OCLN_CANLF
ID OCLN_CANLF Reviewed; 521 AA.
AC Q28269;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Occludin;
GN Name=OCLN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8601611; DOI=10.1083/jcb.133.1.43;
RA Ando-Akatsuka Y., Saitou M., Hirase T., Kishi M., Sakakibara A., Itoh M.,
RA Yonemura S., Furuse M., Tsukita S.;
RT "Interspecies diversity of the occludin sequence: cDNA cloning of human,
RT mouse, dog, and rat-kangaroo homologues.";
RL J. Cell Biol. 133:43-47(1996).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=9182670; DOI=10.1083/jcb.137.6.1393;
RA Sakakibara A., Furuse M., Saitou M., Ando-Akatsuka Y., Tsukita S.;
RT "Possible involvement of phosphorylation of occludin in tight junction
RT formation.";
RL J. Cell Biol. 137:1393-1401(1997).
CC -!- FUNCTION: May play a role in the formation and regulation of the tight
CC junction (TJ) paracellular permeability barrier. Interacts with ZO-1.
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 -!- INTERACTION:
CC Q28269; P24723: PRKCH; Xeno; NbExp=2; IntAct=EBI-16222162, EBI-2865850;
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 -!- TISSUE SPECIFICITY: Localized at tight junctions of both epithelial and
CC endothelial cells.
CC -!- DOMAIN: The C-terminal is cytoplasmic and is important for interaction
CC with ZO-1. Necessary 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 (By similarity). Less-phosphorylated
CC forms are found in basolateral membrane, cytosol and tight junction.
CC More-heavily phosphorylated forms are concentrated exclusively in tight
CC junction. {ECO:0000250, ECO:0000269|PubMed:9182670}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; U49221; AAC48582.1; -; mRNA.
DR RefSeq; NP_001003195.1; NM_001003195.1.
DR AlphaFoldDB; Q28269; -.
DR SMR; Q28269; -.
DR DIP; DIP-48669N; -.
DR IntAct; Q28269; 1.
DR STRING; 9615.ENSCAFP00000011546; -.
DR PaxDb; Q28269; -.
DR GeneID; 403844; -.
DR KEGG; cfa:403844; -.
DR CTD; 100506658; -.
DR eggNOG; ENOG502QS9F; Eukaryota.
DR InParanoid; Q28269; -.
DR OrthoDB; 710557at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070830; P:bicellular tight junction assembly; IBA:GO_Central.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:ARUK-UCL.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:ARUK-UCL.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:ARUK-UCL.
DR GO; GO:1902463; P:protein localization to cell leading edge; IMP:ARUK-UCL.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR008253; Marvel.
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 PROSITE; PS51225; MARVEL; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome; Tight junction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..521
FT /note="Occludin"
FT /id="PRO_0000146738"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 60..268
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT DOMAIN 413..521
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 301..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 424..488
FT /evidence="ECO:0000255"
FT COMPBIAS 378..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61146"
FT MOD_RES 367
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 397
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 401
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 402
FT /note="Phosphothreonine; by PKC/PRKCH"
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 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16625"
FT DISULFID 215..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 521 AA; 59275 MW; 2875E59F8F0A1FFA CRC64;
MSSRPFESPP PYRPDEFKPN HYAPSNDVYG GDMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LVIVMCIAIF GCVASTLAWD RGYGTGLMGG SIGYPYGSGF GSYGTGYGYG
FGYGYGYGGY TDPRAAKGFL LAMVAFCFIA ALVIFVTSVI RSDISRTRRY YLTVIILSAF
LGVMMFIATI VYIMGVNPTA QASGSLYSSQ IYAMCNQFYA STATGLYMDQ YLYHYCVVDP
QEAIAIVLGF MVIVAFALII FFAVKTRRKM DRYDKSNILW DKEHIYDEQP PNVEEWVKNV
SAGTQDMPPP PSDYVERVDS PMAYSSNGKV NDKRLYPESS YKSTPVPEVV QELPATSPAD
DFRQPRYSSS GHLEPPSKRA PSKGRTGRPK RLEQDHYETD YTTGGESCDE LEEDWIREYP
PITSDQQRQL YKRNFDTGLQ EYKSLQAELD EINKELSRLD KELDDYREES EEYMAAADEY
NRLKQVKGSP DYKNKRNYCK QLKSKLSHIK KMVGDYDRQK T
