HSOP_PLAF7
ID HSOP_PLAF7 Reviewed; 564 AA.
AC Q8ILC1; A0A144A2J9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hsp70-Hsp90 organising protein {ECO:0000303|PubMed:22005844};
DE Short=PfHOP {ECO:0000303|PubMed:22005844};
DE AltName: Full=Stress-inducible protein 1 {ECO:0000303|PubMed:32343703};
GN Name=HOP {ECO:0000303|PubMed:22005844};
GN Synonyms=STI1 {ECO:0000303|PubMed:32343703};
GN ORFNames=PF14_0324, PF3D7_1434300;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH HSP70 AND HSP90, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22005844; DOI=10.1007/s12192-011-0299-x;
RA Gitau G.W., Mandal P., Blatch G.L., Przyborski J., Shonhai A.;
RT "Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising
RT protein (PfHop).";
RL Cell Stress Chaperones 17:191-202(2012).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH HSP70 AND HSP90, AND INDUCTION.
RX PubMed=26267894; DOI=10.1371/journal.pone.0135326;
RA Zininga T., Makumire S., Gitau G.W., Njunge J.M., Pooe O.J., Klimek H.,
RA Scheurr R., Raifer H., Prinsloo E., Przyborski J.M., Hoppe H., Shonhai A.;
RT "Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a
RT Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity.";
RL PLoS ONE 10:e0135326-e0135326(2015).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=31525467; DOI=10.1016/j.bbapap.2019.140282;
RA Silva N.S.M., Bertolino-Reis D.E., Dores-Silva P.R., Anneta F.B.,
RA Seraphim T.V., Barbosa L.R.S., Borges J.C.;
RT "Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium
RT falciparum and its modulation of Hsp70 and Hsp90 ATPase activities.";
RL Biochim. Biophys. Acta 1868:140282-140282(2020).
RN [5]
RP SUBUNIT.
RX PubMed=32343703; DOI=10.1371/journal.pone.0226657;
RA Makumire S., Zininga T., Vahokoski J., Kursula I., Shonhai A.;
RT "Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising
RT protein (PfHop) reveals a monomer that is characterised by folded segments
RT connected by flexible linkers.";
RL PLoS ONE 15:e0226657-e0226657(2020).
CC -!- FUNCTION: Acts as a co-chaperone and mediates the association of the
CC chaperones HSP70 and HSP90 probably facilitating substrate transfer
CC from HSP70 to HSP90 (PubMed:22005844, PubMed:26267894). Stimulates
CC HSP70 ATPase activity and, in contrast, inhibits HSP90 ATPase activity
CC (PubMed:31525467). {ECO:0000269|PubMed:22005844,
CC ECO:0000269|PubMed:26267894, ECO:0000269|PubMed:31525467}.
CC -!- SUBUNIT: Monomer (PubMed:32343703). Homodimer (PubMed:26267894,
CC PubMed:31525467). Forms a complex composed of HOP and chaperones HSP70
CC and HSP90; the interaction is stronger in the absence of ATP
CC (PubMed:22005844). Interacts (via TPR 1, 2, 3, 7, 8 and 9 repeats) with
CC HSP70 (via C-terminus); the interaction is direct and is stronger in
CC the absence of ATP (PubMed:26267894). Interacts (via TPR 4, 5 and 6
CC repeats) with HSP90 (via C-terminus); the interaction is direct
CC (PubMed:26267894). {ECO:0000269|PubMed:22005844,
CC ECO:0000269|PubMed:26267894, ECO:0000269|PubMed:31525467,
CC ECO:0000269|PubMed:32343703}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22005844}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage, in
CC trophozoites (at protein level). {ECO:0000269|PubMed:22005844}.
CC -!- INDUCTION: By heat stress (at protein level).
CC {ECO:0000269|PubMed:26267894}.
CC -!- DOMAIN: The TPR repeats form 3 domains; the TPR 1 domain is composed of
CC TPR 1, 2 and 3 repeats, the TPR2A domain of TPR 4, 5 and 6 repeats and
CC TPR2B domain of TPR 7, 8 and 9 repeats. {ECO:0000303|PubMed:22005844}.
CC -!- CAUTION: Showed to form heterodimers (PubMed:26267894,
CC PubMed:31525467). However in a later study, showed to exist
CC predominantly as a monomer (PubMed:32343703).
CC {ECO:0000269|PubMed:26267894, ECO:0000269|PubMed:31525467,
CC ECO:0000269|PubMed:32343703}.
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DR EMBL; LN999946; CZU00040.1; -; Genomic_DNA.
DR RefSeq; XP_001348498.1; XM_001348462.1.
DR AlphaFoldDB; Q8ILC1; -.
DR SASBDB; Q8ILC1; -.
DR SMR; Q8ILC1; -.
DR BioGRID; 1207264; 5.
DR IntAct; Q8ILC1; 4.
DR STRING; 5833.PF14_0324; -.
DR PRIDE; Q8ILC1; -.
DR EnsemblProtists; CZU00040; CZU00040; PF3D7_1434300.
DR GeneID; 811906; -.
DR KEGG; pfa:PF3D7_1434300; -.
DR VEuPathDB; PlasmoDB:PF3D7_1434300; -.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q8ILC1; -.
DR OMA; HYSKAWE; -.
DR PhylomeDB; Q8ILC1; -.
DR Reactome; R-PFA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:GeneDB.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 4.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..564
FT /note="Hsp70-Hsp90 organising protein"
FT /id="PRO_0000295632"
FT REPEAT 7..40
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 42..74
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 76..108
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 243..276
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 278..310
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 318..351
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 378..411
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 413..445
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REPEAT 446..479
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT DOMAIN 513..552
FT /note="STI1"
FT /evidence="ECO:0000255"
FT REGION 199..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 197..239
FT /evidence="ECO:0000255"
SQ SEQUENCE 564 AA; 66057 MW; 215FA96B9A1B67B5 CRC64;
MVNKEEAQRL KELGNKCFQE GKYEEAVKYF SDAITNDPLD HVLYSNLSGA FASLGRFYEA
LESANKCISI KKDWPKGYIR KGCAEHGLRQ LSNAEKTYLE GLKIDPNNKS LQDALSKVRN
ENMLENAQLI AHLNNIIEND PQLKSYKEEN SNYPHELLNT IKSINSNPMN IRIILSTCHP
KISEGVEKFF GFKFTGEGND AEERQRQQRE EEERRKKKEE EERKKKEEEE MKKQNRTPEQ
IQGDEHKLKG NEFYKQKKFD EALKEYEEAI QINPNDIMYH YNKAAVHIEM KNYDKAVETC
LYAIENRYNF KAEFIQVAKL YNRLAISYIN MKKYDLAIEA YRKSLVEDNN RATRNALKEL
ERRKEKEEKE AYIDPDKAEE HKNKGNEYFK NNDFPNAKKE YDEAIRRNPN DAKLYSNRAA
ALTKLIEYPS ALEDVMKAIE LDPTFVKAYS RKGNLHFFMK DYYKALQAYN KGLELDPNNK
ECLEGYQRCA FKIDEMSKSE KVDEEQFKKS MADPEIQQII SDPQFQIILQ KLNENPNSIS
EYIKDPKIFN GLQKLIAAGI LKVR
