ID A0A3N0YN65_ANAGA Unreviewed; 188 AA.
AC A0A3N0YN65;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Claudin {ECO:0000256|RuleBase:RU060637};
GN ORFNames=DPX16_13358 {ECO:0000313|EMBL:ROL47643.1};
OS Anabarilius grahami (Kanglang fish) (Barilius grahami).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Xenocypridinae incertae sedis; Anabarilius.
OX NCBI_TaxID=495550 {ECO:0000313|EMBL:ROL47643.1, ECO:0000313|Proteomes:UP000281406};
RN [1] {ECO:0000313|EMBL:ROL47643.1, ECO:0000313|Proteomes:UP000281406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-KIZ {ECO:0000313|EMBL:ROL47643.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:ROL47643.1};
RA Jiang W.;
RT "Genome assembly for a Yunnan-Guizhou Plateau 3E fish, Anabarilius grahami
RT (Regan), and its evolutionary and genetic applications.";
RL Submitted (OCT-2018) 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}.
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:ROL47643.1}.
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DR EMBL; RJVU01035392; ROL47643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0YN65; -.
DR Proteomes; UP000281406; 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:SF192; CLAUDIN-RELATED; 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:UP000281406};
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 77..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 114..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU060637"
SQ SEQUENCE 188 AA; 19831 MW; 7D0CB02D42650392 CRC64;
MRSRQILAVC LAVLGLCGTI LVCALPMWKV TAFVGANIVT AQVFWEGLWM NCVLQSTSHM
QCKVYDSVLA LTKDLQAARA LICASIAVSV VAVGLSVVGA NCTNFYREER LKKANLGIAA
GAVYIVAGVT CLVAVSWSAY VIIVDFYNPL AAAGRKGELG ASIYVGWVAG VLLIVGGGLF
ISTYSSRC
//