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Database: UniProt
Entry: A0A1S3SZQ4_SALSA
LinkDB: A0A1S3SZQ4_SALSA
Original site: A0A1S3SZQ4_SALSA 
ID   A0A1S3SZQ4_SALSA        Unreviewed;       219 AA.
AC   A0A1S3SZQ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Claudin-3 {ECO:0000256|ARBA:ARBA00022063};
GN   Name=LOC106612823 {ECO:0000313|RefSeq:XP_014069823.1};
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_014069823.1};
RN   [1] {ECO:0000313|RefSeq:XP_014069823.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014069823.1};
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|ARBA:ARBA00002246}.
CC   -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC       Homopolymers interact with CLDN1 and CLDN2 homopolymers. Directly
CC       interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3.
CC       {ECO:0000256|ARBA:ARBA00025914}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC       {ECO:0000256|ARBA:ARBA00008295}.
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DR   RefSeq; XP_014069823.1; XM_014214348.1.
DR   AlphaFoldDB; A0A1S3SZQ4; -.
DR   KEGG; sasa:106612823; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
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; IPR003549; Claudin3.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF112; CLAUDIN-3; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01378; CLAUDIN3.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   219 AA;  23354 MW;  C88295B3ED92B2EC CRC64;
     MAVLGLEILG VILAVLGWIL SIVSCALPMW RVSAFIGVNI ITAQTIWEGI WMTCVVQSTG
     QMQCKVYDSM LALSSDLQAA RALTIISIVV GITGVLVAVV GAKCTNCVED ETAKAQVMIA
     AGVAFIVASL TQLIPVSWSA NSIIMDFYSP ITPEAQKREI GVALYLGWAA AAFLLIGGCI
     LCCSCPPQPE KRYAGPPSRM VYSPTRSVAP SSYDKRDYV
//
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