HSP17_ARATH
ID HSP17_ARATH Reviewed; 156 AA.
AC P19036; Q540N8; Q94EJ5; Q9LX72;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=17.4 kDa class I heat shock protein;
DE AltName: Full=17.4 kDa heat shock protein 1;
DE Short=AtHsp17.4A;
GN Name=HSP17.4A; OrderedLocusNames=At3g46230; ORFNames=F12M12_200;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2482931; DOI=10.1007/bf00259608;
RA Takahashi T., Komeda Y.;
RT "Characterization of two genes encoding small heat-shock proteins in
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 219:365-372(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 INTERACTION WITH AKR2A, AND INDUCTION BY HEAT SHOCK.
RC STRAIN=cv. Columbia;
RX PubMed=21730198; DOI=10.1104/pp.111.178681;
RA Kim D.H., Xu Z.-Y., Na Y.J., Yoo Y.-J., Lee J., Sohn E.-J., Hwang I.;
RT "Small heat shock protein Hsp17.8 functions as an AKR2A cofactor in the
RT targeting of chloroplast outer membrane proteins in Arabidopsis.";
RL Plant Physiol. 157:132-146(2011).
CC -!- SUBUNIT: May form oligomeric structures. Binds to AKR2A
CC (PubMed:21730198). {ECO:0000269|PubMed:21730198, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Accumulates after heat shock. {ECO:0000269|PubMed:21730198}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X17293; CAA35182.1; -; Genomic_DNA.
DR EMBL; AL355775; CAB90950.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78138.1; -; Genomic_DNA.
DR EMBL; AF410266; AAK95252.1; -; mRNA.
DR EMBL; AY143803; AAN28742.1; -; mRNA.
DR PIR; JQ0351; JQ0351.
DR PIR; T49264; T49264.
DR RefSeq; NP_190209.1; NM_114492.4.
DR AlphaFoldDB; P19036; -.
DR SMR; P19036; -.
DR BioGRID; 9088; 2.
DR IntAct; P19036; 1.
DR STRING; 3702.AT3G46230.1; -.
DR PaxDb; P19036; -.
DR PRIDE; P19036; -.
DR ProteomicsDB; 232090; -.
DR EnsemblPlants; AT3G46230.1; AT3G46230.1; AT3G46230.
DR GeneID; 823768; -.
DR Gramene; AT3G46230.1; AT3G46230.1; AT3G46230.
DR KEGG; ath:AT3G46230; -.
DR Araport; AT3G46230; -.
DR TAIR; locus:2075256; AT3G46230.
DR eggNOG; KOG0710; Eukaryota.
DR HOGENOM; CLU_046737_5_0_1; -.
DR InParanoid; P19036; -.
DR OMA; VEVEDHR; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P19036; -.
DR PRO; PR:P19036; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P19036; baseline and differential.
DR Genevisible; P19036; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043621; F:protein self-association; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0051259; P:protein complex oligomerization; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Stress response.
FT CHAIN 1..156
FT /note="17.4 kDa class I heat shock protein"
FT /id="PRO_0000125970"
FT DOMAIN 42..156
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT CONFLICT 6
FT /note="S -> T (in Ref. 4; AAK95252/AAN28742)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="V -> I (in Ref. 1; CAA35182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17440 MW; F6FEA76EA8329501 CRC64;
MSLVPSFFGG RRTNVFDPFS LDVWDPFEGF LTPGLTNAPA KDVAAFTNAK VDWRETPEAH
VFKADVPGLK KEEVKVEVED GNILQISGER SSENEEKSDT WHRVERSSGK FMRRFRLPEN
AKVEEVKASM ENGVLSVTVP KVQESKPEVK SVDISG
