ID A0A1L8H561_XENLA Unreviewed; 231 AA.
AC A0A1L8H561;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN Name=cldn17.3.S {ECO:0000313|RefSeq:XP_018104016.1,
GN ECO:0000313|Xenbase:XB-GENE-22166262};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018104016.1};
RN [1] {ECO:0000313|RefSeq:XP_018104016.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018104016.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018104016.1};
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_018104016.1; XM_018248527.1.
DR AlphaFoldDB; A0A1L8H561; -.
DR STRING; 8355.A0A1L8H561; -.
DR PaxDb; 8355-A0A1L8H561; -.
DR GeneID; 108708865; -.
DR KEGG; xla:108708865; -.
DR AGR; Xenbase:XB-GENE-22166262; -.
DR CTD; 108708865; -.
DR Xenbase; XB-GENE-22166262; cldn17.3.S.
DR OMA; IILCWAC; -.
DR OrthoDB; 5302473at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
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:SF24; CLAUDIN-8; 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:UP000186698};
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 231 AA; 26002 MW; 17EAA397E63E3D0A CRC64;
MVHLVVQIIG FLCGCIGMIL VWVITLMPQW KVSVIFENQG SLNIRPDGQW ISRFDGLWST
CVNQAQNKQQ CKSYDSMVSV TEDLKAGRVL MSFAVILSFL AFMFSFIGLM LTRYQNKYGK
HCIILTSGIL YIVSVVLMLI PVIWVTTNIV RQACEPLCKG GFRIELGEAL FLAWPAVGFL
LVGGIILCWA CPSRHQQETC IYTTPQDQGV ACRVRPTQGE LSDCYNKIEY I
//
