ID A0A3Q3BAW5_KRYMA Unreviewed; 490 AA.
AC A0A3Q3BAW5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000021719.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000021719.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. 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|PROSITE-ProRule:PRU01324}.
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DR AlphaFoldDB; A0A3Q3BAW5; -.
DR Ensembl; ENSKMAT00000022001.1; ENSKMAP00000021719.1; ENSKMAG00000016139.1.
DR GeneTree; ENSGT00730000110989; -.
DR Proteomes; UP000264800; Unplaced.
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:SF4; OCCLUDIN; 1.
DR PANTHER; PTHR23288; OCCLUDIN AND RNA POLYMERASE II ELONGATION FACTOR ELL; 1.
DR Pfam; PF01284; MARVEL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR PRINTS; PR01258; OCCLUDIN.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00581}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00581};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..276
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 407..490
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 318..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54772 MW; 0BF37D7D98DB85BD CRC64;
MLGFYFKVSC NSRNLAGCFF AHQHSVDPAA MSSRPNGSPP PYEEENGYNI APPQPAYSYY
PDDEFQHFYR WTSPPGILKI MAVLVIVLCV AIFACVASTL AWDSSGAMSG YGGTYMVNNG
PYSGNTYNYG YGSIRGNYND PRSGKGFMIA MAVTVSIFVL VVFIIIVSHQ SLSESRKFYL
AVVIICAILA LLMLIATIVY LMAVNPMAQS SGSVYGNQIA ALCAQYQQPQ TSGVFTNQYL
YHYCVVEPQE AIAIVFGFLV TAALIIMLVF ALKTRQKIQN YGKSNIFWKK VKIVDDAEPP
QDVEAWVNNV SATPEVAPVS DYPEKLRGSR SYLDDENTSY DKPPVSYTPQ PVVEDRHLQS
SALYSGNSEI ASSAGRPKKR RPGRPRRTDG QDCDTDYNSS GDELDDNDFD SEFPPVTNEQ
ERNNYKREFD HDHKEYKDLQ AELDSINKNL SELDNELDEL EEGSPQYLDA LDEYNRIRSL
KKVCILLEGI
//