ID Q2XQR4_PLABE Unreviewed; 482 AA.
AC Q2XQR4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 Name=PDI {ECO:0000313|EMBL:ABB72221.1};
GN ORFNames=PBK173_000122300 {ECO:0000313|EMBL:CXI22951.1},
GN PBNK65E_000115700 {ECO:0000313|EMBL:SCN23784.1}, PBNK65NY_000115100
GN {ECO:0000313|EMBL:SCM20146.1}, PBSP11A_000115300
GN {ECO:0000313|EMBL:SCO60155.1}, PBSP11RLL_000114900
GN {ECO:0000313|EMBL:SCO59235.1};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821 {ECO:0000313|EMBL:ABB72221.1};
RN [1] {ECO:0000313|EMBL:ABB72221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ANKA {ECO:0000313|EMBL:ABB72221.1};
RX PubMed=16806221; DOI=10.1016/j.ijpara.2006.04.012;
RA Mahajan B., Noiva R., Yadava A., Zheng H., Majam V., Mohan K.V., Moch J.K.,
RA Haynes J.D., Nakhasi H., Kumar S.;
RT "Protein disulfide isomerase assisted protein folding in malaria
RT parasites.";
RL Int. J. Parasitol. 36:1037-1048(2006).
RN [2] {ECO:0000313|EMBL:SCN23784.1, ECO:0000313|Proteomes:UP000220214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K173 {ECO:0000313|EMBL:CXI22951.1,
RC ECO:0000313|Proteomes:UP000069549}, NK65 ny
RC {ECO:0000313|EMBL:SCM20146.1, ECO:0000313|Proteomes:UP000516480},
RC NK65e {ECO:0000313|EMBL:SCN23784.1,
RC ECO:0000313|Proteomes:UP000220214}, SP11 Antwerpcl1
RC {ECO:0000313|EMBL:SCO60155.1, ECO:0000313|Proteomes:UP000219860}, and
RC SP11 RLL {ECO:0000313|EMBL:SCO59235.1,
RC ECO:0000313|Proteomes:UP000219974};
RG Pathogen Informatics;
RL Submitted (MAY-2016) 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; DQ266891; ABB72221.1; -; mRNA.
DR EMBL; LT160027; CXI22951.1; -; Genomic_DNA.
DR EMBL; LT608143; SCM20146.1; -; Genomic_DNA.
DR EMBL; LT614633; SCN23784.1; -; Genomic_DNA.
DR EMBL; LT608271; SCO59235.1; -; Genomic_DNA.
DR EMBL; LT608255; SCO60155.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2XQR4; -.
DR VEuPathDB; PlasmoDB:PBANKA_0702800; -.
DR OMA; FFGMKKD; -.
DR Proteomes; UP000069549; Chromosome 7.
DR Proteomes; UP000219860; Chromosome 7.
DR Proteomes; UP000219974; Chromosome 7.
DR Proteomes; UP000220214; Chromosome 7.
DR Proteomes; UP000516480; Chromosome 7.
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 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; 2.
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; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 2: Evidence at transcript level;
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..23
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 24..482
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5014205810"
FT DOMAIN 21..137
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 340..462
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 383..386
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 482 AA; 55411 MW; 9274790FD743E0A5 CRC64;
MNTKYISFFL FIIPFIFKNY VRSHEDLFNE HITSIHDGEL NNFITKNDIV LVMFYAPWCG
HCKRLIPEYN EAAIMLSEKK SEIKLASVDA TVERGLSQEY GITGYPTMIL FNKKNRINYG
GGRTAQTIVD WILQMTGPVS TEITGNIEDV LKESNINVAF YMEYISEDNE LFKKFNEVGD
KNREIAKYFI KKNDKHNKIY CYRKDEKTVE YDEKTPLNDF VAIESFPLFG EINTENYRFY
AESPKELVWI CATIEQYNEI KEEVRLAAAE LRNKTHFVLL NIPEYADHAK ASLGINEFPG
LAYQSSEGRY LLANPQQSLK NHKDIISFFK DVEAGKIEKS LKSEPIPEED KNAAVKVVVG
NSFTDVVLNS GKDVLIEIYA PWCGHCKKLE PIYEELGRKL KKYDHIIVAK MDGTLNETSL
KEFEWSGFPT IFFVKAGSKI PLPYEGERTL KGFVDFLNKH STKTPITIDD VSQSYEGSSE
EL
//
