ID W6UL66_ECHGR Unreviewed; 714 AA.
AC W6UL66;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=EGR_03017 {ECO:0000313|EMBL:EUB62265.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB62265.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB62265.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUB62265.1}.
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DR EMBL; APAU02000014; EUB62265.1; -; Genomic_DNA.
DR AlphaFoldDB; W6UL66; -.
DR STRING; 6210.W6UL66; -.
DR EnsemblMetazoa; XM_024492266.1; XP_024353461.1; GeneID_36338732.
DR OMA; QLANKFE; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000019149; 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 Gene3D; 3.40.30.10; Glutaredoxin; 3.
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:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
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:UP000019149};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 265..421
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 568..697
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 297..300
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 618..621
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 714 AA; 81285 MW; 784B4F338A6DD060 CRC64;
MGTERIMHLP CTVILLMQQA VVYLLKIRPK LSSLLASYNL TCHSIGTTDD SNELRHRWTQ
QRGALMTGLT TIQANFIVVI EAQRKRPAPE TTLFQLCAYY LAFLDFALHS FQRGQQLLLA
FPDLPRSGIK ESRIQELPSL ASQTTSVSIT VISEKERTNL IADVTTIKLC RSTVKLLNNH
LSSRYTAANR ISRLLSIVQA TVSRHRASRE HRDSTWSEWR IDTPHEYTQA NNAPRNEEKS
PWIRVCLAPV AKMFRTLLFA LLFHLVFGTD VIPLTKKTRS ELSKHPVALV KYYAPWCGRC
KELAPHYEEA AAELKIKEPS VPLFEVNCDE ETDMCNEAGI KGYPTLKVYN YGEYAEEFDE
GRTTENIVNF MVLRSGPPAT EILDESRYKE LFEGEDYIVS LQSKKSDEID EFEKLARKLR
KLIQLSLPKQ LETKLEDRSK TYDGPLKSAD IEQWIRKNAV GTAGIRDKKM KEFFKKPLLV
VYTQINFERN PSNVRYHRNR LISVAKDTKS ELQFALSDTS AFSDELYEMG LTANDEGAMV
IIMGENGKNY LMSDKFGVSE LKKFVSDFAA GSLEPYIKSE PIPEKQEGSV MKVVGRTFEK
VVLDESKDVL VEFYAPWCGH CEALKPKYEE LAKKLSKEKD VIVAAVDATA NSFPPAFDVQ
GYPTIYWVPK ASKDKPIPYK GGREVDDMLK FVAKSATDEL IHYTRDGQLK QEEL
//
