OCLN_CHICK
ID OCLN_CHICK Reviewed; 504 AA.
AC Q91049;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Occludin;
GN Name=OCLN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic brain;
RX PubMed=8276896; DOI=10.1083/jcb.123.6.1777;
RA Furuse M., Hirase T., Itoh M., Nagafuchi A., Yonemura S., Tsukita S.,
RA Tsukita S.;
RT "Occludin: a novel integral membrane protein localizing at tight
RT junctions.";
RL J. Cell Biol. 123:1777-1788(1993).
RN [2]
RP PHOSPHORYLATION AT TYR-379 AND TYR-383 BY SRC, IDENTIFICATION BY MASS
RP SPECTROMETRY, MUTAGENESIS OF TYR-379 AND TYR-383, AND INTERACTION WITH TJP1
RP AND TJP3.
RX PubMed=19017651; DOI=10.1074/jbc.m804783200;
RA Elias B.C., Suzuki T., Seth A., Giorgianni F., Kale G., Shen L.,
RA Turner J.R., Naren A., Desiderio D.M., Rao R.;
RT "Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its
RT interaction with ZO-1 and destabilizes its assembly at the tight
RT junctions.";
RL J. Biol. Chem. 284:1559-1569(2009).
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier. Interacts with ZO-1.
CC -!- SUBUNIT: Interacts with TJP1 and TJP3. {ECO:0000269|PubMed:19017651}.
CC -!- INTERACTION:
CC Q91049; Q9PTD7: cgn; Xeno; NbExp=2; IntAct=EBI-79619, EBI-79525;
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. Highly expressed in lung and liver. Expressed at a
CC lower level in brain.
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. The second extracellular domain may also be implicated in the
CC permeability barrier function of the tight junction.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; D21837; BAA04865.1; -; mRNA.
DR PIR; A49467; A49467.
DR RefSeq; NP_990459.1; NM_205128.1.
DR AlphaFoldDB; Q91049; -.
DR SMR; Q91049; -.
DR IntAct; Q91049; 1.
DR STRING; 9031.ENSGALP00000041881; -.
DR TCDB; 9.B.41.1.3; the occludin (occludin) family.
DR iPTMnet; Q91049; -.
DR GeneID; 396026; -.
DR KEGG; gga:396026; -.
DR CTD; 100506658; -.
DR VEuPathDB; HostDB:geneid_396026; -.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR InParanoid; Q91049; -.
DR OrthoDB; 642097at2759; -.
DR PhylomeDB; Q91049; -.
DR PRO; PR:Q91049; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..504
FT /note="Occludin"
FT /id="PRO_0000146742"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..253
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 396..504
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 324..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..385
FT /note="Interaction with TJP1"
FT /evidence="ECO:0000269|PubMed:19017651"
FT COILED 412..471
FT /evidence="ECO:0000255"
FT COMPBIAS 342..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19017651"
FT MOD_RES 383
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:19017651"
FT DISULFID 204..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 379
FT /note="Y->D: Lower binding to TJP1, higher binding to TJP3
FT and decrease in phosphorylation. Lower binding to TJP1 and
FT TJP3, loss of phosphorylation and loss of regulation of
FT TJP1 binding; when associated with D-383."
FT /evidence="ECO:0000269|PubMed:19017651"
FT MUTAGEN 379
FT /note="Y->F: Decrease in phosphorylation and decrease in
FT regulation of TJP1 binding. Loss of phosphorylation and
FT loss of regulation of TJP1 binding; when associated with F-
FT 383."
FT /evidence="ECO:0000269|PubMed:19017651"
FT MUTAGEN 383
FT /note="Y->D: Lower binding to TJP1 and TJP3, decrease in
FT phosphorylation and loss of regulation of TJP1 and TJP3
FT binding. Lower binding to TJP1 and TJP3, loss of
FT phosphorylation and loss of regulation of TJP1 binding;
FT when associated with D-379."
FT /evidence="ECO:0000269|PubMed:19017651"
FT MUTAGEN 383
FT /note="Y->F: Decrease in phosphorylation and loss of
FT regulation of TJP1 binding. Loss of phosphorylation and
FT loss of regulation of TJP1 binding; when associated with F-
FT 379."
FT /evidence="ECO:0000269|PubMed:19017651"
SQ SEQUENCE 504 AA; 55864 MW; AD0352A45A0231FF CRC64;
MFSKKSYDGP PAGYGPPTGY GAPTADYGYG SPPPGSYYVD DAPQLFYKWT SPPGAVRGLQ
AGVLVLCIAI FACVASTLAW DYGYGLGGAY GTGLGGFYGS NYYGSGLSYS YGYGGYYGGV
NQRTANGFMI AMAVLCFLAQ LGLLVAALSK SGATRSRRFY LAVLVLSAVL AFVMLIASIV
YIMGVNPQAQ MSSGYYYSPL LAMCSQAYGS TYLNQYIYHY CTVDPQEAVA AVCGFLIVIL
LCLICFFAQK TRSKIWRYGK ANIYWDRAPV VQEGPDVEEW VKNVADGASV QDETATLAYS
EKPTSPVAAP PYSYVPPPSA GYYPSGTYSS RGDQPDRALS ASPVHGEEEE EKGKDQPSRP
PARRGRRRRR NPELDESQYE TDYTTAVESS DERDQEQWAS LYPPITSDGA RQRYKQEFDT
DLKRYKQLCA EMDSINDRLN QLSRRLDSIT EDSPQYQDVA EEYNQLKDLK RSPDYQSKKQ
ESKVLRNKLF HIKRMVSAYD KVRG
