYDSLLAL PQNLQASRAL ICVSIGVSVL AIGLTVVGAR CTNFLHDDWL AKSKVGIAAG
AVFMAAGVLC VIPVSWSAHT IIQGFYNPLA TQERRGELGA SIYVGWVSGA LLMIGGGMLC
STYRC
//
