HS157_ARATH
ID HS157_ARATH Reviewed; 137 AA.
AC Q9FHQ3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=15.7 kDa heat shock protein, peroxisomal;
DE Short=AtHsp15.7;
GN Name=HSP15.7; OrderedLocusNames=At5g37670; ORFNames=K12B20.120;
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], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16531488; DOI=10.1104/pp.105.073841;
RA Ma C., Haslbeck M., Babujee L., Jahn O., Reumann S.;
RT "Identification and characterization of a stress-inducible and a
RT constitutive small heat-shock protein targeted to the matrix of plant
RT peroxisomes.";
RL Plant Physiol. 141:47-60(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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).
CC -!- FUNCTION: Possesses chaperone activity. {ECO:0000269|PubMed:16531488}.
CC -!- SUBUNIT: May form oligomeric structures.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16531488}.
CC -!- INDUCTION: By heat shock and methyl viologen (paraquat).
CC {ECO:0000269|PubMed:16531488}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; DQ403190; ABD67504.1; -; mRNA.
DR EMBL; AB018107; BAB08313.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94218.1; -; Genomic_DNA.
DR EMBL; AK118822; BAC43412.1; -; mRNA.
DR EMBL; BT005449; AAO63869.1; -; mRNA.
DR RefSeq; NP_198583.1; NM_123126.3.
DR AlphaFoldDB; Q9FHQ3; -.
DR SMR; Q9FHQ3; -.
DR BioGRID; 18997; 9.
DR IntAct; Q9FHQ3; 9.
DR STRING; 3702.AT5G37670.1; -.
DR PaxDb; Q9FHQ3; -.
DR PRIDE; Q9FHQ3; -.
DR ProteomicsDB; 228749; -.
DR EnsemblPlants; AT5G37670.1; AT5G37670.1; AT5G37670.
DR GeneID; 833746; -.
DR Gramene; AT5G37670.1; AT5G37670.1; AT5G37670.
DR KEGG; ath:AT5G37670; -.
DR Araport; AT5G37670; -.
DR TAIR; locus:2151719; AT5G37670.
DR eggNOG; KOG0710; Eukaryota.
DR HOGENOM; CLU_046737_5_2_1; -.
DR InParanoid; Q9FHQ3; -.
DR OMA; EIVWHVA; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q9FHQ3; -.
DR PRO; PR:Q9FHQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHQ3; baseline and differential.
DR Genevisible; Q9FHQ3; AT.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
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; IGI:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IEP:UniProtKB.
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 2: Evidence at transcript level;
KW Peroxisome; Reference proteome; Stress response.
FT CHAIN 1..137
FT /note="15.7 kDa heat shock protein, peroxisomal"
FT /id="PRO_0000387492"
FT DOMAIN 15..134
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT MOTIF 135..137
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 137 AA; 15698 MW; 90BDF0BE14F793EB CRC64;
MADRGIFLYP FRRFQEWSRS TALIDWMESN NSHIFKINVP GYNKEDIKVQ IEEGNVLSIR
GEGIKEEKKE NLVWHVAERE AFSGGGSEFL RRIELPENVK VDQVKAYVEN GVLTVVVPKD
TSSKSSKVRN VNITSKL
