HRP_PLABE
ID HRP_PLABE Reviewed; 423 AA.
AC Q08168;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=58 kDa phosphoprotein;
DE AltName: Full=Heat shock-related protein;
DE Short=HRP;
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-423.
RC STRAIN=ANKA;
RX PubMed=8341321; DOI=10.1016/0166-6851(93)90220-r;
RA Uparanukraw P., Toyoshima T., Aikawa M., Kumar N.;
RT "Molecular cloning and localization of an abundant novel protein of
RT Plasmodium berghei.";
RL Mol. Biochem. Parasitol. 59:223-234(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-248.
RC STRAIN=ANKA / HP 8417;
RA Wiser M.F.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=9010839; DOI=10.1016/s0166-6851(96)02743-0;
RA Wiser M.F., Jennings G.J., Uparanukraw P., van Belkum A., van Doorn L.J.,
RA Kumar N.;
RT "Further characterization of a 58 kDa Plasmodium berghei phosphoprotein as
RT a cochaperone.";
RL Mol. Biochem. Parasitol. 83:25-33(1996).
CC -!- FUNCTION: May play a role in protein folding or protein-protein
CC interactions. May act as a co-chaperone.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9010839}.
CC -!- DEVELOPMENTAL STAGE: Present in all the different life cycle stages.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37293.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L04508; AAC37293.1; ALT_INIT; Genomic_DNA.
DR EMBL; L21710; AAC37300.1; -; mRNA.
DR PIR; T10455; T10455.
DR AlphaFoldDB; Q08168; -.
DR SMR; Q08168; -.
DR VEuPathDB; PlasmoDB:PBANKA_1242300; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18253; HipN; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Repeat; TPR repeat.
FT CHAIN 1..423
FT /note="58 kDa phosphoprotein"
FT /id="PRO_0000106343"
FT REPEAT 113..146
FT /note="TPR 1"
FT REPEAT 147..180
FT /note="TPR 2"
FT REPEAT 181..214
FT /note="TPR 3"
FT DOMAIN 361..423
FT /note="STI1"
FT REGION 46..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..362
FT /note="19 X 3-4 AA approximate repeats"
FT COMPBIAS 59..82
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 25
FT /note="K -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Missing (in Ref. 1; AAC37293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 47759 MW; FAF7002202D5C13A CRC64;
MDIEKIEDLK KFVASCEENP SILLKPELSF FKDFIESFGG KIKKDKMGYE KMKSEDSTEE
KSDEEEEDEE EEEEEEEDDD PEKLELIKEE AVECPPLAPI IEGELSEEQI EEICKLKEEA
VDLVENKKYE EALEKYNKII SFGNPSAMIY TKRASILLNL KRPKACIRDC TEALNLNVDS
ANAYKIRAKA YRYLGKWEFA HADMEQGQKI DYDENLWDMQ KLIQEKYKKI YEKRRYKINK
EEEKQRLKRE KELKKKLAAK KKAEKMYKEN NKRENYDSDS SDSSYSEPDF SGDFPGGMPG
GMPGMPGGMG GMGGMPGMPG GFPGMPGGMP GGMPGGMGGM PGMPGGMPGG MGGMPGMPGG
MPDLNSPEMK ELFNNPQFFQ MMQNMMSNPD LINKYASDPK YKNIFENLKN SDLGGMMGEK
PKP