UniProt functional annotation for Q8I4V8



	UniProt functional annotation for Q8I4V8

UniProt code: Q8I4V8.

Organism: Plasmodium falciparum (isolate 3D7).

Taxonomy: Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania).

Function: Has peptidylprolyl isomerase (PPIase) and co-chaperone activities (PubMed:15664653, PubMed:15850699). Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates (PubMed:15664653, PubMed:15850699, PubMed:23974147). Inhibits calcineurin phosphatase activity in vitro (PubMed:15850699, PubMed:17289400, PubMed:23974147). Plays an essential role in merozoite egress from host erythrocytes (PubMed:15664653, PubMed:23974147). {ECO:0000269|PubMed:15664653, ECO:0000269|PubMed:15850699, ECO:0000269|PubMed:17289400, ECO:0000269|PubMed:23974147}.

Catalytic activity: Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000255|PROSITE- ProRule:PRU00277, ECO:0000269|PubMed:15664653, ECO:0000269|PubMed:15850699, ECO:0000269|PubMed:23974147};

Activity regulation: Inhibited by FK506 and its derivates, such as ascomycin, and rapamycin (PubMed:15664653, PubMed:15850699). FK506 and rapamycin inhibit peptidylprolyl isomerase activity but not chaperone activity (PubMed:15664653). Inhibited by N-(2-ethyl-phenyl)-2-(3H- imidazao [4, 5-b] pyridin-2-yl-sulfanyl)-acetamide (D44) (PubMed:23974147). Not inhibited by cyclosporin A (PubMed:15664653, PubMed:15850699). Inhibition of calcineurin phosphatase activity is enhanced by FK506 (PubMed:15850699). {ECO:0000269|PubMed:15664653, ECO:0000269|PubMed:15850699, ECO:0000269|PubMed:23974147}.

Subunit: Homodimer (PubMed:17289400). Interacts (via TPR repeats) with HSP90 (probably via MEEVD motif) (PubMed:15850699, PubMed:19691130). {ECO:0000269|PubMed:15850699, ECO:0000269|PubMed:17289400, ECO:0000269|PubMed:19691130}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:15850699}. Nucleus {ECO:0000269|PubMed:15850699}. Note=During the asexual blood stage, predominantly localizes to the cytoplasm of ring stage parasites and then translocates to the nucleus during the differentiation into trophozoites and schizonts. {ECO:0000269|PubMed:15850699}.

Developmental stage: Expressed during all parasite blood stages (at protein level). {ECO:0000269|PubMed:15850699}.

Domain: The PPIase FKBP-type domain contributes to the chaperone activity (PubMed:15664653). Required for the inhibition of calcineurin phosphatase activity (PubMed:15850699). {ECO:0000269|PubMed:15664653, ECO:0000269|PubMed:15850699}.

Domain: The TPR repeats are important for the chaperone activity (PubMed:15664653). In another study, these repeats appear to be dispensable for chaperone activity (PubMed:15850699). Dispensable for PPIase activity (PubMed:15850699). Dispensable for the inhibition of calcineurin phosphatase activity (PubMed:15850699). {ECO:0000269|PubMed:15664653, ECO:0000269|PubMed:15850699}.

Similarity: Belongs to the FKBP-type PPIase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Plasmodium falciparum (isolate 3D7).
Taxonomy:		Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; Plasmodiidae; Plasmodium; Plasmodium (Laverania).



Function:		Has peptidylprolyl isomerase (PPIase) and co-chaperone activities (PubMed:15664653, PubMed:15850699). Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates (PubMed:15664653, PubMed:15850699, PubMed:23974147). Inhibits calcineurin phosphatase activity in vitro (PubMed:15850699, PubMed:17289400, PubMed:23974147). Plays an essential role in merozoite egress from host erythrocytes (PubMed:15664653, PubMed:23974147). {ECO:0000269\|PubMed:15664653, ECO:0000269\|PubMed:15850699, ECO:0000269\|PubMed:17289400, ECO:0000269\|PubMed:23974147}.


Catalytic activity:		Reaction=[protein]-peptidylproline (omega=180) = [protein]- peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000255\|PROSITE- ProRule:PRU00277, ECO:0000269\|PubMed:15664653, ECO:0000269\|PubMed:15850699, ECO:0000269\|PubMed:23974147};
Activity regulation:		Inhibited by FK506 and its derivates, such as ascomycin, and rapamycin (PubMed:15664653, PubMed:15850699). FK506 and rapamycin inhibit peptidylprolyl isomerase activity but not chaperone activity (PubMed:15664653). Inhibited by N-(2-ethyl-phenyl)-2-(3H- imidazao [4, 5-b] pyridin-2-yl-sulfanyl)-acetamide (D44) (PubMed:23974147). Not inhibited by cyclosporin A (PubMed:15664653, PubMed:15850699). Inhibition of calcineurin phosphatase activity is enhanced by FK506 (PubMed:15850699). {ECO:0000269\|PubMed:15664653, ECO:0000269\|PubMed:15850699, ECO:0000269\|PubMed:23974147}.
Subunit:		Homodimer (PubMed:17289400). Interacts (via TPR repeats) with HSP90 (probably via MEEVD motif) (PubMed:15850699, PubMed:19691130). {ECO:0000269\|PubMed:15850699, ECO:0000269\|PubMed:17289400, ECO:0000269\|PubMed:19691130}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:15850699}. Nucleus {ECO:0000269\|PubMed:15850699}. Note=During the asexual blood stage, predominantly localizes to the cytoplasm of ring stage parasites and then translocates to the nucleus during the differentiation into trophozoites and schizonts. {ECO:0000269\|PubMed:15850699}.
Developmental stage:		Expressed during all parasite blood stages (at protein level). {ECO:0000269\|PubMed:15850699}.
Domain:		The PPIase FKBP-type domain contributes to the chaperone activity (PubMed:15664653). Required for the inhibition of calcineurin phosphatase activity (PubMed:15850699). {ECO:0000269\|PubMed:15664653, ECO:0000269\|PubMed:15850699}.
Domain:		The TPR repeats are important for the chaperone activity (PubMed:15664653). In another study, these repeats appear to be dispensable for chaperone activity (PubMed:15850699). Dispensable for PPIase activity (PubMed:15850699). Dispensable for the inhibition of calcineurin phosphatase activity (PubMed:15850699). {ECO:0000269\|PubMed:15664653, ECO:0000269\|PubMed:15850699}.
Similarity:		Belongs to the FKBP-type PPIase family. {ECO:0000305}.