ID A0A212CG54_CEREH Unreviewed; 211 AA.
AC A0A212CG54;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN ORFNames=Celaphus_00002668 {ECO:0000313|EMBL:OWK04930.1};
OS Cervus elaphus hippelaphus (European red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=46360 {ECO:0000313|EMBL:OWK04930.1, ECO:0000313|Proteomes:UP000242450};
RN [1] {ECO:0000313|Proteomes:UP000242450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29294181;
RA Bana N.A., Nyiri A., Nagy J., Frank K., Nagy T., Steger V., Schiller M.,
RA Lakatos P., Sugar L., Horn P., Barta E., Orosz L.;
RT "The red deer Cervus elaphus genome CerEla1.0: sequencing, annotating,
RT genes, and chromosomes.";
RL Mol. Genet. Genomics 293:665-684(2018).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK04930.1}.
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DR EMBL; MKHE01000020; OWK04930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212CG54; -.
DR Proteomes; UP000242450; Chromosome 20.
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:SF27; CLAUDIN-19; 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:UP000242450};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22108 MW; 68DDAB7874B13221 CRC64;
MANSGLQLLG YFLAMGGWVG IIASTALPQW KQSSYAGDAI ITAVGLYEGL WMSCASQSTG
QVQCKLYDSL LALEGHIQSA RALMVVAVLL GFVAMVLSVV GMKCTRVGDS NPIAKGRVAI
AGGALFLLAG LCTLTAVSWY ATLVTQEFFN PSTPVNARYE FGPALFVGWA AAGLALLGGS
FLCCTCPEPE RANNSPQPYR PGPSAAAREY V
//
