OCLN_XENLA
ID OCLN_XENLA Reviewed; 493 AA.
AC Q9PUN1;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Occludin;
GN Name=ocln;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT THR-375 AND SER-379.
RC TISSUE=Ovary;
RX PubMed=10491082; DOI=10.1046/j.1432-1327.1999.00616.x;
RA Cordenonsi M., Turco F., D'Atri F., Hammar E., Martinucci G., Meggio F.,
RA Citi S.;
RT "Xenopus laevis occludin. Identification of in vitro phosphorylation sites
RT by protein kinase CK2 and association with cingulin.";
RL Eur. J. Biochem. 264:374-384(1999).
RN [2]
RP CHARACTERIZATION.
RX PubMed=9365283; DOI=10.1242/jcs.110.24.3131;
RA Cordenonsi M., Mazzon E., De Rigo L., Baraldo S., Meggio F., Citi S.;
RT "Occludin dephosphorylation in early development of Xenopus laevis.";
RL J. Cell Sci. 110:3131-3139(1997).
CC -!- FUNCTION: Probably plays a role in the formation and regulation of the
CC tight junction (TJ) paracellular permeability barrier.
CC -!- SUBUNIT: Interacts in vitro with cingulin, possibly directly. Interacts
CC with ZO-1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9PUN1; Q9PTD7: cgn; NbExp=2; IntAct=EBI-79607, 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.
CC -!- DEVELOPMENTAL STAGE: A maternally synthesized protein. Found in
CC granules in the peripheral cytoplasm in the fertilized egg, it
CC localizes first to the basolateral membrane, then to tight junctions
CC after cingulin and ZO-1. Nascent tight junctions are in place by the
CC two-cell stage. The maternal form is more highly phosphorylated than
CC the form detected in later developmental stages.
CC -!- DOMAIN: The C-terminus 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: Phosphorylated. {ECO:0000269|PubMed:10491082}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; AF170275; AAD53725.1; -; mRNA.
DR RefSeq; NP_001081943.1; NM_001088474.1.
DR AlphaFoldDB; Q9PUN1; -.
DR SMR; Q9PUN1; -.
DR IntAct; Q9PUN1; 1.
DR iPTMnet; Q9PUN1; -.
DR GeneID; 398133; -.
DR CTD; 398133; -.
DR Xenbase; XB-GENE-866529; ocln.S.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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..493
FT /note="Occludin"
FT /id="PRO_0000146743"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..250
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 386..493
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 334..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..428
FT /evidence="ECO:0000255"
FT MOD_RES 375
FT /note="Phosphothreonine; by CK2; in vitro"
FT /evidence="ECO:0000269|PubMed:10491082"
FT MOD_RES 379
FT /note="Phosphoserine; by CK2; in vitro"
FT /evidence="ECO:0000269|PubMed:10491082"
FT DISULFID 197..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 493 AA; 55112 MW; 9694CD302BEBBEDE CRC64;
MYSRPSNYAP SKDVYGGEMR SQPAYSYYPE EEIQHFYRWS SPPGIIKIMS ILIVVMCVGI
FACVASTLPW DLDITGQSMG YGMGSGSYSG GYTGYGFGGS QMGLGFAYGG NYTDPRAAKG
FILAMAAFCF IIGLVIFVML VTRTPLSTSR KFYLIVIIVS AIIGGLVFIA TIVYTVGVNP
VAQASGSAFY TQIVSICNQF YSPVQTGVFV NQYLYHYCVV EPQEAIAIVL GFLIVVAFAI
IIFFAVKTRK KINQYGKTNI LWKKNHIYED GDPQVEQWVK NVAENSAPAL SDYNEKVDGS
VADYRSANGV QAYPSQNNIS HPIAEEELPL KEDYGMSPRH YSSSSDATTK KAPPKKRPGK
PRRSDLDTNE GGYNTGGESA DELEDDSWDS EYPPITQTKQ RQEYKQEFAS DLHEYKRLQA
ELDELSKIPV PSLNRELGQS SRKDSEEYRT VADKYNRLKE IKSSADYRNK KKRCKGLKTK
LNHIKQMVSN YDK
