ID OCLN_HUMAN Reviewed; 522 AA. AC Q16625; B5BU70; D2DU64; D2DU65; D2IGC0; D2IGC1; E2CYV9; Q5U1V4; Q8N6K1; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Occludin; GN Name=OCLN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Colon carcinoma; 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). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, SUBCELLULAR LOCATION, AND RP TOPOLOGY. RC TISSUE=Liver; RX PubMed=9175707; DOI=10.1242/jcs.110.9.1113; RA Van Itallie C.M., Anderson J.M.; RT "Occludin confers adhesiveness when expressed in fibroblasts."; RL J. Cell Sci. 110:1113-1121(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND ALTERNATIVE RP SPLICING. RC TISSUE=Liver; RX PubMed=20463075; DOI=10.1128/jvi.00196-10; RA Kohaar I., Ploss A., Korol E., Mu K., Schoggins J.W., O'Brien T.R., RA Rice C.M., Prokunina-Olsson L.; RT "Splicing diversity of the human OCLN gene and its biological significance RT for hepatitis C virus entry."; RL J. Virol. 84:6987-6994(2010). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fukasawa M., Toyota T., Yoshitsugu K., Yoshikawa T.; RT "Genomic structure of occludin gene."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Lung; 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 [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH VAPA. RX PubMed=10523508; DOI=10.1242/jcs.112.21.3723; RA Lapierre L.A., Tuma P.L., Navarre J., Goldenring J.R., Anderson J.M.; RT "VAP-33 localizes to both an intracellular vesicle population and with RT occludin at the tight junction."; RL J. Cell Sci. 112:3723-3732(1999). RN [9] RP ALTERNATIVE SPLICING (ISOFORM 2). RX PubMed=12118072; DOI=10.1242/jcs.115.15.3171; RA Ghassemifar M.R., Sheth B., Papenbrock T., Leese H.J., Houghton F.D., RA Fleming T.P.; RT "Occludin TM4(-): an isoform of the tight junction protein present in RT primates lacking the fourth transmembrane domain."; RL J. Cell Sci. 115:3171-3180(2002). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [12] RP INTERACTION WITH TJP1, PHOSPHORYLATION AT TYR-398 AND TYR-402, MUTAGENESIS RP OF TYR-398 AND TYR-402, AND SUBCELLULAR LOCATION. 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). RN [13] RP PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ, AND SUBCELLULAR LOCATION. RX PubMed=19332538; DOI=10.1074/jbc.m901901200; RA Sallee J.L., Burridge K.; RT "Density-enhanced phosphatase 1 regulates phosphorylation of tight junction RT proteins and enhances barrier function of epithelial cells."; RL J. Biol. Chem. 284:14997-15006(2009). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-403 AND THR-404, AND RP MUTAGENESIS OF THR-404. RX PubMed=19114660; DOI=10.1073/pnas.0802741106; RA Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F., RA Desiderio D., Guntaka R., Rao R.; RT "PKC eta regulates occludin phosphorylation and epithelial tight junction RT integrity."; RL Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009). RN [15] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=19182773; DOI=10.1038/nature07684; RA Ploss A., Evans M.J., Gaysinskaya V.A., Panis M., You H., de Jong Y.P., RA Rice C.M.; RT "Human occludin is a hepatitis C virus entry factor required for infection RT of mouse cells."; RL Nature 457:882-886(2009). RN [16] RP INTERACTION WITH CLDN1; CLDN6; CLDN9; CLDN11; CLDN12 AND CLDN17, AND RP FUNCTION (MICROBIAL INFECTION). RX PubMed=20375010; DOI=10.1074/jbc.m110.104836; RA Harris H.J., Davis C., Mullins J.G., Hu K., Goodall M., Farquhar M.J., RA Mee C.J., McCaffrey K., Young S., Drummer H., Balfe P., McKeating J.A.; RT "Claudin