ID A0A3P8PK38_ASTCA Unreviewed; 556 AA.
AC A0A3P8PK38;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772, ECO:0000256|PIRNR:PIRNR005993};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000017343.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000017343.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000017343.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier.
CC {ECO:0000256|PIRNR:PIRNR005993}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR005993};
CC Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR005993}. Cell
CC junction, tight junction {ECO:0000256|PIRNR:PIRNR005993}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family.
CC {ECO:0000256|ARBA:ARBA00009171, ECO:0000256|PIRNR:PIRNR005993,
CC ECO:0000256|PROSITE-ProRule:PRU01324}.
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DR AlphaFoldDB; A0A3P8PK38; -.
DR STRING; 8154.ENSACLP00000017343; -.
DR Ensembl; ENSACLT00000017761.1; ENSACLP00000017343.1; ENSACLG00000011854.1.
DR GeneTree; ENSGT00940000165052; -.
DR OMA; AFFAHKT; -.
DR OrthoDB; 5360956at2759; -.
DR Proteomes; UP000265100; Chromosome 17.
DR Bgee; ENSACLG00000011854; Expressed in liver and 7 other cell types or tissues.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:InterPro.
DR Gene3D; 6.10.140.340; -; 1.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR002958; Occludin.
DR InterPro; IPR010844; Occludin_ELL.
DR PANTHER; PTHR23288:SF6; OCCLUDIN; 1.
DR PANTHER; PTHR23288; OCCLUDIN AND RNA POLYMERASE II ELONGATION FACTOR ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR PIRSF; PIRSF005993; Occludin; 1.
DR SUPFAM; SSF144292; occludin/ELL-like; 1.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949,
KW ECO:0000256|PIRNR:PIRNR005993};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR005993-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005993};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427,
KW ECO:0000256|PIRNR:PIRNR005993};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR005993};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..283
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 449..556
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 341..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..505
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 223..251
FT /evidence="ECO:0000256|PIRSR:PIRSR005993-1"
SQ SEQUENCE 556 AA; 62064 MW; 2B220203FF76E08E CRC64;
MFDKQHYESP PVYSPPFTPP PNNGFGPAAS FHGPQSDYNV YPPPPGSYYM EDKPQHFYKW
LSPPGIVKAM MVTVIVLCLA IFACVASTLM WDIQYGYGSG MGYYGSGMGY GSGYIGGSYG
SGYGGYGGYG NYYGSGSYIS PYSAKAAMIA MAAINFVGAL AFFIASFSKT NAVRSRKYFL
AVLISSVLMA ALQGIINIVY IVGVNPMAQS SSSMMYNPML MMCQNLYQTS YSQMGGVGGF
PMYNQYLYHY CFVDPQEGIA MACGFLVVIA LSVAAFFAQR TRGKIWRYGK PNIYWEEPLV
GGKASEGRDV EDWVNNVEES RSVQDAPTLL VSEKGGGPLN ASVNSVVSYP PPKVESSSYN
DDAYDNNEYS ERTNSRPLVT AHLTQQSHDV DIFFHSGGTS SSPSEETGGG RKPSANRGKR
RRRNPELDES QYDTEYTTGG ETGNELDAEE LESMYPEITS DDQRHDYKRE FDADLREYKR
LCAEMDDIND QLNKLSRQLD TLDDTSAKYQ IVAEEYNQLK DLKQTSDYQA KKTECRRLRH
KLFHIKRMVK DYDKNH
//
