ID A0A2K5JTW5_COLAP Unreviewed; 522 AA.
AC A0A2K5JTW5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Occludin {ECO:0000256|ARBA:ARBA00016772, ECO:0000256|PIRNR:PIRNR005993};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000032282.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000032282.1}
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 RefSeq; XP_011814709.1; XM_011959319.1.
DR AlphaFoldDB; A0A2K5JTW5; -.
DR STRING; 336983.ENSCANP00000032282; -.
DR Ensembl; ENSCANT00000055504.1; ENSCANP00000032282.1; ENSCANG00000039808.1.
DR GeneID; 105524161; -.
DR CTD; 100506658; -.
DR OMA; SNYDKPP; -.
DR OrthoDB; 5360956at2759; -.
DR Proteomes; UP000233080; 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; IPR036259; MFS_trans_sf.
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; SSF103473; MFS general substrate transporter; 1.
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:UP000233080};
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 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..269
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT DOMAIN 414..522
FT /note="OCEL"
FT /evidence="ECO:0000259|PROSITE:PS51980"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..487
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 363..380
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 DISULFID 216..237
FT /evidence="ECO:0000256|PIRSR:PIRSR005993-1"
SQ SEQUENCE 522 AA; 59096 MW; 01FA776AF8381131 CRC64;
MSSRPLESPP PYRPDEFKPN HYAPSNDVYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS
PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SIGYPYGGSG FGSYGSGYGY
GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFATSV IRSEMSRTRR YYLSVIIVSA
ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAVSGLYVD QYLYHYCVVD
PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKENIYEEQ SPNVEEWVKN
VSAGTQDVPP PPSDYAERVD SPVAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV
DDFRQPRYSS SGNFETPSKR TSAKGRAGKS KRTEQDHYET DYTTGGESCD ELEEDWIREY
PPITSDQQRQ LYKRNFDIGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMAAADE
YNRLKQVKGS ADYKSKKDHC KQLKSKLSHI KKMVGDYDRQ KT
//
