ID A0A5E4C0Y5_MARMO Unreviewed; 218 AA.
AC A0A5E4C0Y5;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN ORFNames=GHT09_004956 {ECO:0000313|EMBL:KAF7483504.1}, MONAX_5E032287
GN {ECO:0000313|EMBL:VTJ74819.1};
OS Marmota monax (Woodchuck).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Marmota.
OX NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ74819.1, ECO:0000313|Proteomes:UP000335636};
RN [1] {ECO:0000313|EMBL:VTJ74819.1, ECO:0000313|Proteomes:UP000335636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF7483504.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WC2-LM {ECO:0000313|EMBL:KAF7483504.1};
RC TISSUE=Liver {ECO:0000313|EMBL:KAF7483504.1};
RA Shumante A., Zimin A.V., Puiu D., Salzberg S.L.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; WJEC01000362; KAF7483504.1; -; Genomic_DNA.
DR EMBL; CABDUW010000763; VTJ74819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4C0Y5; -.
DR OrthoDB; 4040914at2759; -.
DR Proteomes; UP000335636; Unassembled WGS sequence.
DR Proteomes; UP000662637; Unassembled WGS sequence.
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; IPR003551; Claudin5.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; CLAUDIN; 1.
DR PANTHER; PTHR12002:SF35; CLAUDIN-5; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01077; CLAUDIN.
DR PRINTS; PR01380; CLAUDIN5.
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:UP000335636};
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 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 164..189
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 218 AA; 22919 MW; 52ABD2FA8D9203A2 CRC64;
MGSAALEILG LVLCLVGWVG LILACGLPMW QVTAFLDHNI VTAQTTWKGL WMSCVVQSTG
HMQCKVYESV LALSTEVQAA RALTVGAVLL ALVALFVSLA GAQCTTCVAP GPAKARVALT
GGVLYALCGL LALVPLCWFA NIVVREFYDP AVPVSQKYEL GAALYIGWAA SALLMCGGGL
VCCGAWVCAG RPDLSFPVKY SAPRRPTASG DYDKKNYV
//
