ID A0A1U7RCG7_ALLSI Unreviewed; 514 AA.
AC A0A1U7RCG7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772, ECO:0000256|PIRNR:PIRNR005993};
GN Name=LOC102373195 {ECO:0000313|RefSeq:XP_006017479.1,
GN ECO:0000313|RefSeq:XP_025052158.1, ECO:0000313|RefSeq:XP_025052159.1,
GN ECO:0000313|RefSeq:XP_025052160.1, ECO:0000313|RefSeq:XP_025052161.1,
GN ECO:0000313|RefSeq:XP_025052162.1, ECO:0000313|RefSeq:XP_025052163.1,
GN ECO:0000313|RefSeq:XP_025052164.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006017479.1};
RN [1] {ECO:0000313|RefSeq:XP_006017479.1, ECO:0000313|RefSeq:XP_025052158.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_006017479.1; XM_006017417.3.
DR RefSeq; XP_025052158.1; XM_025196373.1.
DR RefSeq; XP_025052159.1; XM_025196374.1.
DR RefSeq; XP_025052160.1; XM_025196375.1.
DR RefSeq; XP_025052161.1; XM_025196376.1.
DR RefSeq; XP_025052162.1; XM_025196377.1.
DR RefSeq; XP_025052163.1; XM_025196378.1.
DR RefSeq; XP_025052164.1; XM_025196379.1.
DR STRING; 38654.A0A1U7RCG7; -.
DR GeneID; 102373195; -.
DR KEGG; asn:102373195; -.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR OrthoDB; 5360956at2759; -.
DR Proteomes; UP000189705; 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:SF6; 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:UP000189705};
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 54..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..260
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 406..514
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 340..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 435..462
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 340..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 209..228
FT /evidence="ECO:0000256|PIRSR:PIRSR005993-1"
SQ SEQUENCE 514 AA; 57106 MW; 12C565E18C174C9F CRC64;
MYSKKSYDGA PIAYGPPGDE YGYDAQSPPP GSYYIEDVPQ HFYKWSSPPG VVRVLEAMAI
LLCVAIFACV ASTLAWEYGL GYGGLYGSGM GGYYGGTGYY GGAMGYSGYG GGYGGGYGGY
YGGVTNPRAA NGFMMAMSVL CFLALLGLFV ASLTKGSGSR SRKFYLVVIV LCAILAFLML
IASIVYIMGV NPQAQMSGSY SYNPMLTMCN QMYATGGAYL NQYMYHYCTV DPQEAIAIVC
GFLIVIILCV VCFFAHKTRS KIWQYGKPNI YWDKPLAMQE GPNVEEWVKN VANGTSTHDE
TATLAYSEKP TSPVHAAPSA YSYPPPPSTY YVPENYHTAS SPAPVSEGQP ATTFSTSMLE
EKGRESTSRP SARRGRRRRR NPELDESQYE TDYTTAMESS DERDKDEWSS VYPPITSDGA
RQEYKQEFDV DLKHYKQLCA EMDNINDELN QLSKQLDSLS EDSPQYQGVA EEYNRLKDLK
RSPDYQTKKL ETKSLRNKLF HIKRMVSDYD KLRG
//
