HS25P_ARATH
ID HS25P_ARATH Reviewed; 227 AA.
AC P31170; A0MFA3; Q1PE43; Q6ZWL5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Heat shock protein 21, chloroplastic {ECO:0000303|PubMed:2038305};
DE AltName: Full=25.3 kDa heat shock protein, chloroplastic;
DE Short=AtHsp25.3;
DE Flags: Precursor;
GN Name=HSP21 {ECO:0000303|PubMed:2038305}; Synonyms=HSP25.3;
GN OrderedLocusNames=At4g27670 {ECO:0000312|Araport:AT4G27670};
GN ORFNames=T29A15.160 {ECO:0000312|EMBL:CAB38279.1};
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=2038305; DOI=10.1007/bf00260655;
RA Chen Q., Vierling E.;
RT "Analysis of conserved domains identifies a unique structural feature of a
RT chloroplast heat shock protein.";
RL Mol. Gen. Genet. 226:425-431(1991).
RN [2]
RP ERRATUM OF PUBMED:2038305.
RX PubMed=1886617; DOI=10.1007/bf00282486;
RA Chen Q., Vierling E.;
RL Mol. Gen. Genet. 228:328-328(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8391109; DOI=10.1007/bf00276930;
RA Osteryoung K.W., Sundberg H., Vierling E.;
RT "Poly(A) tail length of a heat shock protein RNA is increased by severe
RT heat stress, but intron splicing is unaffected.";
RL Mol. Gen. Genet. 239:323-333(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INTERACTION WITH PTAC5, AND INDUCTION BY HEAT SHOCK.
RC STRAIN=cv. Columbia;
RX PubMed=23922206; DOI=10.1105/tpc.113.111229;
RA Zhong L., Zhou W., Wang H., Ding S., Lu Q., Wen X., Peng L., Zhang L.,
RA Lu C.;
RT "Chloroplast small heat shock protein HSP21 interacts with plastid nucleoid
RT protein pTAC5 and is essential for chloroplast development in Arabidopsis
RT under heat stress.";
RL Plant Cell 25:2925-2943(2013).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (10.00 ANGSTROMS) OF 85-227, SUBUNIT, AND
RP MUTAGENESIS OF VAL-181.
RX PubMed=28325834; DOI=10.1074/jbc.m116.766816;
RA Rutsdottir G., Haermark J., Weide Y., Hebert H., Rasmussen M.I.,
RA Wernersson S., Respondek M., Akke M., Hojrup P., Koeck P.J.B.,
RA Soederberg C.A.G., Emanuelsson C.;
RT "Structural model of dodecameric heat-shock protein Hsp21: Flexible N-
RT terminal arms interact with client proteins while C-terminal tails maintain
RT the dodecamer and chaperone activity.";
RL J. Biol. Chem. 292:8103-8121(2017).
CC -!- FUNCTION: Chaperone protein required for seedling and chloroplast
CC development under heat stress, probably by maintaining plastid-encoded
CC RNA polymerase (PEP)-dependent transcription.
CC {ECO:0000269|PubMed:23922206}.
CC -!- SUBUNIT: Forms oligomeric structures: dodecameric arrangement of two
CC trimer- of-dimer disks stabilized by the C-terminal tails, possibly
CC through tail-to-tail interactions between the disks (PubMed:28325834).
CC Interacts with PTAC5; the formed complex associates with the plastid-
CC encoded RNA polymerase (PEP) complex not only during transcription
CC initiation, but also during elongation and termination, and with a
CC stronger efficiency in illuminated chloroplasts. Binds to promoter
CC regions of PEP-dependent genes (PubMed:23922206).
CC {ECO:0000269|PubMed:23922206, ECO:0000269|PubMed:28325834}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000269|PubMed:23922206}.
CC -!- TISSUE SPECIFICITY: Confined to pollen grains of budding flowers.
CC {ECO:0000269|PubMed:23922206}.
