OCLN_PONAB
ID OCLN_PONAB Reviewed; 522 AA.
AC Q5RFS5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Occludin;
GN Name=OCLN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TJP1/ZO1. Interacts with VAPA. Interacts with
CC CLDN1, CLDN6, CLDN9, CLDN11, CLDN12 and CLDN17. Interacts with PLSCR1.
CC Interacts with LSR, ILDR1 and ILDR2. {ECO:0000250|UniProtKB:Q16625}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16625};
CC Multi-pass membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q16625}.
CC -!- DOMAIN: The C-terminal is cytoplasmic and is important for interaction
CC with ZO-1. Sufficient for the tight junction localization. Involved in
CC the regulation of the permeability barrier function of the tight
CC junction (By similarity). {ECO:0000250}.
CC -!- PTM: Dephosphorylated by PTPRJ. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; CR857077; CAH89382.1; -; mRNA.
DR RefSeq; NP_001127140.1; NM_001133668.1.
DR AlphaFoldDB; Q5RFS5; -.
DR SMR; Q5RFS5; -.
DR STRING; 9601.ENSPPYP00000017356; -.
DR PRIDE; Q5RFS5; -.
DR GeneID; 100174190; -.
DR KEGG; pon:100174190; -.
DR CTD; 100506658; -.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR InParanoid; Q5RFS5; -.
DR OrthoDB; 710557at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070830; P:bicellular tight junction assembly; IEA:InterPro.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002958; Occludin.
DR InterPro; IPR010844; Occludin_ELL.
DR PANTHER; PTHR23288; PTHR23288; 1.
DR PANTHER; PTHR23288:SF4; PTHR23288:SF4; 1.
DR Pfam; PF01284; MARVEL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR PIRSF; PIRSF005993; Occludin; 1.
DR PRINTS; PR01258; OCCLUDIN.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Coiled coil; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..522
FT /note="Occludin"
FT /id="PRO_0000236102"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..269
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 414..522
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..488
FT /evidence="ECO:0000255"
FT COMPBIAS 363..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 368
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 398
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 402
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 403
FT /note="Phosphothreonine; by PKC/PRKCH"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 404
FT /note="Phosphothreonine; by PKC/PRKCH"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT DISULFID 216..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 522 AA; 59234 MW; F70775CAD26A9CE7 CRC64;
MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LIIVMCIAIF TCVASTLAWD RGYGTSLLGG SIGYPYGGSG FGSYGSGYGY
SYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA
ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD
PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN
VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV
DDFRQPRYSS SGNFETPSKR APAKGRAAKS KRTEQDHYET DYTTGGESCD ELEEDWIREY
PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMAAADE
YNRLKQVKGS ADYKSKKNHC KQLKSKLSHI KKMVGDYDRQ KT
