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Database: UniProt
Entry: W5NLM4_LEPOC
LinkDB: W5NLM4_LEPOC
Original site: W5NLM4_LEPOC 
ID   W5NLM4_LEPOC            Unreviewed;       216 AA.
AC   W5NLM4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Claudin-3-like {ECO:0000313|Ensembl:ENSLOCP00000021533.1};
GN   Name=CLDN3 {ECO:0000313|Ensembl:ENSLOCP00000021533.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000021533.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000021533.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC       {ECO:0000256|ARBA:ARBA00008295}.
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DR   EMBL; AHAT01005728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015223339.1; XM_015367853.1.
DR   AlphaFoldDB; W5NLM4; -.
DR   STRING; 7918.ENSLOCP00000021533; -.
DR   Ensembl; ENSLOCT00000021570.1; ENSLOCP00000021533.1; ENSLOCG00000017428.1.
DR   GeneID; 102699254; -.
DR   KEGG; loc:102699254; -.
DR   CTD; 81582; -.
DR   eggNOG; ENOG502QRZ8; Eukaryota.
DR   GeneTree; ENSGT00940000162095; -.
DR   HOGENOM; CLU_076370_1_2_1; -.
DR   InParanoid; W5NLM4; -.
DR   OMA; RYGPPSK; -.
DR   OrthoDB; 4040914at2759; -.
DR   Proteomes; UP000018468; Linkage group LG22.
DR   Bgee; ENSLOCG00000017428; Expressed in intestine and 10 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF112; CLAUDIN-3; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   216 AA;  23366 MW;  E23A3BC32399DEE7 CRC64;
     MASLGLEILG VALAVFGWIG SILACALPMW RVSAFIGINI MTAQIFWEGI WMSCVVQSTG
     QMQCKVYDSM LALPQDLQAA RALEVISIIL GFLGILVSIV GAKCTSCIED EVTKSRVMIT
     TGVTFNIASI MQLIPVSWSA NTIIREFYSP IIPEAQKREI GASLYIGWAA AALLLLGGSI
     LCCSCPPRET KYTPPRLAYS TARSGVPSGY DRKDYV
//
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