association with CD81 defines hepatitis C virus entry."; RL J. Biol. Chem. 285:21092-21102(2010). RN [17] RP INTERACTION WITH PLSCR1. RX PubMed=21806988; DOI=10.1016/j.febslet.2011.07.019; RA Gong Q., Cheng M., Chen H., Liu X., Si Y., Yang Y., Yuan Y., Jin C., RA Yang W., He F., Wang J.; RT "Phospholipid scramblase 1 mediates hepatitis C virus entry into host RT cells."; RL FEBS Lett. 585:2647-2652(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-369 AND SER-370, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; TYR-368 AND SER-408, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-522, AND PHOSPHORYLATION AT RP SER-490. RX PubMed=19125584; DOI=10.1021/pr7007913; RA Sundstrom J.M., Tash B.R., Murakami T., Flanagan J.M., Bewley M.C., RA Stanley B.A., Gonsar K.B., Antonetti D.A.; RT "Identification and analysis of occludin phosphosites: a combined mass RT spectrometry and bioinformatics approach."; RL J. Proteome Res. 8:808-817(2009). RN [21] RP VARIANT PTORCH1 SER-219. RX PubMed=20727516; DOI=10.1016/j.ajhg.2010.07.012; RA O'Driscoll M.C., Daly S.B., Urquhart J.E., Black G.C., Pilz D.T., RA Brockmann K., McEntagart M., Abdel-Salam G., Zaki M., Wolf N.I., RA Ladda R.L., Sell S., D'Arrigo S., Squier W., Dobyns W.B., Livingston J.H., RA Crow Y.J.; RT "Recessive mutations in the gene encoding the tight junction protein RT occludin cause band-like calcification with simplified gyration and RT polymicrogyria."; RL Am. J. Hum. Genet. 87:354-364(2010). RN [22] RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=23532847; DOI=10.1074/jbc.m113.459875; RA Sumitomo T., Nakata M., Higashino M., Terao Y., Kawabata S.; RT "Group A streptococcal cysteine protease cleaves epithelial junctions and RT contributes to bacterial translocation."; RL J. Biol. Chem. 288:13317-13324(2013). RN [23] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH LSR; ILDR1 RP AND ILDR2. RX PubMed=23239027; DOI=10.1242/jcs.116442; RA Higashi T., Tokuda S., Kitajiri S., Masuda S., Nakamura H., Oda Y., RA Furuse M.; RT "Analysis of the 'angulin' proteins LSR, ILDR1 and ILDR2--tricellulin RT recruitment, epithelial barrier function and implication in deafness RT pathogenesis."; RL J. Cell Sci. 126:966-977(2013). RN [24] RP DISULFIDE BOND. RX PubMed=23923978; DOI=10.1089/ars.2013.5288; RA Bellmann C., Schreivogel S., Gunther R., Dabrowski S., Schumann M., RA Wolburg H., Blasig I.E.; RT "Highly conserved cysteines are involved in the oligomerization of RT occludin-redox dependency of the second extracellular loop."; RL Antioxid. Redox Signal. 20:855-867(2014). CC -!- FUNCTION: May play a role in the formation and regulation of the tight CC junction (TJ) paracellular permeability barrier. It is able to induce CC adhesion when expressed in cells lacking tight junctions. CC {ECO:0000269|PubMed:19114660}. CC -!- FUNCTION: (Microbial infection) Acts as a coreceptor for hepatitis C CC virus (HCV) in hepatocytes. {ECO:0000269|PubMed:19182773, CC ECO:0000269|PubMed:20375010}. CC -!- SUBUNIT: Interacts with TJP1/ZO1 (PubMed:19017651). Interacts with VAPA CC (PubMed:10523508). Interacts with CLDN1, CLDN6, CLDN9, CLDN11, CLDN12 CC and CLDN17 (PubMed:20375010). Interacts with PLSCR1 (PubMed:21806988). CC Interacts with LSR, ILDR1 and ILDR2 (PubMed:23239027). Interacts with CC TJP2/ZO2 (By similarity). {ECO:0000250|UniProtKB:Q61146, CC ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19017651, CC ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:21806988, CC ECO:0000269|PubMed:23239027}. CC -!