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Protein

Occludin

Gene

OCLN

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. Interacts with ZO-1.

GO - Biological processi

Protein family/group databases

TCDBi9.B.41.1.3 the occludin (occludin) family

Names & Taxonomyi

Protein namesi
Recommended name:
Occludin
Gene namesi
Name:OCLN
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 57CytoplasmicSequence analysisAdd BLAST57
Transmembranei58 – 80HelicalSequence analysisAdd BLAST23
Topological domaini81 – 123ExtracellularSequence analysisAdd BLAST43
Transmembranei124 – 148HelicalSequence analysisAdd BLAST25
Topological domaini149 – 158CytoplasmicSequence analysis10
Transmembranei159 – 183HelicalSequence analysisAdd BLAST25
Topological domaini184 – 227ExtracellularSequence analysisAdd BLAST44
Transmembranei228 – 249HelicalSequence analysisAdd BLAST22
Topological domaini250 – 504CytoplasmicSequence analysisAdd BLAST255

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi379Y → D: Lower binding to TJP1, higher binding to TJP3 and decrease in phosphorylation. Lower binding to TJP1 and TJP3, loss of phosphorylation and loss of regulation of TJP1 binding; when associated with D-383. 1 Publication1
Mutagenesisi379Y → F: Decrease in phosphorylation and decrease in regulation of TJP1 binding. Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with F-383. 1 Publication1
Mutagenesisi383Y → D: Lower binding to TJP1 and TJP3, decrease in phosphorylation and loss of regulation of TJP1 and TJP3 binding. Lower binding to TJP1 and TJP3, loss of phosphorylation and loss of regulation of TJP1 binding; when associated with D-379. 1 Publication1
Mutagenesisi383Y → F: Decrease in phosphorylation and loss of regulation of TJP1 binding. Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with F-379. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467421 – 504OccludinAdd BLAST504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi204 ↔ 221PROSITE-ProRule annotation
Modified residuei379Phosphotyrosine1 Publication1
Modified residuei383Phosphotyrosine1 Publication1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

PTM databases

iPTMnetiQ91049

Expressioni

Tissue specificityi

Localized at tight junctions of both epithelial and endothelial cells. Highly expressed in lung and liver. Expressed at a lower level in brain.

Interactioni

Subunit structurei

Interacts with TJP1 and TJP3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
cgnQ9PTD72EBI-79619,EBI-79525From Xenopus laevis.

Protein-protein interaction databases

IntActiQ91049, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliQ91049
SMRiQ91049
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 253MARVELPROSITE-ProRule annotationAdd BLAST203

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 385Interaction with TJP11 Publication7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili412 – 471Sequence analysisAdd BLAST60

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi82 – 119Gly/Tyr-richAdd BLAST38
Compositional biasi347 – 351Poly-Glu5
Compositional biasi363 – 370Poly-Arg8

Domaini

The C-terminal is cytoplasmic and is important for interaction with ZO-1. Necessary for the tight junction localization. Involved in the regulation of the permeability barrier function of the tight junction. The second extracellular domain may also be implicated in the permeability barrier function of the tight junction.

Sequence similaritiesi

Belongs to the ELL/occludin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG004523
InParanoidiQ91049
KOiK06088
PhylomeDBiQ91049

Family and domain databases

InterProiView protein in InterPro
IPR031176 ELL/occludin
IPR008253 Marvel
IPR002958 Occludin
IPR010844 Occludin_ELL
PANTHERiPTHR23288 PTHR23288, 1 hit
PTHR23288:SF6 PTHR23288:SF6, 1 hit
PfamiView protein in Pfam
PF01284 MARVEL, 1 hit
PF07303 Occludin_ELL, 1 hit
PIRSFiPIRSF005993 Occludin, 1 hit
PRINTSiPR01258 OCCLUDIN
PROSITEiView protein in PROSITE
PS51225 MARVEL, 1 hit

Sequencei

Sequence statusi: Complete.

Q91049-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSKKSYDGP PAGYGPPTGY GAPTADYGYG SPPPGSYYVD DAPQLFYKWT
60 70 80 90 100
SPPGAVRGLQ AGVLVLCIAI FACVASTLAW DYGYGLGGAY GTGLGGFYGS
110 120 130 140 150
NYYGSGLSYS YGYGGYYGGV NQRTANGFMI AMAVLCFLAQ LGLLVAALSK
160 170 180 190 200
SGATRSRRFY LAVLVLSAVL AFVMLIASIV YIMGVNPQAQ MSSGYYYSPL
210 220 230 240 250
LAMCSQAYGS TYLNQYIYHY CTVDPQEAVA AVCGFLIVIL LCLICFFAQK
260 270 280 290 300
TRSKIWRYGK ANIYWDRAPV VQEGPDVEEW VKNVADGASV QDETATLAYS
310 320 330 340 350
EKPTSPVAAP PYSYVPPPSA GYYPSGTYSS RGDQPDRALS ASPVHGEEEE
360 370 380 390 400
EKGKDQPSRP PARRGRRRRR NPELDESQYE TDYTTAVESS DERDQEQWAS
410 420 430 440 450
LYPPITSDGA RQRYKQEFDT DLKRYKQLCA EMDSINDRLN QLSRRLDSIT
460 470 480 490 500
EDSPQYQDVA EEYNQLKDLK RSPDYQSKKQ ESKVLRNKLF HIKRMVSAYD

KVRG
Length:504
Mass (Da):55,864
Last modified:November 1, 1996 - v1
Checksum:iAD0352A45A0231FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21837 mRNA Translation: BAA04865.1
PIRiA49467
RefSeqiNP_990459.1, NM_205128.1
UniGeneiGga.603

Genome annotation databases

GeneIDi396026
KEGGigga:396026

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21837 mRNA Translation: BAA04865.1
PIRiA49467
RefSeqiNP_990459.1, NM_205128.1
UniGeneiGga.603

3D structure databases

ProteinModelPortaliQ91049
SMRiQ91049
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91049, 1 interactor

Protein family/group databases

TCDBi9.B.41.1.3 the occludin (occludin) family

PTM databases

iPTMnetiQ91049

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396026
KEGGigga:396026

Organism-specific databases

CTDi100506658

Phylogenomic databases

HOVERGENiHBG004523
InParanoidiQ91049
KOiK06088
PhylomeDBiQ91049

Miscellaneous databases

PROiPR:Q91049

Family and domain databases

InterProiView protein in InterPro
IPR031176 ELL/occludin
IPR008253 Marvel
IPR002958 Occludin
IPR010844 Occludin_ELL
PANTHERiPTHR23288 PTHR23288, 1 hit
PTHR23288:SF6 PTHR23288:SF6, 1 hit
PfamiView protein in Pfam
PF01284 MARVEL, 1 hit
PF07303 Occludin_ELL, 1 hit
PIRSFiPIRSF005993 Occludin, 1 hit
PRINTSiPR01258 OCCLUDIN
PROSITEiView protein in PROSITE
PS51225 MARVEL, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiOCLN_CHICK
AccessioniPrimary (citable) accession number: Q91049
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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