ID A0A0R3RV38_9BILA Unreviewed; 498 AA.
AC A0A0R3RV38;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-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};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000593801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000593801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0R3RV38; -.
DR STRING; 1147741.A0A0R3RV38; -.
DR WBParaSite; EEL_0000593801-mRNA-1; EEL_0000593801-mRNA-1; EEL_0000593801.
DR Proteomes; UP000050640; Unplaced.
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; cd03073; PDI_b'_ERp72_ERp57; 1.
DR CDD; cd03069; PDI_b_ERp57; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR041868; PDIA3_PDI_b.
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; 2.
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; 4.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 27..498
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005967595"
FT DOMAIN 10..136
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 352..478
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 399..402
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 498 AA; 56967 MW; 6ED28C6E4D8D3B5E CRC64;
MALLRSFNTA LISYSLSLLL LPVAKADGDV MEFTDSDFKE GIKPYDVLLV KFYAPWCGHC
KKLAPEFEKA ATKLLQNDPP IHLAKVDCTE EKKTCDEFSV SGFPTLKIFR KGELAQDYDG
PRVAEGIVKY MRGQAGPSAA EISTPQEFEK MLEADDVTIC GFFEGDSKLK DSFLKVADTE
RDRFKFVWTS NKQILESNGY NDDIVAYQPK KFHNKFEPNG FKYDGNYDTD KIKEFLLHET
NGLVGIRTSE NRYQFDQLPM FVVYSKIDYE LDPKGSNYWR NRVLIVANAY KRKAYFAISN
KDDFSFDLDE FGLADRKDTK PLVAARSKKG KFFMKEEFSV ENLRKFVEDV VNDRLEPHMK
SEEPPEEQGD VKVVVAKTFQ EMVIDAEKDV LIEFYAPWCG HCNALAPKYD ELGQKLSGES
GVIIAKMDAT ANDVPPPFQV QGFPTLYWVP KNRKDKPEPY SGGREVDDFI KYIAKHATEE
LEGYKRDGKP KKKKKEEL
//
