ID I3K1F9_ORENI Unreviewed; 258 AA.
AC I3K1F9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Claudin-10-like {ECO:0000313|Ensembl:ENSONIP00000014954.1};
GN Name=CLDN10 {ECO:0000313|Ensembl:ENSONIP00000014954.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000014954.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000014954.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. 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}.
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DR RefSeq; XP_005449998.1; XM_005449941.3.
DR AlphaFoldDB; I3K1F9; -.
DR STRING; 8128.ENSONIP00000014954; -.
DR Ensembl; ENSONIT00000014966.2; ENSONIP00000014954.1; ENSONIG00000011879.2.
DR GeneID; 100700264; -.
DR KEGG; onl:100700264; -.
DR CTD; 563994; -.
DR eggNOG; ENOG502QWMH; Eukaryota.
DR GeneTree; ENSGT00940000155232; -.
DR HOGENOM; CLU_076370_0_1_1; -.
DR InParanoid; I3K1F9; -.
DR OMA; SWWANKV; -.
DR OrthoDB; 4040914at2759; -.
DR TreeFam; TF331936; -.
DR Proteomes; UP000005207; Linkage group LG23.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:SF115; CLAUDIN; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 237..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 258 AA; 28235 MW; D38CF40CD358A49E CRC64;
MKYRTVVMYV EIGCFVSCLC GWILVSSTLP TEYWTFSEVG TLVLTTSNYY SNLWMDCISD
TTGVSDCKYY PSMLALPAFL HACRALAVCA VITGFFGGVL TLIGMKCTKI GGTEIVNSRV
TFSGAITYLA SGGCGMITYS WWANRVITEF KDPNFRAQKF ELGAAIFVGW GGSLLLICAG
AVLAYLSGKE LVPSCISSNQ RPERPVSYAT ARTMRTYMMP PPSSRVTLVP PLYNKGMNGR
TTRATNKTDQ TLGRDSFV
//
