ID A0A3Q1IWX2_ANATE Unreviewed; 483 AA.
AC A0A3Q1IWX2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000026682.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000026682.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family.
CC {ECO:0000256|ARBA:ARBA00009171, ECO:0000256|PROSITE-ProRule:PRU01324}.
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DR AlphaFoldDB; A0A3Q1IWX2; -.
DR Ensembl; ENSATET00000027106.2; ENSATEP00000026682.2; ENSATEG00000018404.2.
DR GeneTree; ENSGT00940000167296; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:InterPro.
DR Gene3D; 6.10.140.340; -; 1.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR002958; Occludin.
DR InterPro; IPR010844; Occludin_ELL.
DR PANTHER; PTHR23288:SF38; OCCLUDIN; 1.
DR PANTHER; PTHR23288; OCCLUDIN AND RNA POLYMERASE II ELONGATION FACTOR ELL; 1.
DR Pfam; PF01284; MARVEL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR PRINTS; PR01258; OCCLUDIN.
DR SUPFAM; SSF144292; occludin/ELL-like; 1.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00581}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00581};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..254
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 383..483
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 331..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 54939 MW; A52944229D05E77A CRC64;
WLLRPHQDVT IANMSPTPTT SLQDSYYMEE RPQHFYRWFS PPGFVKTFQG ATVLICFLIF
SCVASTLVWD MNGFGYGGYG SIGGVAGTGS GYYGGSYGYG NSYMTPHSAK SAMISMAAIN
FLVSLGFLTG SFSRSRMTRG CRFYLIVFIC DIILAVLQVS GIIDIIFVIG VNPMSQSSQS
MLYNPMLMMC QNIQGSPSLS GSVGAGFPGG FLMYNQYLQH YCYMDPEEAV ALVLGLMVVL
ALSLSAYYAY KTRSKIWRHG KANIYWDEPV ARPSDGQDVQ DWVSKVKFIS SSGTLGMIVC
QQSLTVKDRS KTVKPLYQDS RVVVCSSSSS DETESIWKPP DYHVEREKRK DREPRSAAQK
TVEYQYETGY TTEDTGNELD HKDYLYRLYP EITSDEQRQQ YKKEFDSDLA RYKSLCAEMD
GISDQMHNLS RELDTLDEGS MKYEVQKNKR EPDYQAKKKR CKELRQKLFH IKRLVKLYDR
HLC
//