ID A0A3P8WN27_CYNSE Unreviewed; 551 AA.
AC A0A3P8WN27;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772, ECO:0000256|PIRNR:PIRNR005993};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000026065.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000026065.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000026065.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier.
CC {ECO:0000256|PIRNR:PIRNR005993}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR005993};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR005993}. Cell
CC junction, tight junction {ECO:0000256|PIRNR:PIRNR005993}. 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|PIRNR:PIRNR005993,
CC ECO:0000256|PROSITE-ProRule:PRU01324}.
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DR RefSeq; XP_008330735.1; XM_008332513.2.
DR RefSeq; XP_008330743.1; XM_008332521.2.
DR RefSeq; XP_016886593.1; XM_017031104.1.
DR Ensembl; ENSCSET00000026406.1; ENSCSEP00000026065.1; ENSCSEG00000016641.1.
DR Ensembl; ENSCSET00000026419.1; ENSCSEP00000026078.1; ENSCSEG00000016641.1.
DR GeneID; 103394989; -.
DR KEGG; csem:103394989; -.
DR GeneTree; ENSGT00940000165052; -.
DR OrthoDB; 5360956at2759; -.
DR Proteomes; UP000265120; Chromosome 2.
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:SF6; 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 PIRSF; PIRSF005993; Occludin; 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 ECO:0000256|PIRNR:PIRNR005993};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR005993-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005993};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427,
KW ECO:0000256|PIRNR:PIRNR005993};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR005993};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..290
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 443..551
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 351..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 365..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 230..258
FT /evidence="ECO:0000256|PIRSR:PIRSR005993-1"
SQ SEQUENCE 551 AA; 61906 MW; BD26CC1A0E9B44DC CRC64;
MFSGMFEKQH YDSPPVYSPP FSSPSNKSYG APGSFHGPQS DYNAYPPAPG SYYIEDKPQH
FYKWLSPPGI IKAMMVTVVV LCVAIFACVA STLMWDMQYG YGAGGGYYGS GLGYGGGYSG
GSYGSGYGGY GGYGGYGNGN YYGSYVSPYS AKTAMIAMAA INFVVSLGFF ISSFSKSPMF
RSRKFFLAVL ITCIIVGLLQ GIINIVYIVG VNPMAQGSSS MMYNPMLMMC QNLYQTTYSQ
MGGVGGFPIY NQYLYHYCFV DPQEGIAMAC GFLVVIALGV AAFFAFKTRG KIWRYGKPNI
YWEEPLVGGK ASEGRDVEEW VNNVEENRSV QDAPTLLVSE KGAGLLNSSA NSVLSFPPHK
TNSSVYKDEP YDNEYSERTI SRPSEAHSHR GRTSSSLSEE TSGGRKPSAN RGKRRRRNPD
FDESQYETEY TTGGETGNEL DTEEWESSYP EITTDVQRQD YKREFDADLR NYKRMCAEMD
DMNDQLNKLS RQLDTLDDTS DKYQDVAEEY NRLKDLKQTP DYQFKKRECR RLRRKLFHIK
RMVKNYDKNH S
//
