OCLN_RAT
ID OCLN_RAT Reviewed; 523 AA.
AC Q6P6T5; Q9Z303;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Occludin;
GN Name=Ocln;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11810420; DOI=10.1007/s007950050003;
RA Atsumi Si S., Kokai Y., Tobioka H., Kuwahara K., Kuwabara H., Takakuwa Y.,
RA Sasaki Ki K., Sawada N., Mitaka T., Mochizuki Y., Imai K., Mori M.;
RT "Occludin modulates organization of perijunctional circumferential actin in
RT rat endothelial cells.";
RL Med. Electron Microsc. 32:11-19(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier. May be involved in the
CC organization of actin in endothelial cells.
CC {ECO:0000269|PubMed:11810420}.
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 -!- INTERACTION:
CC Q6P6T5; O35346: Ptk2; NbExp=2; IntAct=EBI-15348891, EBI-6252940;
CC Q6P6T5; F1M4A0: Tjp1; NbExp=2; IntAct=EBI-15348891, EBI-15783773;
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 -!- DOMAIN: The C-terminal is cytoplasmic and is important for interaction
CC with ZO-1. Sufficient 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; AB016425; BAA36681.1; -; mRNA.
DR EMBL; BC062037; AAH62037.1; -; mRNA.
DR RefSeq; NP_112619.2; NM_031329.2.
DR RefSeq; XP_006231915.1; XM_006231853.3.
DR RefSeq; XP_006231916.1; XM_006231854.3.
DR RefSeq; XP_006231917.1; XM_006231855.3.
DR AlphaFoldDB; Q6P6T5; -.
DR SMR; Q6P6T5; -.
DR BioGRID; 249716; 2.
DR CORUM; Q6P6T5; -.
DR DIP; DIP-48891N; -.
DR IntAct; Q6P6T5; 2.
DR STRING; 10116.ENSRNOP00000024674; -.
DR iPTMnet; Q6P6T5; -.
DR PhosphoSitePlus; Q6P6T5; -.
DR PaxDb; Q6P6T5; -.
DR PRIDE; Q6P6T5; -.
DR Ensembl; ENSRNOT00000024674; ENSRNOP00000024674; ENSRNOG00000018297.
DR GeneID; 83497; -.
DR KEGG; rno:83497; -.
DR CTD; 100506658; -.
DR RGD; 620089; Ocln.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR GeneTree; ENSGT00940000155771; -.
DR HOGENOM; CLU_039628_1_0_1; -.
DR InParanoid; Q6P6T5; -.
DR OMA; PEQDHYE; -.
DR OrthoDB; 710557at2759; -.
DR TreeFam; TF326161; -.
DR Reactome; R-RNO-351906; Apoptotic cleavage of cell adhesion proteins.
DR PRO; PR:Q6P6T5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000018297; Expressed in jejunum and 18 other tissues.
DR Genevisible; Q6P6T5; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; ISO:RGD.
DR GO; GO:0140459; P:response to Gram-positive bacterium; IEP:RGD.
DR GO; GO:0070673; P:response to interleukin-18; IMP:RGD.
DR GO; GO:0120193; P:tight junction organization; ISO:RGD.
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:SF4; PTHR23288:SF4; 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..523
FT /note="Occludin"
FT /id="PRO_0000236103"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..269
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 415..523
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 433..489
FT /evidence="ECO:0000255"
FT COMPBIAS 364..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 369
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 399
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 403
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 404
FT /note="Phosphothreonine; by PKC/PRKCH"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 405
FT /note="Phosphothreonine; by PKC/PRKCH"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT DISULFID 216..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 276
FT /note="K -> R (in Ref. 1; BAA36681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59186 MW; A31E007B58AEA5B5 CRC64;
MSVRPFESPP PYRPDEFKPN HYAPSNDMYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LVIVMCIAVF ACVASTLAWD RAYGTGIFGG SMNYPYGSGF GSYGGGFGGY
GYGYGYGYGG YTDPRAAKGF LLAMAAFCFI ASLVIFVTSV IRSGMSRTRR YYLIVIIVSA
ILGIMVFIAT IVYIMGVNPT AQASGSMYGS QIYTICSQFY TPGGTGLYVD QYLYHYCVVD
PQEAIAIVLG FMIIVAFALI IVFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN
VSAGTQDMPP PPSDYAERVD SPMAYSSNGK VNGKRSYPDS LYKSPPLVPE VAQEIPLTLS
VDDFRQPRYS SNDNLETPSK RTPTKGKAGK AKRTDPDHYE TDYTTGGESC DELEEDWLRE
YPPITSDQQR QLYKRNFDAG LQEYKSLLAE LDEVNKELSR LDRELDDYRE ESEEYMAAAD
EYNRLKQVKG SADYKSKKNY CKQLKSKLSH IKRMVGDYDR RKT
