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HSP7G_ARATH
ID   HSP7G_ARATH             Reviewed;         718 AA.
AC   Q9LTX9; Q8RXD1; Q9M637;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Heat shock 70 kDa protein 7, chloroplastic;
DE   AltName: Full=Chloroplast heat shock protein 70-2;
DE            Short=cpHsc70-2;
DE   AltName: Full=Heat shock protein 70-7;
DE            Short=AtHsp70-7;
DE   Flags: Precursor;
GN   Name=HSP70-7; Synonyms=CPHSC70-2, HSC70-7; OrderedLocusNames=At5g49910;
GN   ORFNames=K9P8.5;
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 [MRNA] (ISOFORM 1), DNAK GENE SUBFAMILY, INDUCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [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   SUBCELLULAR LOCATION.
RX   PubMed=18997426; DOI=10.1271/bbb.80408;
RA   Ratnayake R.M., Inoue H., Nonami H., Akita M.;
RT   "Alternative processing of Arabidopsis Hsp70 precursors during protein
RT   import into chloroplasts.";
RL   Biosci. Biotechnol. Biochem. 72:2926-2935(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=18192441; DOI=10.1104/pp.107.114496;
RA   Su P.H., Li H.M.;
RT   "Arabidopsis stromal 70-kD heat shock proteins are essential for plant
RT   development and important for thermotolerance of germinating seeds.";
RL   Plant Physiol. 146:1231-1241(2008).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20506024; DOI=10.1007/s00425-010-1192-z;
RA   Latijnhouwers M., Xu X.M., Moeller S.G.;
RT   "Arabidopsis stromal 70-kDa heat shock proteins are essential for
RT   chloroplast development.";
RL   Planta 232:567-578(2010).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20484004; DOI=10.1105/tpc.109.071415;
RA   Su P.H., Li H.M.;
RT   "Stromal Hsp70 is important for protein translocation into pea and
RT   Arabidopsis chloroplasts.";
RL   Plant Cell 22:1516-1531(2010).
CC   -!- FUNCTION: Acts redundantly with HSP70-6 in the thermotolerance of
CC       germinating seeds. Plays an important role in the protein precursor
CC       import into chloroplasts. {ECO:0000269|PubMed:18192441,
CC       ECO:0000269|PubMed:20484004, ECO:0000269|PubMed:20506024}.
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: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LTX9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LTX9-2; Sequence=VSP_042242, VSP_042243;
CC   -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC       regulated during germination. {ECO:0000269|PubMed:11402207}.
CC   -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11402207}.
CC   -!- DISRUPTION PHENOTYPE: Defective in protein import into chloroplasts
CC       during early developmental stages. {ECO:0000269|PubMed:20484004}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
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; AF217459; AAF27639.1; -; mRNA.
DR   EMBL; AB024032; BAA97012.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95870.1; -; Genomic_DNA.
DR   EMBL; BT000919; AAN41319.1; -; mRNA.
DR   EMBL; AY081331; AAL91220.1; -; mRNA.
DR   EMBL; BT008452; AAP37811.1; -; mRNA.
DR   RefSeq; NP_199802.1; NM_124369.4. [Q9LTX9-1]
DR   AlphaFoldDB; Q9LTX9; -.
DR   SMR; Q9LTX9; -.
DR   BioGRID; 20300; 35.
DR   IntAct; Q9LTX9; 1.
DR   MINT; Q9LTX9; -.
DR   STRING; 3702.AT5G49910.1; -.
DR   iPTMnet; Q9LTX9; -.
DR   World-2DPAGE; 0003:Q9LTX9; -.
DR   PaxDb; Q9LTX9; -.
DR   PRIDE; Q9LTX9; -.
DR   ProteomicsDB; 230253; -. [Q9LTX9-1]
DR   EnsemblPlants; AT5G49910.1; AT5G49910.1; AT5G49910. [Q9LTX9-1]
DR   GeneID; 835054; -.
DR   Gramene; AT5G49910.1; AT5G49910.1; AT5G49910. [Q9LTX9-1]
DR   KEGG; ath:AT5G49910; -.
DR   Araport; AT5G49910; -.
DR   TAIR; locus:2158834; AT5G49910.
DR   eggNOG; KOG0102; Eukaryota.
DR   HOGENOM; CLU_005965_2_4_1; -.
DR   InParanoid; Q9LTX9; -.
DR   OMA; QIHILGG; -.
DR   OrthoDB; 288077at2759; -.
DR   PhylomeDB; Q9LTX9; -.
DR   PRO; PR:Q9LTX9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LTX9; baseline and differential.
DR   Genevisible; Q9LTX9; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; 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:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
DR   GO; GO:0009408; P:response to heat; IEP:TAIR.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
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   TIGRFAMs; TIGR02350; prok_dnaK; 1.
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   Alternative splicing; ATP-binding; Chaperone; Chloroplast;
KW   Nucleotide-binding; Plastid; Protein transport; Reference proteome;
KW   Stress response; Transit peptide; Transport.
FT   TRANSIT         1..92
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           93..718
FT                   /note="Heat shock 70 kDa protein 7, chloroplastic"
FT                   /id="PRO_0000415426"
FT   REGION          668..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         353..371
FT                   /note="SLPFITATADGPKHIETTL -> RFTFPSQIYLPRSHWYVGY (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_042242"
FT   VAR_SEQ         372..718
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_042243"
FT   CONFLICT        18..21
FT                   /note="TSSS -> NSFC (in Ref. 1; AAF27639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="T -> S (in Ref. 1; AAF27639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="L -> F (in Ref. 1; AAF27639)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        562
FT                   /note="K -> Q (in Ref. 1; AAF27639)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   718 AA;  76997 MW;  FFD96CC29E3A463B CRC64;
     MASSAAQIHI LGGIGFPTSS SSSSTKNLDN KTNSIPRSVF FGNRTSPFTT PTSAFLRMGR
     RNNNASRYTV GPVRVVNEKV VGIDLGTTNS AVAAMEGGKP TIVTNAEGQR TTPSVVAYTK
     SKDRLVGQIA KRQAVVNPEN TFFSVKRFIG RRMNEVAEES KQVSYRVIKD ENGNVKLDCP
     AIGKQFAAEE ISAQVLRKLV DDASRFLNDK VTKAVITVPA YFNDSQRTAT KDAGRIAGLE
     VLRIINEPTA ASLAYGFERK SNETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG
     DDFDKRVVDW LASTFKKDEG IDLLKDKQAL QRLTEAAEKA KIELSSLTQT NMSLPFITAT
     ADGPKHIETT LTRGKFEELC SDLLDRVRTP VENSLRDAKL SFKDIDEVIL VGGSTRIPAV
     QDLVRKLTGK EPNVSVNPDE VVALGAAVQA GVLSGDVSDI VLLDVTPLSL GLETLGGVMT
     KIIPRNTTLP TSKSEVFSTA ADGQTSVEIN VLQGEREFVR DNKSIGSFRL DGIPPAPRGV
     PQIEVKFDID ANGILSVSAS DKGTGKKQDI TITGASTLPK DEVDTMVQEA ERFAKEDKEK
     RDAIDTKNQA DSVVYQTEKQ LKELGEKIPG PVKEKVEAKL QELKEKIASG STQEIKDTMA
     ALNQEVMQIG QSLYNQPQPG GADSPPGGEA SSSSDTSSSA KGGDNGGDVI DADFTDSN
 
 
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