CC -!- INDUCTION: Highly induced in roots, stems, leaves, flowers and siliques
CC after a heat shock at 30 degrees Celsius. Highly and quickly induced by
CC heat stress during early seedling development.
CC {ECO:0000269|PubMed:23922206}.
CC -!- DISRUPTION PHENOTYPE: Ivory phenotype seedling under heat stress (30
CC degrees Celsius). Decrease in transcript levels of class I genes, but
CC enhanced expression of class III genes (e.g. accD, rpoB and clpP) after
CC heat shock. {ECO:0000269|PubMed:23922206}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28654.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; X54102; CAA38036.1; -; mRNA.
DR EMBL; M94455; AAA32818.1; -; Genomic_DNA.
DR EMBL; AL035602; CAB38279.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81417.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85379.1; -; Genomic_DNA.
DR EMBL; AK119078; BAC43654.2; -; mRNA.
DR EMBL; DQ446875; ABE66096.1; -; mRNA.
DR EMBL; DQ653229; ABK28654.1; ALT_SEQ; mRNA.
DR PIR; S35240; S35240.
DR RefSeq; NP_194497.1; NM_118906.3.
DR PDB; 5NMS; EM; 10.00 A; A/C/D/G/I/J=85-227, B/E/F/H/K/L=126-227.
DR PDB; 7BZW; EM; 4.60 A; 1/10/11/12/2/3/4/5/6/7/8/9=44-227.
DR PDB; 7BZY; EM; 3.70 A; 12=44-227.
DR PDBsum; 5NMS; -.
DR PDBsum; 7BZW; -.
DR PDBsum; 7BZY; -.
DR AlphaFoldDB; P31170; -.
DR SMR; P31170; -.
DR BioGRID; 14168; 3.
DR STRING; 3702.AT4G27670.1; -.
DR MetOSite; P31170; -.
DR PaxDb; P31170; -.
DR PRIDE; P31170; -.
DR ProteomicsDB; 230144; -.
DR EnsemblPlants; AT4G27670.1; AT4G27670.1; AT4G27670.
DR GeneID; 828881; -.
DR Gramene; AT4G27670.1; AT4G27670.1; AT4G27670.
DR KEGG; ath:AT4G27670; -.
DR Araport; AT4G27670; -.
DR TAIR; locus:2137762; AT4G27670.
DR eggNOG; KOG0710; Eukaryota.
DR HOGENOM; CLU_046737_3_0_1; -.
DR InParanoid; P31170; -.
DR OMA; RTMRQMM; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P31170; -.
DR PRO; PR:P31170; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P31170; baseline and differential.
DR Genevisible; P31170; AT.
DR GO; GO:0101031; C:chaperone complex; IMP:UniProtKB.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR044587; HSP21-like.
DR PANTHER; PTHR46733; PTHR46733; 1.
DR Pfam; PF00011; HSP20; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Chloroplast; Plastid; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..227
FT /note="Heat shock protein 21, chloroplastic"
FT /id="PRO_0000013528"
FT DOMAIN 120..227
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 14..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 181
FT /note="V->A: Impaired dodecameric oligomer structures
FT formation leading to reduced chaperone activity."
FT /evidence="ECO:0000269|PubMed:28325834"
FT CONFLICT 24
FT /note="S -> P (in Ref. 6; BAC43654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25344 MW; B25400AF6C01972E CRC64;
MASTLSFAAS ALCSPLAPSP SVSSKSATPF SVSFPRKIPS RIRAQDQREN SIDVVQQGQQ
KGNQGSSVEK RPQQRLTMDV SPFGLLDPLS PMRTMRQMLD TMDRMFEDTM PVSGRNRGGS
GVSEIRAPWD IKEEEHEIKM RFDMPGLSKE DVKISVEDNV LVIKGEQKKE DSDDSWSGRS
VSSYGTRLQL PDNCEKDKIK AELKNGVLFI TIPKTKVERK VIDVQIQ
