HSOP3_ARATH
ID HSOP3_ARATH Reviewed; 558 AA.
AC Q9STH1; B9DG66; F4JQM6; Q8L724;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Hsp70-Hsp90 organizing protein 3;
DE Short=AtHop3;
GN Name=HOP3; OrderedLocusNames=At4g12400; ORFNames=T4C9.240;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17085506; DOI=10.1104/pp.106.091322;
RA Charng Y.-Y., Liu H.-C., Liu N.-Y., Chi W.-T., Wang C.-N., Chang S.-H.,
RA Wang T.-T.;
RT "A heat-inducible transcription factor, HsfA2, is required for extension of
RT acquired thermotolerance in Arabidopsis.";
RL Plant Physiol. 143:251-262(2007).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20856808; DOI=10.1371/journal.pone.0012761;
RA Prasad B.D., Goel S., Krishna P.;
RT "In silico identification of carboxylate clamp type tetratricopeptide
RT repeat proteins in Arabidopsis and rice as putative co-chaperones of
RT Hsp90/Hsp70.";
RL PLoS ONE 5:E12761-E12761(2010).
CC -!- FUNCTION: Mediates the association of the molecular chaperones HSP70
CC and HSP90. Mediates nuclear encoded chloroplast preproteins binding to
CC HSP90 prior to chloroplastic sorting (By similarity). Involved in
CC acclimation to heat. {ECO:0000250, ECO:0000269|PubMed:17085506}.
CC -!- SUBUNIT: Co-chaperone that forms a complex with HSP70 and HSP90 and
CC preproteins (e.g. chloroplast preproteins) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9STH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9STH1-2; Sequence=VSP_053940, VSP_053941;
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 -!- DISRUPTION PHENOTYPE: Decreased thermotolerance after a long recovery
CC (2 days) under nonstress conditions following an acclimation heat
CC treatment. {ECO:0000269|PubMed:17085506}.
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DR EMBL; AL080318; CAB45987.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78283.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83125.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83126.1; -; Genomic_DNA.
DR EMBL; AY140001; AAM98143.1; -; mRNA.
DR EMBL; AK317040; BAH19733.1; -; mRNA.
DR PIR; T48150; T48150.
DR RefSeq; NP_001031620.1; NM_001036543.2. [Q9STH1-1]
DR RefSeq; NP_192977.2; NM_117310.4. [Q9STH1-2]
DR AlphaFoldDB; Q9STH1; -.
DR SMR; Q9STH1; -.
DR BioGRID; 12147; 15.
DR STRING; 3702.AT4G12400.2; -.
DR iPTMnet; Q9STH1; -.
DR PaxDb; Q9STH1; -.
DR PRIDE; Q9STH1; -.
DR ProteomicsDB; 228752; -. [Q9STH1-1]
DR EnsemblPlants; AT4G12400.1; AT4G12400.1; AT4G12400. [Q9STH1-2]
DR EnsemblPlants; AT4G12400.2; AT4G12400.2; AT4G12400. [Q9STH1-1]
DR GeneID; 826849; -.
DR Gramene; AT4G12400.1; AT4G12400.1; AT4G12400. [Q9STH1-2]
DR Gramene; AT4G12400.2; AT4G12400.2; AT4G12400. [Q9STH1-1]
DR KEGG; ath:AT4G12400; -.
DR Araport; AT4G12400; -.
DR TAIR; locus:2139109; AT4G12400.
DR eggNOG; KOG0548; Eukaryota.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q9STH1; -.
DR OMA; HYSKAWE; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; Q9STH1; -.
DR PRO; PR:Q9STH1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STH1; baseline and differential.
DR Genevisible; Q9STH1; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; ISS:UniProtKB.
DR GO; GO:0070678; F:preprotein binding; ISS:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:UniProtKB.
DR GO; GO:0010286; P:heat acclimation; IMP: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; 2.
DR Pfam; PF00515; TPR_1; 3.
DR Pfam; PF13181; TPR_8; 1.
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; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Chaperone; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Stress response; TPR repeat.
FT CHAIN 1..558
FT /note="Hsp70-Hsp90 organizing protein 3"
FT /id="PRO_0000426703"
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 131..170
FT /note="STI1 1"
FT REPEAT 136..173
FT /note="TPR 4"
FT REPEAT 230..263
FT /note="TPR 5"
FT REPEAT 265..297
FT /note="TPR 6"
FT REPEAT 305..342
FT /note="TPR 7"
FT REPEAT 369..402
FT /note="TPR 8"
FT REPEAT 404..436
FT /note="TPR 9"
FT REPEAT 437..470
FT /note="TPR 10"
FT DOMAIN 507..546
FT /note="STI1 2"
FT REGION 191..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 227..244
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 193..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 523..530
FT /note="LVDFQENP -> KAVASIVF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053940"
FT VAR_SEQ 531..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_053941"
FT CONFLICT 98
FT /note="E -> G (in Ref. 4; BAH19733)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="E -> K (in Ref. 3; AAM98143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 63706 MW; 47010D35F0F98DB9 CRC64;
MAEEAKSKGN AAFSSGDYAT AITHFTEAIN LSPTNHILYS NRSASYASLH RYEEALSDAK
KTIELKPDWS KGYSRLGAAF IGLSKFDEAV DSYKKGLEID PSNEMLKSGL ADASRSRVSS
KSNPFVDAFQ GKEMWEKLTA DPGTRVYLEQ DDFVKTMKEI QRNPNNLNLY MKDKRVMKAL
GVLLNVKFGG SSGEDTEMKE ADERKEPEPE MEPMELTEEE RQKKERKEKA LKEKGEGNVA
YKKKDFGRAV EHYTKAMELD DEDISYLTNR AAVYLEMGKY EECIEDCDKA VERGRELRSD
FKMIARALTR KGSALVKMAR CSKDFEPAIE TFQKALTEHR NPDTLKKLND AEKVKKELEQ
QEYFDPTIAE EEREKGNGFF KEQKYPEAVK HYSEAIKRNP NDVRAYSNRA ACYTKLGALP
EGLKDAEKCI ELDPSFTKGY SRKGAIQFFM KEYDKAMETY QEGLKHDPKN QEFLDGVRRC
VEQINKASRG DLTPEELKER QAKAMQDPEV QNILSDPVMR QVLVDFQENP KAAQEHMKNP
MVMNKIQKLV SAGIVQVR
