ID A0A182DWZ8_ONCOC Unreviewed; 600 AA.
AC A0A182DWZ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN ORFNames=NOO_LOCUS168 {ECO:0000313|EMBL:VDK61536.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00168-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00168-RA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t00168-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK61536.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; UYRW01000014; VDK61536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182DWZ8; -.
DR STRING; 42157.A0A182DWZ8; -.
DR WBParaSite; nOo.2.0.1.t00168-RA; nOo.2.0.1.t00168-RA; nOo.2.0.1.g00168.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF246; PROTEIN DISULFIDE-ISOMERASE; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 41..182
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 394..575
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 571..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 104..107
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 445..448
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 600 AA; 67088 MW; A0E43EDC369D0C88 CRC64;
MRNRSSHAEF VQEKKGSTND FSGVCHVDYP MGEQHTIQCA TTIGKGRGTI VIEETMDDGM
AVVRWWLCRV LLKSLAVSDH VQNNFDDAVA AHEFILVEFY APWCGHCKAL APEYAKAAQL
LKKEDSPIKL GKCDATVHGE LASKYEVRGY PTLKLFRSGK PQEYGGGRDA ASIVAWLKKK
TGPAAKTMLS ADDVKDFQEN NEVCVIGYFK DTESADAKVF LEVAGGFDDI PFGITTEIDA
AKQLGLENDG IVLLKKFDEG RAEFGEKLVA DALRSWVQVE RLPLVSEFTQ DTAPIIFGGD
IKSHNLLFIS KESSEFEKLE KEFRAAAKKF KGKVFFVIID TDVEDNARIL EFFGLKKEDL
AALRLISLEE DMTKYKPDFK EIIAENIVQF TEMYLAGKLK PHLMTQDIPS DWDKNPVKIL
VGKNFEDVAK NAKKDVLVLF YAPWCGHCKQ LMPTWDKLGE KYKDHDTILI AKMDATANEV
ENVKVQSFPT IKFFPASSNK ASFTRNRGGH ETGKLYPFIL VHNSGNICFV KLVTIYDQGK
LKRALILMFG FVNVIDFTGE RTLEGLTKFL ESGGKDGAGL SDEEKAEAEA ESEDDEHTEL
//