- INTERACTION: CC Q16625; Q9BXN2: CLEC7A; NbExp=3; IntAct=EBI-2903088, EBI-3939278; CC Q16625; P49674: CSNK1E; NbExp=8; IntAct=EBI-2903088, EBI-749343; CC Q16625; P50570-2: DNM2; NbExp=3; IntAct=EBI-2903088, EBI-10968534; CC Q16625; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2903088, EBI-11721746; CC Q16625; P19404: NDUFV2; NbExp=3; IntAct=EBI-2903088, EBI-713665; CC Q16625; O15162: PLSCR1; NbExp=2; IntAct=EBI-2903088, EBI-740019; CC Q16625; Q8N205: SYNE4; NbExp=3; IntAct=EBI-2903088, EBI-7131783; CC Q16625-1; P24723: PRKCH; NbExp=2; IntAct=EBI-16115673, EBI-2865850; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19017651, CC ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:9175707}; Multi-pass CC membrane protein {ECO:0000255}. Cell junction, tight junction CC {ECO:0000269|PubMed:10523508, ECO:0000269|PubMed:19017651, CC ECO:0000269|PubMed:19114660, ECO:0000269|PubMed:19332538, CC ECO:0000269|PubMed:23239027, ECO:0000269|PubMed:9175707}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=WT-OCLN, TM4(+); CC IsoId=Q16625-1; Sequence=Displayed; CC Name=2; Synonyms=OCLN-ex4del, TM4(-); CC IsoId=Q16625-2; Sequence=VSP_043877; CC Name=3; Synonyms=OCLN-ex7ext; CC IsoId=Q16625-3; Sequence=VSP_043879; CC Name=4; Synonyms=OCLN-ex3del, OCLN-ex3pdel; CC IsoId=Q16625-4; Sequence=VSP_043872; CC Name=5; Synonyms=OCLN-ex3-4del; CC IsoId=Q16625-5; Sequence=VSP_043872, VSP_043878; CC Name=6; Synonyms=OCLN-ex3p-9pdel; CC IsoId=Q16625-6; Sequence=VSP_043873, VSP_043875, VSP_043876; CC Name=7; Synonyms=OCLN-ex3p-7pdel; CC IsoId=Q16625-7; Sequence=VSP_043874, VSP_043876; CC -!- TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and CC endothelial cells. Highly expressed in kidney. Not detected in testis. CC {ECO:0000269|PubMed:23239027}. 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). The first extracellular loop participates in CC an adhesive interaction. {ECO:0000250, ECO:0000269|PubMed:9175707}. CC -!- PTM: Dephosphorylated by PTPRJ. The tyrosine phosphorylation on Tyr-398 CC and Tyr-402 reduces its ability to interact with TJP1. Phosphorylation CC at Ser-490 also attenuates the interaction with TJP1. CC {ECO:0000269|PubMed:19017651, ECO:0000269|PubMed:19114660, CC ECO:0000269|PubMed:19125584, ECO:0000269|PubMed:19332538}. CC -!- PTM: (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading CC to its degradation (PubMed:23532847). Degradation by SpeB promotes CC bacterial translocation across the host epithelial barrier CC (PubMed:23532847). {ECO:0000269|PubMed:23532847}. CC -!- DISEASE: Pseudo-TORCH syndrome 1 (PTORCH1) [MIM:251290]: An autosomal CC recessive neurologic disorder with characteristic clinical and CC neuroradiologic features that mimic intrauterine TORCH infection in the CC absence of evidence of infection. Affected individuals have congenital CC microcephaly, intracranial calcifications, and severe developmental CC delay. {ECO:0000269|PubMed:20727516}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Occludin entry; CC URL="https://en.wikipedia.org/wiki/Occludin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49184; AAC50451.1; -; mRNA. DR EMBL; U53823; AAB00195.1; -; mRNA. DR EMBL; FJ786083; ACT53743.1; -; mRNA. DR EMBL; FJ786084; ACT53744.1; -; mRNA. DR EMBL; AF400630; AAL47094.1; -; Genomic_DNA. DR EMBL; AF400623; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400624; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400625; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400626; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400627; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400628; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; AF400629; AAL47094.1; JOINED; Genomic_DNA. DR