HSOP1_SOYBN
ID HSOP1_SOYBN Reviewed; 572 AA.
AC Q43468; A0A0R0FCV3; I1MUX1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Hsp70-Hsp90 organizing protein 1;
DE Short=GmHop-1;
DE AltName: Full=Heat shock protein STI;
DE Short=GmSTI;
DE AltName: Full=Stress-inducible protein;
GN Name=HOP1; Synonyms=STI; OrderedLocusNames=Glyma17g137700;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000312|EMBL:CAA56165.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Williams {ECO:0000312|EMBL:CAA56165.1};
RC TISSUE=Epicotyl {ECO:0000312|EMBL:CAA56165.1};
RX PubMed=7766904; DOI=10.1007/bf00020896;
RA Torres J.H., Chatellard P., Stutz E.;
RT "Isolation and characterization of gmsti, a stress-inducible gene from
RT soybean (Glycine max) coding for a protein belonging to the TPR
RT (tetratricopeptide repeats) family.";
RL Plant Mol. Biol. 27:1221-1226(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82; TISSUE=Callus;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [3]
RP FUNCTION, INTERACTION WITH HSP90, MUTAGENESIS OF 327-THR--GLN-397, TISSUE
RP SPECIFICITY, AND INDUCTION BY ABIOTIC STRESS.
RX PubMed=12586877; DOI=10.1104/pp.011940;
RA Zhang Z., Quick M.K., Kanelakis K.C., Gijzen M., Krishna P.;
RT "Characterization of a plant homolog of hop, a cochaperone of hsp90.";
RL Plant Physiol. 131:525-535(2003).
CC -!- FUNCTION: Mediates nuclear encoded chloroplast preproteins binding to
CC HSP90 prior to chloroplastic sorting (By similarity). Mediates the
CC association of the molecular chaperones HSP70 and HSP90. {ECO:0000250,
CC ECO:0000269|PubMed:12586877}.
CC -!- SUBUNIT: Co-chaperone that forms a complex with HSP70 and HSP90 and
CC preproteins (e.g. chloroplast preproteins) (By similarity). Interacts
CC with HSP90. {ECO:0000250, ECO:0000269|PubMed:12586877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously, with maximal expression in
CC cotyledons, followed by shoots and flowers.
CC {ECO:0000269|PubMed:12586877}.
CC -!- INDUCTION: By heat shock, heat, cold shock and wounding.
CC {ECO:0000269|PubMed:12586877, ECO:0000269|PubMed:7766904}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56165.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CM000850; KRH04070.1; -; Genomic_DNA.
DR EMBL; X79770; CAA56165.1; ALT_FRAME; mRNA.
DR PIR; S56658; S56658.
DR RefSeq; NP_001236261.1; NM_001249332.1.
DR AlphaFoldDB; Q43468; -.
DR SMR; Q43468; -.
DR STRING; 3847.GLYMA17G14660.1; -.
DR PRIDE; Q43468; -.
DR ProMEX; Q43468; -.
DR EnsemblPlants; KRH04070; KRH04070; GLYMA_17G137700.
DR GeneID; 547932; -.
DR Gramene; KRH04070; KRH04070; GLYMA_17G137700.
DR KEGG; gmx:547932; -.
DR eggNOG; KOG0548; Eukaryota.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q43468; -.
DR OrthoDB; 1070087at2759; -.
DR Proteomes; UP000008827; Chromosome 17.
DR Genevisible; Q43468; GM.
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; ISS:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IEP:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEP:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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; 2.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 1.
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..572
FT /note="Hsp70-Hsp90 organizing protein 1"
FT /id="PRO_0000106328"
FT REPEAT 2..35
FT /note="TPR 1"
FT /evidence="ECO:0000305"
FT REPEAT 37..69
FT /note="TPR 2"
FT REPEAT 70..103
FT /note="TPR 3"
FT DOMAIN 142..181
FT /note="STI1 1"
FT REPEAT 244..277
FT /note="TPR 4"
FT REPEAT 279..311
FT /note="TPR 5"
FT REPEAT 319..356
FT /note="TPR 6"
FT REPEAT 383..416
FT /note="TPR 7"
FT REPEAT 417..450
FT /note="TPR 8"
FT REPEAT 451..484
FT /note="TPR 9"
FT DOMAIN 521..560
FT /note="STI1 2"
FT REGION 192..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 241..258
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 327..397
FT /note="Missing: Loss of binding with HSP90."
FT /evidence="ECO:0000269|PubMed:12586877"
SQ SEQUENCE 572 AA; 64178 MW; C0F7CAB4E4E0403C CRC64;
MAEEAKAKGN AAFSAGDFAA AVRHFSDAIA LSPSNHVLYS NRSAAHASLQ NYAEALADAQ
KTVDLKPDWP KAYSRLGAAH LGLRRHRDAF SAYKTGLQLD PDNAALKSGL ADAQAAASRP
PPTSPFATAF SGPDMWARLT ADPTARANLQ DPEFVKIMQD IQKDPNKFNL HLSDQRVMHA
IGVLLNVKIQ TPNHDENDHD ADDDVSEDEV VSQPEPEHEP EAAVEVAEEE EEEEKETRDR
KGQAQKEKEA GNAAYKKKDF ETAIGHYSKA LELDDEDISY LTNRAAVYLE MGKFEDCIKD
CEKAVERGKE LRSDYKMIAR ALTRKGTALA KMAKCSKDFE PAIEIFQKAL TENRNPDTLK
KLNEAEKAKK ELEQQEYFDP KLADEAREKG NELFKQQKYP EATKHYTEAI KRNPKDAKAY
SNRAACYTKL GAMPEGLKDA EKCIELDPTF SKGYTRKGAV QFSMKEYDKA LETYREGLKH
DPNNQELLDG IRRCVEQINK ASRGDFTPEE LKERQAKAMQ DPEIQSILQD PVMTQVLTDF
QENPRAAEEH VKNPMVMNKI QKLISAGIVQ MR
