HSOP1_ARATH
ID HSOP1_ARATH Reviewed; 572 AA.
AC Q9LNB6; Q7Y1Y9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Hsp70-Hsp90 organizing protein 1;
DE Short=AtHop1;
DE AltName: Full=Stress-induced-phosphoprotein 1;
DE Short=STI1;
GN Name=HOP1; OrderedLocusNames=At1g12270; ORFNames=F5O11.2;
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 [MRNA] OF 408-572.
RA Shen W.H.;
RT "Proteins contain similarity to TPR domains.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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}.
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DR EMBL; AC025416; AAF79628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28860.1; -; Genomic_DNA.
DR EMBL; AY064967; AAL38384.1; -; mRNA.
DR EMBL; BT000651; AAN18217.1; -; mRNA.
DR EMBL; AJ319538; CAC85343.1; -; mRNA.
DR PIR; H86257; H86257.
DR RefSeq; NP_172691.1; NM_101099.5.
DR AlphaFoldDB; Q9LNB6; -.
DR SMR; Q9LNB6; -.
DR BioGRID; 23021; 18.
DR IntAct; Q9LNB6; 2.
DR STRING; 3702.AT1G12270.1; -.
DR iPTMnet; Q9LNB6; -.
DR MetOSite; Q9LNB6; -.
DR PaxDb; Q9LNB6; -.
DR PRIDE; Q9LNB6; -.
DR ProteomicsDB; 230217; -.
DR EnsemblPlants; AT1G12270.1; AT1G12270.1; AT1G12270.
DR GeneID; 837781; -.
DR Gramene; AT1G12270.1; AT1G12270.1; AT1G12270.
DR KEGG; ath:AT1G12270; -.
DR Araport; AT1G12270; -.
DR TAIR; locus:2034620; AT1G12270.
DR eggNOG; KOG0548; Eukaryota.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; Q9LNB6; -.
DR OMA; ARCESGD; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; Q9LNB6; -.
DR PRO; PR:Q9LNB6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNB6; baseline and differential.
DR Genevisible; Q9LNB6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; 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: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; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 2.
DR Pfam; PF13181; TPR_8; 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 2: Evidence at transcript 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_0000426701"
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 133..172
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 358..382
FT /note="TPR 7"
FT REPEAT 383..416
FT /note="TPR 8"
FT REPEAT 418..450
FT /note="TPR 9"
FT REPEAT 451..484
FT /note="TPR 10"
FT DOMAIN 521..560
FT /note="STI1 2"
FT REGION 189..248
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 213..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5XEP2"
SQ SEQUENCE 572 AA; 64585 MW; 57F1BADE195D7C63 CRC64;
MAEEAKAKGN AAFSSGDFTT AINHFTEAIA LAPTNHVLFS NRSAAHASLH QYAEALSDAK
ETIKLKPYWP KGYSRLGAAH LGLNQFELAV TAYKKGLDVD PTNEALKSGL ADAEASVARS
RAAPNPFGDA FQGPEMWTKL TSDPSTRGFL QQPDFVNMMQ EIQKNPSSLN LYLKDQRVMQ
SLGVLLNVKF RPPPPQGDEA EVPESDMGQS SSNEPEVEKK REPEPEPEPE VTEEKEKKER
KEKAKKEKEL GNAAYKKKDF ETAIQHYSTA IEIDDEDISY LTNRAAVYLE MGKYNECIED
CNKAVERGRE LRSDYKMVAR ALTRKGTALT KMAKCSKDYE PAIEAFQKAL TEHRNPDTLK
RLNDAERAKK EWEQKQYFDP KLGDEEREKG NDFFKEQKYP EAIKHYTEAI KRNPNDHKAY
SNRAASYTKL GAMPEGLKDA EKCIELDPTF SKGYSRKAAV QFFLKEYDNA METYQAGLEH
DPSNQELLDG VKRCVQQINK ANRGDLTPEE LKERQAKGMQ DPEIQNILTD PVMRQVLSDL
QENPSAAQKH MQNPMVMNKI QKLISAGIVQ MK
