ID   HSOP_WHEAT              Reviewed;         581 AA.
AC   F8RP11;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Hsp70-Hsp90 organizing protein;
DE            Short=TaHop;
GN   Name=HOP;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=21596689; DOI=10.1093/mp/ssr037;
RA   Fellerer C., Schweiger R., Schoengruber K., Soll J., Schwenkert S.;
RT   "Cytosolic HSP90 cochaperones HOP and FKBP interact with freshly
RT   synthesized chloroplast preproteins of Arabidopsis.";
RL   Mol. Plant 4:1133-1145(2011).
CC   -!- FUNCTION: Mediates the association of the molecular chaperones HSP70
CC       and HSP90 (By similarity). Mediates nuclear encoded chloroplast
CC       preproteins binding to HSP90 prior to chloroplastic sorting.
CC       {ECO:0000250, ECO:0000269|PubMed:21596689}.
CC   -!- SUBUNIT: Co-chaperone that forms a complex with HSP70 and HSP90 and
CC       preproteins (e.g. chloroplast preproteins).
CC       {ECO:0000269|PubMed:21596689}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The tetratricopeptide repeat (TPR) domain, forming a
CC       carboxylate clamp (CC), mediates interaction with the highly conserved
CC       'EEVD' motif at the C-terminal ends of HSP90 and HSP70. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- PTM: Acetylated. {ECO:0000250}.
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DR   EMBL; HM998695; ADN05856.1; -; mRNA.
DR   AlphaFoldDB; F8RP11; -.
DR   SMR; F8RP11; -.
DR   STRING; 4565.Traes_6DL_3E8CC7CF1.2; -.
DR   PRIDE; F8RP11; -.
DR   eggNOG; KOG0548; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; F8RP11; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR   GO; GO:0070678; F:preprotein binding; IDA:UniProtKB.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; 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; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR22904; PTHR22904; 1.
DR   Pfam; PF17830; STI1; 2.
DR   Pfam; PF07719; TPR_2; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00727; STI1; 2.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Stress response; TPR repeat.
FT   CHAIN           1..581
FT                   /note="Hsp70-Hsp90 organizing protein"
FT                   /id="PRO_0000426704"
FT   REPEAT          2..35
FT                   /note="TPR 1"
FT   REPEAT          37..69
FT                   /note="TPR 2"
FT   REPEAT          70..103
FT                   /note="TPR 3"
FT   DOMAIN          148..187
FT                   /note="STI1 1"
FT   REPEAT          253..286
FT                   /note="TPR 4"
FT   REPEAT          288..320
FT                   /note="TPR 5"
FT   REPEAT          332..365
FT                   /note="TPR 6"
FT   REPEAT          392..425
FT                   /note="TPR 7"
FT   REPEAT          427..459
FT                   /note="TPR 8"
FT   REPEAT          460..493
FT                   /note="TPR 9"
FT   DOMAIN          530..569
FT                   /note="STI1 2"
FT   REGION          199..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           250..267
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        199..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  65097 MW;  A9264F6DEA4EF743 CRC64;
     MADEAKAKGN AAFSAGRFEE AAGHFSDAIA LAPANHVLYS NRSAALASIH RYSDALADAE
     KTVELKPDWA KGYSRLGAAH LGLGDAASAA AAYEKGLALD PSNEGLKAGL ADAKKAAAAP
     PRRAPSGGAD AIGQMFQGPE LWTKIASDPA TRAYLDQPDF MQMLREVQRN PSSLNTYLSD
     PRMMQVLSLM LNIKIQTPQD SDFSQSSSPS QPPPQQQKQQ PETKAREMEP EPQPEPMEVS
     DEEKERKERK AAALKEKEAG NASYKKKDFE TAIQHYTKAL ELDDEDISYL TNRAAVYIEM
     GKYDECIEDC DKAVERGREL RADFKMVARA LTRKGTALAK LAKNSKDYDI AIETFQKALT
     EHRNPDTLKR LNEAEKAKKD LEQQEYYDPK LADEEREKGN EMFKQQKYPE AIKHYNEAIR
     RNPKDARVYS NRAACYTKLG AMPEGLKDAE KCIELDPTFT KGYTRKGAVQ FFMKEYEKAM
     ETYQAGLKYD PNNQELLDGI RRCVEQINKA NRGDISQEDL QEKQSKAMQD PEIQNILTDP
     IMRQVLMDFQ ENPRAAQDHL KDPGVAQKIQ KLINAGIVQT R