HSP7O_ARATH
ID HSP7O_ARATH Reviewed; 831 AA.
AC Q9S7C0; Q0WVB9; Q96269;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Heat shock 70 kDa protein 14;
DE AltName: Full=Heat shock protein 70-14;
DE Short=AtHsp70-14;
DE AltName: Full=Heat shock protein 91;
GN Name=HSP70-14; Synonyms=HSP91; OrderedLocusNames=At1g79930;
GN ORFNames=F18B13.1, F19K16.11;
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), TISSUE SPECIFICITY, AND INDUCTION
RP BY HEAT.
RX PubMed=8706819; DOI=10.1016/0014-5793(96)00640-0;
RA Storozhenko S., De Pauw P., Kushnir S., Van Montagu M., Inze D.;
RT "Identification of an Arabidopsis thaliana cDNA encoding a HSP70-related
RT protein belonging to the HSP110/SSE1 subfamily.";
RL FEBS Lett. 390:113-118(1996).
RN [2]
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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN [8]
RP INTERACTION WITH HTT1, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=24728648; DOI=10.1105/tpc.114.124883;
RA Li S., Liu J., Liu Z., Li X., Wu F., He Y.;
RT "HEAT-INDUCED TAS1 TARGET1 Mediates Thermotolerance via HEAT STRESS
RT TRANSCRIPTION FACTOR A1a-Directed Pathways in Arabidopsis.";
RL Plant Cell 26:1764-1780(2014).
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 -!- SUBUNIT: Interacts with HTT1 in both cytoplasm and nucleus.
CC {ECO:0000269|PubMed:24728648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21418353,
CC ECO:0000269|PubMed:24728648}. Nucleus {ECO:0000269|PubMed:21418353,
CC ECO:0000269|PubMed:24728648}. Note=Predominantly detected in the
CC cytoplasm. {ECO:0000269|PubMed:21418353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9S7C0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S7C0-2; Sequence=VSP_042245, VSP_042246;
CC -!- TISSUE SPECIFICITY: Constitutively expressed.
CC {ECO:0000269|PubMed:8706819}.
CC -!- INDUCTION: By heat. {ECO:0000269|PubMed:8706819}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
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}.
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DR EMBL; Z70314; CAA94389.1; -; mRNA.
DR EMBL; AC009322; AAD55461.1; -; Genomic_DNA.
DR EMBL; AC011717; AAG52240.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36327.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36328.1; -; Genomic_DNA.
DR EMBL; AY079015; AAL84971.1; -; mRNA.
DR EMBL; BT002625; AAO11541.1; -; mRNA.
DR EMBL; AK226836; BAE98929.1; -; mRNA.
DR PIR; E96830; E96830.
DR PIR; S74252; S74252.
DR RefSeq; NP_001031305.1; NM_001036228.2. [Q9S7C0-2]
DR RefSeq; NP_178111.1; NM_106642.5. [Q9S7C0-1]
DR AlphaFoldDB; Q9S7C0; -.
DR SMR; Q9S7C0; -.
DR BioGRID; 29551; 11.
DR STRING; 3702.AT1G79930.1; -.
DR MetOSite; Q9S7C0; -.
DR PaxDb; Q9S7C0; -.
DR PRIDE; Q9S7C0; -.
DR ProteomicsDB; 232120; -. [Q9S7C0-1]
DR EnsemblPlants; AT1G79930.1; AT1G79930.1; AT1G79930. [Q9S7C0-1]
DR EnsemblPlants; AT1G79930.2; AT1G79930.2; AT1G79930. [Q9S7C0-2]
DR GeneID; 844333; -.
DR Gramene; AT1G79930.1; AT1G79930.1; AT1G79930. [Q9S7C0-1]
DR Gramene; AT1G79930.2; AT1G79930.2; AT1G79930. [Q9S7C0-2]
DR KEGG; ath:AT1G79930; -.
DR Araport; AT1G79930; -.
DR TAIR; locus:2016364; AT1G79930.
DR eggNOG; KOG0103; Eukaryota.
DR InParanoid; Q9S7C0; -.
DR OMA; AYDRHFG; -.
DR OrthoDB; 406172at2759; -.
DR PhylomeDB; Q9S7C0; -.
DR PRO; PR:Q9S7C0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7C0; baseline and differential.
DR Genevisible; Q9S7C0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:TAIR.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 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 14"
FT /id="PRO_0000415432"
FT REGION 503..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..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 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:0000250|UniProtKB:F4HQD4"
FT VAR_SEQ 779..789
FT /note="KFCRPIMTKPK -> NYGCFTGFAGL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042245"
FT VAR_SEQ 790..831
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042246"
FT CONFLICT 4
FT /note="V -> I (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="KQ -> NE (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> F (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="V -> A (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="G -> S (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="R -> T (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="V -> A (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="A -> G (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="E -> G (in Ref. 1; CAA94389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 91750 MW; AEE1CC1C4FC122D7 CRC64;
MSVVGFDFGN ENCLVAVARQ RGIDVVLNDE SNRETPAIVC FGDKQRFIGT AGAASTMMNP
KNSISQIKRL IGRQFSDPEL QRDIKSLPFS VTEGPDGYPL IHANYLGEKR AFTPTQVMGM
MLSNLKGIAE KNLNTAVVDC CIGIPVYFTD LQRRAVLDAA TIAGLHPLRL IHETTATALA
YGIYKTDLPE SDQLNVAFID IGHASMQVCI AGFKKGQLKI LSHAFDRSLG GRDFDEVLFN
HFAAKFKDEY KIDVSQNAKA SLRLRATCEK LKKVLSANPL APLNIECLMD EKDVRGVIKR
EEFEEISIPI LERVKRPLEK ALSDAGLTVE DVHMVEVIGS GSRVPAMIKI LTEFFGKEPR
RTMNASECVS RGCALQCAIL SPTFKVREFQ VHESFPFSIS LAWKGAASEA QNGGAENQQS
TIVFPKGNPI PSVKALTFYR SGTFSVDVQY SDVNDLQAPP KISTYTIGPF QSSKGERAKL
KVKVRLNLHG IVSVESATLL EEEEVEVPVT KEHSEETTKM DSDKASAEAA PASGDCDVNM
QDAKDTSDAT GTDNGVPESA EKPVQMETDS KAEAPKKKVK KTNVPLSELV YGALKTVEVE
KAVEKEFEMA LQDRVMEETK DRKNAVESYV YDMRNKLSDK YQEYITDSER EAFLANLQEV
EDWLYEDGED ETKGVYVAKL EELKKVGDPV EVRYKESLER GSVIDQLGYC INSYREAAMS
TDPKFDHIEL AEKQKVLNEC VEAEAWLRGK QQQQDTLPKY ATPALLSADV KSKAEALDKF
CRPIMTKPKP VAKAEAPQAK GGEQADEGKS EPEQPASAEP METENPAEGS T
