HSP7P_ARATH
ID HSP7P_ARATH Reviewed; 831 AA.
AC F4HQD4; Q8VZ83; Q9CA95;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Heat shock 70 kDa protein 15;
DE AltName: Full=Heat shock protein 70-15;
DE Short=AtHsp70-15;
GN Name=HSP70-15; OrderedLocusNames=At1g79920; ORFNames=F19K16.12;
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:gaoths>2.0.co;2;
RA Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.;
RT "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
RL Cell Stress Chaperones 6:201-208(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-536, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21418353; DOI=10.1111/j.1365-313x.2011.04558.x;
RA Jungkunz I., Link K., Vogel F., Voll L.M., Sonnewald S., Sonnewald U.;
RT "AtHsp70-15-deficient Arabidopsis plants are characterized by reduced
RT growth, a constitutive cytosolic protein response and enhanced resistance
RT to TuMV.";
RL Plant J. 66:983-995(2011).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s are key
CC components that facilitate folding of de novo synthesized proteins,
CC assist translocation of precursor proteins into organelles, and are
CC responsible for degradation of damaged protein under stress conditions.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21418353}. Nucleus
CC {ECO:0000269|PubMed:21418353}. Note=Predominantly detected in the
CC cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=F4HQD4-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Knockout mutation impairs stomatal closure and
CC accelerates wilting, enhances sensitivity to heat treatment, and
CC strengthens tolerance to potyvirus TuMV infection.
CC {ECO:0000269|PubMed:21418353}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC HSP110/SSE subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011717; AAG52244.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY065177; AAL38353.1; -; mRNA.
DR EMBL; BT000810; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D96830; D96830.
DR RefSeq; NP_001319422.1; NM_001334936.1.
DR RefSeq; NP_001322111.1; NM_001334937.1.
DR RefSeq; NP_178110.7; NM_106641.8.
DR AlphaFoldDB; F4HQD4; -.
DR SMR; F4HQD4; -.
DR BioGRID; 29550; 11.
DR STRING; 3702.AT1G79920.1; -.
DR iPTMnet; F4HQD4; -.
DR PaxDb; F4HQD4; -.
DR PeptideAtlas; F4HQD4; -.
DR PRIDE; F4HQD4; -.
DR GeneID; 844332; -.
DR KEGG; ath:AT1G79920; -.
DR Araport; AT1G79920; -.
DR TAIR; locus:2017859; AT1G79920.
DR eggNOG; KOG0103; Eukaryota.
DR InParanoid; F4HQD4; -.
DR PhylomeDB; F4HQD4; -.
DR PRO; PR:F4HQD4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HQD4; baseline and differential.
DR Genevisible; F4HQD4; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 2.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 2.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..831
FT /note="Heat shock 70 kDa protein 15"
FT /id="PRO_0000415433"
FT REGION 502..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 792
FT /note="A -> T (in Ref. 3; AAL38353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 91681 MW; BBDBB4ADF08D31ED CRC64;
MSVVGFDFGN ENCLVAVARQ RGIDVVLNDE SNRETPAIVC FGDKQRFIGT AGAASTMMNP
KNSISQIKRL IGRQFSDPEL QRDIKSLPFS VTEGPDGYPL IHANYLGEIR AFTPTQVMGM
MLSNLKGIAE KNLNTAVVDC CIGIPVYFTD LQRRAVLDAA TIAGLHPLHL IHETTATALA
YGIYKTDLPE NDQLNVAFID IGHASMQVCI AGFKKGQLKI LSHAFDRSLG GRDFDEVLFN
HFAAKFKDEY KIDVSQNAKA SLRLRATCEK LKKVLSANPM APLNIECLMA EKDVRGVIKR
EEFEEISIPI LERVKRPLEK ALSDAGLTVE DVHMVEVVGS GSRVPAMIKI LTEFFGKEPR
RTMNASECVS RGCALQCAIL SPTFKVREFQ VHESFPFSIS LAWKGAATDA QNGGTENQQS
TIVFPKGNPI PSVKALTFYR SGTFSIDVQY SDVNDLQAPP KISTYTIGPF QSSKGERAKL
KVKVRLNLHG IVSVESATLL EEEEVEVSVT KDQSEETAKM DTDKASAEAA PASGDSDVNM
QDAKDTSDAT GTDNGVPESA EKPVQMETDS KAEAPKKKVK KTNVPLSELV YGALKTVEVE
KAVEKEFEMA LQDRVMEETK DRKNAVESYV YDMRNKLSDK YQEYITDSER EAFLANLQEV
EDWLYEDGED ETKGVYVAKL EELKKVGDPV EVRYKESLER GSVIDQLGYC INSYREAAVS
NDPKFDHIEL AEKQKVLNEC VEAEAWLREK QQQQDTLPKY ATPALLSADV KSKAEALDKF
CRPIMTKPKP AAKAEAPQAK GGEQADEGKS EPEQPASAEA METENPAEGS T
