ID A0A452QI74_URSAM Unreviewed; 520 AA.
AC A0A452QI74;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772, ECO:0000256|PIRNR:PIRNR005993};
GN Name=OCLN {ECO:0000313|Ensembl:ENSUAMP00000004802.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000004802.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000004802.1}
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; A0A452QI74; -.
DR STRING; 9643.ENSUAMP00000004802; -.
DR Ensembl; ENSUAMT00000005462.1; ENSUAMP00000004802.1; ENSUAMG00000004365.1.
DR GeneTree; ENSGT00730000110989; -.
DR OMA; SNYDKPP; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
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 PIRSF; PIRSF005993; Occludin; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000291022};
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 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..268
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 412..520
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 301..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..485
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 215..236
FT /evidence="ECO:0000256|PIRSR:PIRSR005993-1"
SQ SEQUENCE 520 AA; 59152 MW; D8005F0EB7A48EF7 CRC64;
MSSRPFESPP PYRPDEFKPN HYAPSNDVYG GDMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LIIVMCIAIF ACVASTLAWD RSYGTGLLGG GLGYPYSSGF GSYGSGYAYG
YGYGYGYGGY TDPRAAKGFL LAMVAFCFIA ALVIFVTSVI RSDISRTRRY YLTVIILSAI
LGIMMFIATI VYIMGVNPTA QASGSIYSSQ IYAICNQFYT SATTGLYMDQ YLYHYCVVDP
QEAIAIVLGF MVIVAFALII FFAVKTRRKM DRYDKSNIMW DKEHVYDEQP PNVEEWVKNV
SAGTQDMPPP PSDYVERVDS PMAYSSNGKV NDKRLYSESS YKSTPVPEVV QELPVTSPVD
DGRQPRYSSG NLETPSKRAP TKGRAGRSKR PEQDHYETDY TTGGESCDEL EEDWIREYPP
ITSDQQRQFY KRNFDTGLQE YKSLQAELDE VNKELSRLDK ELDDYREESE EYMAAADEYN
RLKQVKGSAD YKNKRHYCKQ LKSKLSHIKK MVGDYDRQKT
//
