HRD11_ARATH
ID HRD11_ARATH Reviewed; 98 AA.
AC Q9SLJ2; Q8H7A6; Q8LG75;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Dehydrin HIRD11 {ECO:0000305};
DE AltName: Full=Histidine-rich dehydrin of 11 kDa {ECO:0000303|Ref.8};
DE Short=AtHIRD11 {ECO:0000303|Ref.8};
DE AltName: Full=Protein SRC1 homolog {ECO:0000305};
GN Name=HIRD11 {ECO:0000303|Ref.8}; Synonyms=SRC1 {ECO:0000305};
GN OrderedLocusNames=At1g54410 {ECO:0000312|Araport:AT1G54410};
GN ORFNames=F20D21.23 {ECO:0000312|EMBL:AAD25619.1};
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].
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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].
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION BY COLD STRESS.
RX PubMed=15165189; DOI=10.1111/j.1365-313x.2004.02100.x;
RA Maruyama K., Sakuma Y., Kasuga M., Ito Y., Seki M., Goda H., Shimada Y.,
RA Yoshida S., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Identification of cold-inducible downstream genes of the Arabidopsis
RT DREB1A/CBF3 transcriptional factor using two microarray systems.";
RL Plant J. 38:982-993(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX DOI=10.1007/s11738-011-0749-1;
RA Hara M., Shinoda Y., Kubo M., Kashima D., Takahashi I., Kato T.,
RA Horiike T., Kuboi T.;
RT "Biochemical characterization of the Arabidopsis KS-type dehydrin protein,
RT whose gene expression is constitutively abundant rather than stress
RT dependent.";
RL Acta Physiol. Plant. 33:2103-2116(2011).
RN [9]
RP FUNCTION.
RX PubMed=23382551; DOI=10.1093/jxb/ert016;
RA Hara M., Kondo M., Kato T.;
RT "A KS-type dehydrin and its related domains reduce Cu-promoted radical
RT generation and the histidine residues contribute to the radical-reducing
RT activities.";
RL J. Exp. Bot. 64:1615-1624(2013).
RN [10]
RP INTERACTION WITH PXL1, AND PHOSPHORYLATION.
RX PubMed=25602612; DOI=10.1016/j.jplph.2015.01.001;
RA Jung C.G., Hwang S.G., Park Y.C., Park H.M., Kim D.S., Park D.H.,
RA Jang C.S.;
RT "Molecular characterization of the cold- and heat-induced Arabidopsis PXL1
RT gene and its potential role in transduction pathways under temperature
RT fluctuations.";
RL J. Plant Physiol. 176:138-146(2015).
CC -!- FUNCTION: Intrinsically disordered and metal-binding protein. Binds to
CC the divalent cations cobalt, nickel, copper and zinc, but not to
CC magnesium, calcium, manganese or cadmium (Ref.8). Binding to metal ions
CC decreases disordered state, decreases susceptibility to trypsin and
CC promotes self-association. Can reduce the formation of reactive oxygen
CC species (ROS) in a copper-ascorbate in vitro system (PubMed:23382551).
CC {ECO:0000269|PubMed:23382551, ECO:0000269|Ref.8}.
CC -!- SUBUNIT: Interacts with PXL1. {ECO:0000269|PubMed:25602612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.8}. Nucleus
CC {ECO:0000269|Ref.8}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the cambial zone of the stem
CC vasculature (at protein level). Expressed in roots, rosettes leaves,
CC stems, cauline leaves, flowers and siliques. {ECO:0000269|Ref.8}.
CC -!- INDUCTION: By cold stress (PubMed:15165189).
CC {ECO:0000269|PubMed:15165189}.
CC -!- PTM: Phosphorylated in vivo (Ref.8). Phosphorylated in vitro by PXL1
CC (PubMed:25602612). {ECO:0000269|PubMed:25602612, ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the KS-type dehydrin family. {ECO:0000305}.
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DR EMBL; AF083768; AAN60326.1; -; mRNA.
DR EMBL; AC005287; AAD25619.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33100.1; -; Genomic_DNA.
DR EMBL; AF325000; AAG40352.1; -; mRNA.
DR EMBL; AY070750; AAL50089.1; -; mRNA.
DR EMBL; AY097376; AAM19892.1; -; mRNA.
DR EMBL; AK230245; BAF02048.1; -; mRNA.
DR EMBL; AY084428; AAM67282.1; -; mRNA.
DR PIR; H96585; H96585.
DR RefSeq; NP_175843.1; NM_104319.6.
DR AlphaFoldDB; Q9SLJ2; -.
DR STRING; 3702.AT1G54410.1; -.
DR iPTMnet; Q9SLJ2; -.
DR PaxDb; Q9SLJ2; -.
DR PRIDE; Q9SLJ2; -.
DR ProteomicsDB; 230140; -.
DR EnsemblPlants; AT1G54410.1; AT1G54410.1; AT1G54410.
DR GeneID; 841883; -.
DR Gramene; AT1G54410.1; AT1G54410.1; AT1G54410.
DR KEGG; ath:AT1G54410; -.
DR Araport; AT1G54410; -.
DR TAIR; locus:2020178; AT1G54410.
DR eggNOG; ENOG502S99J; Eukaryota.
DR HOGENOM; CLU_144452_1_0_1; -.
DR InParanoid; Q9SLJ2; -.
DR OMA; HADEHKS; -.
DR PRO; PR:Q9SLJ2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SLJ2; baseline and differential.
DR Genevisible; Q9SLJ2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016151; F:nickel cation binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IDA:TAIR.
DR DisProt; DP01300; -.
DR InterPro; IPR039285; HIRD11-like.
DR PANTHER; PTHR34941; PTHR34941; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..98
FT /note="Dehydrin HIRD11"
FT /id="PRO_0000433971"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 94
FT /note="D -> V (in Ref. 1; AAN60326)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="D -> I (in Ref. 6; AAM67282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 98 AA; 10796 MW; 2D385EB945E95589 CRC64;
MAGLINKIGD ALHIGGGNKE GEHKKEEEHK KHVDEHKSGE HKEGIVDKIK DKIHGGEGKS
HDGEGKSHDG EKKKKKDKKE KKHHDDGHHS SSSDSDSD
