ID A0A4U1F120_MONMO Unreviewed; 208 AA.
AC A0A4U1F120;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN ORFNames=EI555_004156 {ECO:0000313|EMBL:TKC42945.1};
OS Monodon monoceros (Narwhal) (Ceratodon monodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Monodon.
OX NCBI_TaxID=40151 {ECO:0000313|EMBL:TKC42945.1, ECO:0000313|Proteomes:UP000308365};
RN [1] {ECO:0000313|Proteomes:UP000308365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31054839; DOI=10.1016/j.isci.2019.03.023;
RA Westbury M.V., Petersen B., Garde E., Heide-Jorgensen M.P., Lorenzen E.D.;
RT "Narwhal Genome Reveals Long-Term Low Genetic Diversity despite Current
RT Large Abundance Size.";
RL IScience 15:592-599(2019).
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}.
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:TKC42945.1}.
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DR EMBL; RWIC01000508; TKC42945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U1F120; -.
DR Proteomes; UP000308365; 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; 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 PRINTS; PR01446; CLAUDIN8.
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:UP000308365};
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 62..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 97..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 149..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 208 AA; 22974 MW; 2D153D8B6800B74D CRC64;
MVGTVAVTIM PQWRVSAFIG SNIVVFENLW EGLWMNCMRH ANIRMQCKIY DSLLALSPDL
QASRGLMCAA SVLSFLAFMT AVLGMKCTRC TGDDEKVKGY ILLTAGAVFI VTGLVVLIPV
SWVANSIIRD FYNPIVDIAQ KRELGEALYI GWTTALVLIA GGALFCCVSC CNEKSGSYRY
SIPSHRATQK SYHMEKKSPS VYSKSQYV
//