EMBL; GQ225096; ACT83431.1; -; mRNA. DR EMBL; GQ225097; ACT83432.1; -; mRNA. DR EMBL; GQ225098; ACT83433.1; -; mRNA. DR EMBL; GQ402517; ACZ80515.1; -; mRNA. DR EMBL; AB451306; BAG70120.1; -; mRNA. DR EMBL; AB451437; BAG70251.1; -; mRNA. DR EMBL; AC145146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC147575; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029886; AAH29886.1; -; mRNA. DR EMBL; BK001650; DAA01837.1; -; mRNA. DR CCDS; CCDS4006.1; -. [Q16625-1] DR CCDS; CCDS54864.1; -. [Q16625-4] DR CCDS; CCDS93725.1; -. [Q16625-2] DR PIR; G02533; G02533. DR RefSeq; NP_001192183.1; NM_001205254.1. [Q16625-1] DR RefSeq; NP_001192184.1; NM_001205255.1. [Q16625-4] DR RefSeq; NP_002529.1; NM_002538.3. [Q16625-1] DR RefSeq; XP_016864402.1; XM_017008913.1. [Q16625-2] DR RefSeq; XP_016864403.1; XM_017008914.1. DR PDB; 1WPA; X-ray; 1.50 A; A=413-522. DR PDB; 1XAW; X-ray; 1.45 A; A=383-522. DR PDB; 3G7C; X-ray; 2.00 A; A=416-522. DR PDBsum; 1WPA; -. DR PDBsum; 1XAW; -. DR PDBsum; 3G7C; -. DR AlphaFoldDB; Q16625; -. DR SMR; Q16625; -. DR BioGRID; 111004; 523. DR DIP; DIP-42791N; -. DR IntAct; Q16625; 57. DR MINT; Q16625; -. DR STRING; 9606.ENSP00000347379; -. DR TCDB; 9.B.41.1.1; the occludin (occludin) family. DR GlyGen; Q16625; 2 sites. DR iPTMnet; Q16625; -. DR PhosphoSitePlus; Q16625; -. DR SwissPalm; Q16625; -. DR BioMuta; OCLN; -. DR DMDM; 3914196; -. DR EPD; Q16625; -. DR jPOST; Q16625; -. DR MassIVE; Q16625; -. DR MaxQB; Q16625; -. DR PaxDb; 9606-ENSP00000347379; -. DR PeptideAtlas; Q16625; -. DR ProteomicsDB; 60966; -. [Q16625-1] DR ProteomicsDB; 60967; -. [Q16625-2] DR ProteomicsDB; 60968; -. [Q16625-3] DR ProteomicsDB; 60969; -. [Q16625-4] DR ProteomicsDB; 60970; -. [Q16625-5] DR ProteomicsDB; 60971; -. [Q16625-6] DR ProteomicsDB; 60972; -. [Q16625-7] DR Pumba; Q16625; -. DR TopDownProteomics; Q16625-3; -. [Q16625-3] DR TopDownProteomics; Q16625-6; -. [Q16625-6] DR Antibodypedia; 782; 631 antibodies from 39 providers. DR DNASU; 100506658; -. DR Ensembl; ENST00000355237.6; ENSP00000347379.2; ENSG00000197822.12. [Q16625-1] DR Ensembl; ENST00000396442.7; ENSP00000379719.2; ENSG00000197822.12. [Q16625-1] DR Ensembl; ENST00000538151.2; ENSP00000445940.1; ENSG00000197822.12. [Q16625-4] DR Ensembl; ENST00000680027.1; ENSP00000506162.1; ENSG00000197822.12. [Q16625-1] DR Ensembl; ENST00000680496.1; ENSP00000504966.1; ENSG00000197822.12. [Q16625-2] DR Ensembl; ENST00000680784.1; ENSP00000506305.1; ENSG00000197822.12. [Q16625-2] DR Ensembl; ENST00000681041.1; ENSP00000505426.1; ENSG00000197822.12. [Q16625-1] DR Ensembl; ENST00000681586.1; ENSP00000505541.1; ENSG00000197822.12. [Q16625-1] DR GeneID; 100506658; -. DR KEGG; hsa:100506658; -. DR MANE-Select; ENST00000396442.7; ENSP00000379719.2; NM_001205254.2; NP_001192183.1. DR UCSC; uc003jwu.3; human. [Q16625-1] DR AGR; HGNC:8104; -. DR CTD; 100506658; -. DR DisGeNET; 100506658; -. DR GeneCards; OCLN; -. DR HGNC; HGNC:8104; OCLN. DR HPA; ENSG00000197822; Tissue enhanced (thyroid). DR MalaCards; OCLN; -. DR MIM; 251290; phenotype. DR MIM; 602876; gene. DR neXtProt; NX_Q16625; -. DR OpenTargets; ENSG00000197822; -. DR Orphanet; 1229; Congenital intrauterine infection-like syndrome. DR PharmGKB; PA31893; -. DR VEuPathDB; HostDB:ENSG00000197822; -. DR eggNOG; ENOG502QS9F; Eukaryota. DR GeneTree; ENSGT00730000110989; -. DR HOGENOM; CLU_039628_1_0_1; -. DR InParanoid; Q16625; -. DR OMA; SNYDKPP; -. DR OrthoDB; 5360956at2759; -. DR PhylomeDB; Q16625; -. DR TreeFam; TF326161; -. DR