OCLN_MOUSE
ID OCLN_MOUSE Reviewed; 521 AA.
AC Q61146; Q544A7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Occludin {ECO:0000305};
GN Name=Ocln; Synonyms=Ocl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=11102513; DOI=10.1091/mbc.11.12.4131;
RA Saitou M., Furuse M., Sasaki H., Schulzke J.D., Fromm M., Takano H.,
RA Noda T., Tsukita S.;
RT "Complex phenotype of mice lacking occludin, a component of tight junction
RT strands.";
RL Mol. Biol. Cell 11:4131-4142(2000).
RN [4]
RP PHOSPHORYLATION AT SER-338, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11502742; DOI=10.1074/jbc.m104923200;
RA Andreeva A.Y., Krause E., Mueller E.-C., Blasig I.E., Utepbergenov D.I.;
RT "Protein kinase C regulates the phosphorylation and cellular localization
RT of occludin.";
RL J. Biol. Chem. 276:38480-38486(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; THR-303; SER-311;
RP SER-358; SER-368; SER-369; THR-403 AND SER-407, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH LSR, ILDR1 AND ILDR2, AND SUBCELLULAR LOCATION.
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).
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:0000269|PubMed:23239027}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16625};
CC Multi-pass membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000269|PubMed:23239027}.
CC -!- TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and
CC endothelial cells. Highly expressed in the testis, kidney, lung, liver
CC and brain. Not detected in skeletal muscle, spleen and heart.
CC -!- DEVELOPMENTAL STAGE: Found diffusely on the lateral membranes of
CC Sertoli cells in the early prepubertal period. With development, became
CC gradually concentrated at the most basal regions of Sertoli 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 (By similarity). May be phosphorylated
CC by PKC during translocation to cell-cell contacts. {ECO:0000250,
CC ECO:0000269|PubMed:11502742}.
CC -!- DISRUPTION PHENOTYPE: Mice have a complex phenotype including
CC abnormalities of salivary gland, gastric epithelium, bone, testis and
CC intracranial calcification. {ECO:0000269|PubMed:11102513}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; U49185; AAC52515.1; -; mRNA.
DR EMBL; AK019880; BAB31900.1; -; mRNA.
DR EMBL; AK042576; BAC31298.1; -; mRNA.
DR CCDS; CCDS26731.1; -.
DR RefSeq; NP_032782.1; NM_008756.2.
DR RefSeq; XP_006517626.1; XM_006517563.3.
DR RefSeq; XP_006517627.1; XM_006517564.3.
DR RefSeq; XP_006517629.1; XM_006517566.2.
DR RefSeq; XP_011242936.1; XM_011244634.2.
DR AlphaFoldDB; Q61146; -.
DR SMR; Q61146; -.
DR BioGRID; 201894; 9.
DR DIP; DIP-49005N; -.
DR IntAct; Q61146; 1.
DR STRING; 10090.ENSMUSP00000065284; -.
DR iPTMnet; Q61146; -.
DR PhosphoSitePlus; Q61146; -.
DR CPTAC; non-CPTAC-4054; -.
DR MaxQB; Q61146; -.
DR PaxDb; Q61146; -.
DR PRIDE; Q61146; -.
DR ProteomicsDB; 294266; -.
DR Antibodypedia; 782; 503 antibodies from 39 providers.
DR DNASU; 18260; -.
DR Ensembl; ENSMUST00000022140; ENSMUSP00000022140; ENSMUSG00000021638.
DR Ensembl; ENSMUST00000069756; ENSMUSP00000065284; ENSMUSG00000021638.
DR Ensembl; ENSMUST00000160859; ENSMUSP00000124849; ENSMUSG00000021638.
DR GeneID; 18260; -.
DR KEGG; mmu:18260; -.
DR UCSC; uc007rqy.1; mouse.
DR CTD; 100506658; -.
DR MGI; MGI:106183; Ocln.
DR VEuPathDB; HostDB:ENSMUSG00000021638; -.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR GeneTree; ENSGT00730000110989; -.
DR HOGENOM; CLU_039628_1_0_1; -.
DR InParanoid; Q61146; -.
DR OMA; PEQDHYE; -.
DR OrthoDB; 710557at2759; -.
DR PhylomeDB; Q61146; -.
DR TreeFam; TF326161; -.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR BioGRID-ORCS; 18260; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ocln; mouse.
DR PRO; PR:Q61146; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61146; protein.
DR Bgee; ENSMUSG00000021638; Expressed in brain blood vessel and 181 other tissues.
DR ExpressionAtlas; Q61146; baseline and differential.
DR Genevisible; Q61146; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; ISO:MGI.
DR GO; GO:0070673; P:response to interleukin-18; ISO:MGI.
DR GO; GO:0120193; P:tight junction organization; IMP:ARUK-UCL.
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..521
FT /note="Occludin"
FT /id="PRO_0000146740"
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..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..267
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 413..521
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 300..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..488
FT /evidence="ECO:0000255"
FT COMPBIAS 362..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 338
FT /note="Phosphoserine; by PKC; in vitro"
FT /evidence="ECO:0000269|PubMed:11502742"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 401
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 402
FT /note="Phosphothreonine; by PKC/PRKCH"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT DISULFID 214..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 521 AA; 59000 MW; 21D62F370EB33E7D CRC64;
MSVRPFESPP PYRPDEFKPN HYAPSNDMYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTGLFGG SLNYPYSGFG YGGGYGGGYG
GYGYGYGGYT DPRAAKGFLL AMAAFCFIAS LVIFVTSVIR SGMSRTRRYY LIVIIVSAIL
GIMVFIATIV YIMGVNPTAQ ASGSMYGSQI YMICNQFYTP GGTGLYVDQY LYHYCVVDPQ
EAIAIVLGFM IIVAFALIIF FAVKTRRKMD RYDKSNILWD KEHIYDEQPP NVEEWVKNVS
AGTQDMPPPP SDYAERVDSP MAYSSNGKVN GKRSYPESFY KSTPLVPEVA QEIPLTLSVD
DFRQPRYSSN GNLETPSKRA PTKGKAGKGK RTDPDHYETD YTTGGESCEE LEEDWVREYP
PITSDQQRQL YKRNFDAGLQ EYKSLQAELD DVNKELSRLD KELDDYREES EEYMAAADEY
NRLKQVKGSA DYKSKRNYCK QLKSKLSHIK RMVGDYDRRK P
