ID   OCLN_POTTR              Reviewed;         489 AA.
AC   Q28793;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Occludin;
GN   Name=OCLN;
OS   Potorous tridactylus (Potoroo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Potoroidae; Potorous.
OX   NCBI_TaxID=9310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=8601611; DOI=10.1083/jcb.133.1.43;
RA   Ando-Akatsuka Y., Saitou M., Hirase T., Kishi M., Sakakibara A., Itoh M.,
RA   Yonemura S., Furuse M., Tsukita S.;
RT   "Interspecies diversity of the occludin sequence: cDNA cloning of human,
RT   mouse, dog, and rat-kangaroo homologues.";
RL   J. Cell Biol. 133:43-47(1996).
CC   -!- FUNCTION: May play a role in the formation and regulation of the tight
CC       junction (TJ) paracellular permeability barrier.
CC   -!- SUBUNIT: Interacts with TJP1/ZO1. Interacts with VAPA. Interacts with
CC       CLDN1, CLDN6, CLDN9, CLDN11, CLDN12 and CLDN17. Interacts with PLSCR1.
CC       Interacts with LSR, ILDR1 and ILDR2. {ECO:0000250|UniProtKB:Q16625}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16625};
CC       Multi-pass membrane protein {ECO:0000255}. Cell junction, tight
CC       junction {ECO:0000250|UniProtKB:Q16625}.
CC   -!- TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and
CC       endothelial cells.
CC   -!- DOMAIN: The C-terminal is cytoplasmic and is important for interaction
CC       with ZO-1. Necessary for the tight junction localization. Involved in
CC       the regulation of the permeability barrier function of the tight
CC       junction (By similarity). {ECO:0000250}.
CC   -!- PTM: Dephosphorylated by PTPRJ. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR   EMBL; U49183; AAC48565.1; -; mRNA.
DR   AlphaFoldDB; Q28793; -.
DR   SMR; Q28793; -.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IEA:InterPro.
DR   InterPro; IPR031176; ELL/occludin.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR002958; Occludin.
DR   InterPro; IPR010844; Occludin_ELL.
DR   PANTHER; PTHR23288; PTHR23288; 1.
DR   PANTHER; PTHR23288:SF6; PTHR23288:SF6; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   Pfam; PF07303; Occludin_ELL; 1.
DR   PIRSF; PIRSF005993; Occludin; 1.
DR   PRINTS; PR01258; OCCLUDIN.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS51980; OCEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Coiled coil; Disulfide bond; Membrane;
KW   Phosphoprotein; Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN           1..489
FT                   /note="Occludin"
FT                   /id="PRO_0000146741"
FT   TOPO_DOM        1..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..222
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..248
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   DOMAIN          381..489
FT                   /note="OCEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT   REGION          308..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..434
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        362..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61146"
FT   MOD_RES         285
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61146"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         364
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         368
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         369
FT                   /note="Phosphothreonine; by PKC/PRKCH"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         370
FT                   /note="Phosphothreonine; by PKC/PRKCH"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   MOD_RES         457
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16625"
FT   DISULFID        196..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   489 AA;  54076 MW;  4F0CA45A41094860 CRC64;
     MMYEKRSYTG YGHPSSHYDY PPPSGPPGSF YLADVPPQHF YQWRSPPGIV RILQGSVVIL
     CLVIFACVAS TLAWEYYGSG GLLGYGGGLG SYYNGYYGGY NGYYYGGLTN PRAANGFMIA
     MAVLCFLVTL GLVIAGLSKA SGARSRRFYL LVAVLSGLLA FVMLIASIVY VVGVNPRAGL
     GASSGSLYYN QMLMLCNQMM SPVAGGIMNQ YLYHYCMVDP QEAVAIVCGF LTVILLCVIC
     YFAQKTRHKI WKYGKPNIFW DKPLATAEGP NVEEWVKNVS GDVGTQDETA TLAYSEKPIS
     PLTSAFLPAQ ENGYGHSTPS SPSVPPPEGP SPPEEKDKGS VSRPPARRGH RQRPRPTGLE
     ESQYETDYTT AAESSGEQNR DDWASLYPPI ISDAIRQTYK AEFNNDLQRY KALCAEMDDI
     GTQLRQLSHE LDCLPEGSLR YQGVAEEYNR LKDLKRSPEY QSKKLETQSL RDKLCHIKRM
     VGGYDQSRS