HSOP2_ARATH
ID HSOP2_ARATH Reviewed; 571 AA.
AC Q5XEP2; Q84TJ2; Q9SI76;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Hsp70-Hsp90 organizing protein 2;
DE Short=AtHop2;
GN Name=HOP2; OrderedLocusNames=At1g62740; ORFNames=F23N19.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
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). {ECO:0000250}.
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 -!- 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=AAF19538.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007190; AAF19538.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33999.1; -; Genomic_DNA.
DR EMBL; BT005735; AAO64147.1; -; mRNA.
DR EMBL; BT015924; AAU95460.1; -; mRNA.
DR EMBL; BT020538; AAW70384.1; -; mRNA.
DR EMBL; AK228637; BAF00546.1; -; mRNA.
DR RefSeq; NP_176461.1; NM_104951.4.
DR AlphaFoldDB; Q5XEP2; -.
DR SMR; Q5XEP2; -.
DR BioGRID; 27793; 17.
DR IntAct; Q5XEP2; 2.
DR STRING; 3702.AT1G62740.1; -.
DR iPTMnet; Q5XEP2; -.
DR MetOSite; Q5XEP2; -.
DR PaxDb; Q5XEP2; -.
DR PRIDE; Q5XEP2; -.
DR ProteomicsDB; 230154; -.
DR EnsemblPlants; AT1G62740.1; AT1G62740.1; AT1G62740.
DR GeneID; 842572; -.
DR Gramene; AT1G62740.1; AT1G62740.1; AT1G62740.
DR KEGG; ath:AT1G62740; -.
DR Araport; AT1G62740; -.
DR TAIR; locus:2026197; AT1G62740.
DR eggNOG; KOG0548; Eukaryota.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q5XEP2; -.
DR OMA; TCNDAID; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; Q5XEP2; -.
DR PRO; PR:Q5XEP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XEP2; baseline and differential.
DR Genevisible; Q5XEP2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
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; 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..571
FT /note="Hsp70-Hsp90 organizing protein 2"
FT /id="PRO_0000426702"
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 134..173
FT /note="STI1 1"
FT REPEAT 243..276
FT /note="TPR 4"
FT REPEAT 278..310
FT /note="TPR 5"
FT REPEAT 322..355
FT /note="TPR 6"
FT REPEAT 382..415
FT /note="TPR 7"
FT REPEAT 417..449
FT /note="TPR 8"
FT REPEAT 450..483
FT /note="TPR 9"
FT DOMAIN 520..559
FT /note="STI1 2"
FT REGION 117..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..257
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 205..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 349
FT /note="L -> I (in Ref. 3; AAO64147 and 5; BAF00546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 64520 MW; 0AB71C7433DF1CFB CRC64;
MADEAKAKGN AAFSSGDFNS AVNHFTDAIN LTPTNHVLFS NRSAAHASLN HYDEALSDAK
KTVELKPDWG KGYSRLGAAH LGLNQFDEAV EAYSKGLEID PSNEGLKSGL ADAKASASRS
RASAPNPFGD AFQGPEMWSK LTADPSTRGL LKQPDFVNMM KEIQRNPSNL NLYLQDQRVM
QALGVLLNIQ IRTQQAGDDM EIGEEEMAVP SRKEPEVEKK RKPEPEPEPE PEFGEEKQKK
LKAQKEKELG NAAYKKKDFE TAIQHYSTAM EIDDEDISYI TNRAAVHLEM GKYDECIKDC
DKAVERGREL RSDYKMVAKA LTRKGTALGK MAKVSKDYEP VIQTYQKALT EHRNPETLKR
LNEAERAKKE LEQQEYYDPN IGDEEREKGN DFFKEQKYPD AVRHYTEAIK RNPKDPRAYS
NRAACYTKLG AMPEGLKDAE KCIELDPTFL KGYSRKGAVQ FFMKEYDNAM ETYQKGLEHD
PNNQELLDGV KRCVQQINKA NRGDLTPEEL KERQAKGMQD PEIQNILTDP VMRQVLSDLQ
ENPAAAQKHM QNPMIMNKIQ KLISSGIVQM K
