OCLN_HUMAN
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 03-AUG-2022, entry version 192.
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 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 [23]
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).
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 -!- 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";
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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 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. [Q16625-2]
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; 497.
DR DIP; DIP-42791N; -.
DR IntAct; Q16625; 48.
DR MINT; Q16625; -.
DR STRING; 9606.ENSP00000347379; -.
DR TCDB; 9.B.41.1.1; the occludin (occludin) family.
DR iPTMnet; Q16625; -.
DR PhosphoSitePlus; Q16625; -.
DR BioMuta; OCLN; -.
DR DMDM; 3914196; -.
DR EPD; Q16625; -.
DR jPOST; Q16625; -.
DR MassIVE; Q16625; -.
DR MaxQB; Q16625; -.
DR PaxDb; Q16625; -.
DR PeptideAtlas; Q16625; -.
DR PRIDE; 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 TopDownProteomics; Q16625-3; -. [Q16625-3]
DR TopDownProteomics; Q16625-6; -. [Q16625-6]
DR Antibodypedia; 782; 503 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 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; PEQDHYE; -.
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 1061 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 126 other tissues.
DR Genevisible; Q16625; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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 SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
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 cell-
FT 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 cell-
FT 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