PathwayCommons; Q16625; -. DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins. DR Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions. DR SignaLink; Q16625; -. DR SIGNOR; Q16625; -. DR BioGRID-ORCS; 100506658; 13 hits in 1139 CRISPR screens. DR ChiTaRS; OCLN; human. DR EvolutionaryTrace; Q16625; -. DR GeneWiki; Occludin; -. DR GenomeRNAi; 100506658; -. DR Pharos; Q16625; Tbio. DR PRO; PR:Q16625; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q16625; Protein. DR Bgee; ENSG00000197822; Expressed in islet of Langerhans and 128 other cell types or tissues. DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central. DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl. DR GO; GO:0005923; C:bicellular tight junction; IDA:BHF-UCL. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0031252; C:cell leading edge; ISS:ARUK-UCL. DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL. DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB. DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI. DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:ARUK-UCL. DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IMP:ARUK-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL. DR GO; GO:0046326; P:positive regulation of glucose import; IMP:ARUK-UCL. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:ARUK-UCL. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:ARUK-UCL. DR GO; GO:0090303; P:positive regulation of wound healing; ISS:ARUK-UCL. DR GO; GO:1902463; P:protein localization to cell leading edge; ISS:ARUK-UCL. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IMP:ARUK-UCL. DR Gene3D; 6.10.140.340; -; 1. DR InterPro; IPR031176; ELL/occludin. DR InterPro; IPR008253; Marvel. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR002958; Occludin. DR InterPro; IPR010844; Occludin_ELL. DR PANTHER; PTHR23288:SF4; 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; SSF103473; MFS general substrate transporter; 1. DR SUPFAM; SSF144292; occludin/ELL-like; 1. DR PROSITE; PS51225; MARVEL; 1. DR PROSITE; PS51980; OCEL; 1. DR Genevisible; Q16625; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Coiled coil; Disease variant; Disulfide bond; Membrane; Phosphoprotein; KW Reference proteome; Tight junction; Transmembrane; Transmembrane helix. FT CHAIN 1..522 FT /note="Occludin" FT /id="PRO_0000146739" FT TOPO_DOM 1..66 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 67..89 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 90..135 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:9175707" FT TRANSMEM 136..160 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 161..170 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 171..195 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 196..243 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 244..265 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 266..522 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 60..269 FT /note="MARVEL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581" FT DOMAIN 414..522 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 360..407 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 426..489 FT /evidence="ECO:0000255" FT COMPBIAS 387..404 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:0007744|PubMed:24275569" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 340 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q61146" FT MOD_RES 368 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 398 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:19017651" FT MOD_RES 