HSP7H_ARATH
ID HSP7H_ARATH Reviewed; 563 AA.
AC Q9SKY8; Q8L8N8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Heat shock 70 kDa protein 8;
DE AltName: Full=Heat shock protein 70-8;
DE Short=AtHsp70-8;
DE AltName: Full=Heat-shock protein 70T-2;
GN Name=HSP70-8; Synonyms=HSP70T-2; OrderedLocusNames=At2g32120;
GN ORFNames=F22D22.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP DNAK GENE SUBFAMILY.
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
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DR EMBL; AC006223; AAD15393.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08636.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08637.1; -; Genomic_DNA.
DR EMBL; AY123990; AAM74502.1; -; mRNA.
DR EMBL; BT001079; AAN46859.1; -; mRNA.
DR EMBL; AY088895; AAM67201.1; -; mRNA.
DR PIR; B84729; B84729.
DR RefSeq; NP_180771.1; NM_128771.4.
DR RefSeq; NP_850183.1; NM_179852.3.
DR AlphaFoldDB; Q9SKY8; -.
DR SMR; Q9SKY8; -.
DR STRING; 3702.AT2G32120.1; -.
DR iPTMnet; Q9SKY8; -.
DR PaxDb; Q9SKY8; -.
DR PRIDE; Q9SKY8; -.
DR ProteomicsDB; 232091; -.
DR EnsemblPlants; AT2G32120.1; AT2G32120.1; AT2G32120.
DR EnsemblPlants; AT2G32120.2; AT2G32120.2; AT2G32120.
DR GeneID; 817771; -.
DR Gramene; AT2G32120.1; AT2G32120.1; AT2G32120.
DR Gramene; AT2G32120.2; AT2G32120.2; AT2G32120.
DR KEGG; ath:AT2G32120; -.
DR Araport; AT2G32120; -.
DR TAIR; locus:2045457; AT2G32120.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; Q9SKY8; -.
DR OMA; ELYSGMN; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9SKY8; -.
DR PRO; PR:Q9SKY8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKY8; baseline and differential.
DR Genevisible; Q9SKY8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:TAIR.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
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; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Chaperone; Nucleotide-binding;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..563
FT /note="Heat shock 70 kDa protein 8"
FT /id="PRO_0000415427"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 270
FT /note="N -> S (in Ref. 4; AAM67201)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="V -> A (in Ref. 4; AAM67201)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="S -> T (in Ref. 4; AAM67201)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="L -> F (in Ref. 4; AAM67201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 60989 MW; F537CE0865066D6D CRC64;
MAEAAYTVAS DSENTGEEKS SSSPSLPEIA LGIDIGTSQC SIAVWNGSQV HILRNTRNQK
LIKSFVTFKD EVPAGGVSNQ LAHEQEMLTG AAIFNMKRLV GRVDTDPVVH ASKNLPFLVQ
TLDIGVRPFI AALVNNAWRS TTPEEVLAIF LVELRLMAEA QLKRPVRNVV LTVPVSFSRF
QLTRFERACA MAGLHVLRLM PEPTAIALLY AQQQQMTTHD NMGSGSERLA VIFNMGAGYC
DVAVTATAGG VSQIKALAGS PIGGEDILQN TIRHIAPPNE EASGLLRVAA QDAIHRLTDQ
ENVQIEVDLG NGNKISKVLD RLEFEEVNQK VFEECERLVV QCLRDARVNG GDIDDLIMVG
GCSYIPKVRT IIKNVCKKDE IYKGVNPLEA AVRGAALEGA VTSGIHDPFG SLDLLTIQAT
PLAVGVRANG NKFIPVIPRN TMVPARKDLF FTTVQDNQKE ALIIIYEGEG ETVEENHLLG
YFKLVGIPPA PKGVPEINVC MDIDASNALR VFAAVLMPGS SSPVVPVIEV RMPTVDDGHG
WCAQALNVKY GATLDLITLQ RKM
