(data stored in ACNUC9543 zone)
SWISSPROT: C0H4Y6_PLAF7
ID C0H4Y6_PLAF7 Unreviewed; 483 AA.
AC C0H4Y6;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 08-MAY-2019, entry version 90.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|RuleBase:RU361130};
GN ORFNames=PF3D7_0827900 {ECO:0000313|EMBL:CAX64161.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CAX64161.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S.,
RA Chan M.S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S.,
RA Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B.,
RA Martin D.M., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A.,
RA McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C.,
RA Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W.,
RA Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium
RT falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C.,
RA Chillingworth T., Christodoulou Z., Clark L., Clark R., Corton C.,
RA Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J.,
RA Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z.,
RA Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P.,
RA Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A.,
RA Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N.,
RA Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L.,
RA Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E.,
RA Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M.,
RA Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K.,
RA Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|RuleBase:RU361130};
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|RuleBase:RU004208, ECO:0000256|SAAS:SAAS00569802}.
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DR EMBL; AL844507; CAX64161.1; -; Genomic_DNA.
DR RefSeq; XP_002808883.1; XM_002808837.1.
DR SMR; C0H4Y6; -.
DR DrugBank; DB11638; Artenimol.
DR SwissPalm; C0H4Y6; -.
DR PRIDE; C0H4Y6; -.
DR EnsemblProtists; CAX64161; CAX64161; PF3D7_0827900.
DR GeneDB; PF3D7_0827900.1:pep; -.
DR GeneID; 2655362; -.
DR KEGG; pfa:PF3D7_0827900; -.
DR EuPathDB; PlasmoDB:PF3D7_0827900; -.
DR HOGENOM; HOG000065811; -.
DR InParanoid; C0H4Y6; -.
DR KO; K01829; -.
DR OMA; VAIVKMD; -.
DR PhylomeDB; C0H4Y6; -.
DR Reactome; R-PFA-3299685; Detoxification of Reactive Oxygen Species.
DR Proteomes; UP000001450; Chromosome 8.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:GeneDB.
DR GO; GO:0020009; C:microneme; IDA:GeneDB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:GeneDB.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IDA:GeneDB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
DR PRODOM; C0H4Y6.
DR SWISS-2DPAGE; C0H4Y6.
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000001450};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51,
KW ECO:0000256|SAAS:SAAS00903405};
KW Isomerase {ECO:0000256|RuleBase:RU361130,
KW ECO:0000313|EMBL:CAX64161.1};
KW Redox-active center {ECO:0000256|PIRSR:PIRSR605792-51,
KW ECO:0000256|SAAS:SAAS00903442};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW Repeat {ECO:0000256|SAAS:SAAS00038388};
KW Signal {ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1 24 {ECO:0000256|RuleBase:RU361130}.
FT CHAIN 25 483 Protein disulfide-isomerase.
FT {ECO:0000256|RuleBase:RU361130}.
FT /FTId=PRO_5005124648.
FT DOMAIN 23 138 Thioredoxin. {ECO:0000259|PROSITE:
FT PS51352}.
FT DOMAIN 333 463 Thioredoxin. {ECO:0000259|PROSITE:
FT PS51352}.
FT COILED 255 275 {ECO:0000256|SAM:Coils}.
FT DISULFID 60 63 Redox-active. {ECO:0000256|PIRSR:
FT PIRSR605792-51}.
FT DISULFID 384 387 Redox-active. {ECO:0000256|PIRSR:
FT PIRSR605792-51}.
SQ SEQUENCE 483 AA; 55514 MW; 3DE86F4BCC20BAD6 CRC64;
MNRKYFSSLF LFLISFVFES FVRSHGDLFN HFVTDIHDGE LDKFITKNDI VLVMFYAPWC
GHCKRLIPEY NEAANMLNEK KSEIKLVSID ATSENALAQE YGITGYPTLI LFNKKNKINY
GGGRTAQSIV DWLLQMTGPV FSHVEGNIED VLKEKKINVA FYLEYTSEDN DLYKKFNEVG
DKNREIAKYF VKKNDKHNKL FCFRTDEKKV EYDEKTPLEE FVTSESFPLF GEINTENYRF
YAESPKELVW VCATYEQYNE IKEHVRLAAQ ELRKKTHFVL LNIPEYAEHA KASLGLTEFP
GLAFQSNEGR YLLKNPKESL LNHNAIINFF KDVEAGKIEK SLKSEPIPED DKNAPVKIVV
GNSFVDVVLK SGKDVLIEIY APWCGHCKKL EPVYEDLGRK LKKYDSIIVA KMDGTLNETP
IKDFEWSGFP TIFFVKAGSK IPLPYEGERS LKGFVDFLNK HATNTPISID GVPEFEDGTS
EEL
//
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