402 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:19017651" FT MOD_RES 403 FT /note="Phosphothreonine; by PKC/PRKCH" FT /evidence="ECO:0000269|PubMed:19114660" FT MOD_RES 404 FT /note="Phosphothreonine; by PKC/PRKCH" FT /evidence="ECO:0000269|PubMed:19114660" FT MOD_RES 408 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:24275569" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19125584" FT DISULFID 216..237 FT /evidence="ECO:0000269|PubMed:23923978" FT VAR_SEQ 1..251 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043872" FT VAR_SEQ 50..69 FT /note="DEILHFYKWTSPPGVIRILS -> ESLQAVKEQIVTHQEDGWRL (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043873" FT VAR_SEQ 52..70 FT /note="ILHFYKWTSPPGVIRILSM -> MTIEKKVKSTWLLLMNTID (in FT isoform 7)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043874" FT VAR_SEQ 70 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043875" FT VAR_SEQ 71..522 FT /note="Missing (in isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043876" FT VAR_SEQ 244..297 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_043877" FT VAR_SEQ 252..322 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043878" FT VAR_SEQ 476..522 FT /note="AAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT -> V FT NST (in isoform 3)" FT /evidence="ECO:0000303|PubMed:20463075" FT /id="VSP_043879" FT VARIANT 219 FT /note="F -> S (in PTORCH1; dbSNP:rs267606926)" FT /evidence="ECO:0000269|PubMed:20727516" FT /id="VAR_064910" FT MUTAGEN 398 FT /note="Y->A: Loss of phosphorylation and loss of regulation FT of TJP1 binding; when associated with A-402." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 398 FT /note="Y->D: Loss of phosphorylation, almost complete loss FT of binding to TJP1, loss of regulation of TJP1 binding and FT loss of localization to plasma membrane and sites of FT cell-cell contact; when associated with D-402." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 398 FT /note="Y->F: Loss of phosphorylation, decrease in binding FT to TJP1 and significant loss of regulation of TJP1 binding; FT when associated with F-402." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 402 FT /note="Y->A: Loss of phosphorylation and loss of regulation FT of TJP1 binding; when associated with A-398." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 402 FT /note="Y->D: Loss of phosphorylation, almost complete loss FT of binding to TJP1, loss of regulation of TJP1 binding and FT loss of localization to plasma membrane and sites of FT cell-cell contact; when associated with D-398." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 402 FT /note="Y->F: Loss of phosphorylation, decrease in binding FT to TJP1 and significant loss of regulation of TJP1 binding; FT when associated with F-398." FT /evidence="ECO:0000269|PubMed:19017651" FT MUTAGEN 404 FT /note="T->A: Loss of localization to the tight junctions." FT /evidence="ECO:0000269|PubMed:19114660" FT CONFLICT 233 FT /note="L -> S (in Ref. 7; AAH29886)" FT /evidence="ECO:0000305" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:1XAW" FT HELIX 426..466 FT /evidence="ECO:0007829|PDB:1XAW" FT HELIX 472..488 FT /evidence="ECO:0007829|PDB:1XAW" FT HELIX 491..520 FT /evidence="ECO:0007829|PDB:1XAW" SQ SEQUENCE 522 AA; 59144 MW; A0CF9574BCF6E974 CRC64; MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SVGYPYGGSG FGSYGSGYGY GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET DYTTGGESCD ELEEDWIREY PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMAAADE YNRLKQVKGS ADYKSKKNHC KQLKSKLSHI KKMVGDYDRQ KT //