HSP7E_ARATH
ID HSP7E_ARATH Reviewed; 646 AA.
AC Q9S9N1;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Heat shock 70 kDa protein 5;
DE AltName: Full=Heat shock protein 70-5;
DE Short=AtHsp70-5;
DE AltName: Full=Heat shock protein 70b;
GN Name=HSP70-5; Synonyms=HSP70B; OrderedLocusNames=At1g16030;
GN ORFNames=T24D18.14;
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 DNAK GENE SUBFAMILY, AND INDUCTION.
RX PubMed=11402207; DOI=10.1104/pp.126.2.789;
RA Sung D.Y., Vierling E., Guy C.L.;
RT "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene
RT family.";
RL Plant Physiol. 126:789-800(2001).
RN [6]
RP INDUCTION.
RX PubMed=15805473; DOI=10.1104/pp.104.058958;
RA Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
RT "Virus induction of heat shock protein 70 reflects a general response to
RT protein accumulation in the plant cytosol.";
RL Plant Physiol. 138:529-536(2005).
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:0000305}.
CC -!- INDUCTION: By heat shock. Up-regulated by virus infection.
CC {ECO:0000269|PubMed:11402207, ECO:0000269|PubMed:15805473}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010924; AAF18501.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29402.1; -; Genomic_DNA.
DR EMBL; BT001988; AAN71999.1; -; mRNA.
DR EMBL; BT008401; AAP37760.1; -; mRNA.
DR PIR; B86295; B86295.
DR RefSeq; NP_173055.1; NM_101471.3.
DR AlphaFoldDB; Q9S9N1; -.
DR SMR; Q9S9N1; -.
DR BioGRID; 23414; 10.
DR IntAct; Q9S9N1; 4.
DR MINT; Q9S9N1; -.
DR STRING; 3702.AT1G16030.1; -.
DR PaxDb; Q9S9N1; -.
DR PRIDE; Q9S9N1; -.
DR ProteomicsDB; 230155; -.
DR EnsemblPlants; AT1G16030.1; AT1G16030.1; AT1G16030.
DR GeneID; 838174; -.
DR Gramene; AT1G16030.1; AT1G16030.1; AT1G16030.
DR KEGG; ath:AT1G16030; -.
DR Araport; AT1G16030; -.
DR TAIR; locus:2200462; AT1G16030.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; Q9S9N1; -.
DR OMA; ELATFME; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9S9N1; -.
DR PRO; PR:Q9S9N1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9N1; baseline and differential.
DR Genevisible; Q9S9N1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..646
FT /note="Heat shock 70 kDa protein 5"
FT /id="PRO_0000415424"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70915 MW; 46137E1DC9139895 CRC64;
MATKSEKAIG IDLGTTYSCV GVWMNDRVEI IPNDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VALNPQNTVF DAKRLIGRKF SDPSVQSDIL HWPFKVVSGP GEKPMIVVSY KNEEKQFSPE
EISSMVLVKM KEVAEAFLGR TVKNAVVTVP AYFNDSQRQA TKDAGAISGL NVLRIINEPT
AAAIAYGLDK KGTKAGEKNV LIFDLGGGTF DVSLLTIEEG VFEVKATAGD THLGGEDFDN
RLVNHFVAEF RRKHKKDIAG NARALRRLRT ACERAKRTLS STAQTTIEID SLHEGIDFYA
TISRARFEEM NMDLFRKCMD PVEKVLKDAK LDKSSVHDVV LVGGSTRIPK IQQLLQDFFN
GKELCKSINP DEAVAYGAAV QAAILTGEGS EKVQDLLLLD VAPLSLGLET AGGVMTVLIP
RNTTVPCKKE QVFSTYADNQ PGVLIQVYEG ERARTRDNNL LGTFELKGIP PAPRGVPQIN
VCFDIDANGI LNVSAEDKTA GVKNQITITN DKGRLSKEEI EKMVQDAEKY KAEDEQVKKK
VEAKNSLENY AYNMRNTIKD EKLAQKLTQE DKQKIEKAID ETIEWIEGNQ LAEVDEFEYK
LKELEGICNP IISKMYQGGA AAGGMPTDGD FSSSGAAGGP KIEEVD
