HTD1_ARATH
ID HTD1_ARATH Reviewed; 469 AA.
AC Q9ZUN8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein HEAT STRESS TOLERANT DWD 1 {ECO:0000303|PubMed:25358503};
GN Name=HTD1 {ECO:0000303|PubMed:25358503};
GN OrderedLocusNames=At2g19540 {ECO:0000312|Araport:AT2G19540};
GN ORFNames=F3P11.14 {ECO:0000312|EMBL:AAD10153.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP GENE FAMILY.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [5]
RP GENE FAMILY.
RX PubMed=18552200; DOI=10.1105/tpc.108.058891;
RA Zhang Y., Feng S., Chen F., Chen H., Wang J., McCall C., Xiong Y.,
RA Deng X.W.;
RT "Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 forms a nuclear E3 ubiquitin
RT ligase with DDB1 and CUL4 that is involved in multiple plant developmental
RT processes.";
RL Plant Cell 20:1437-1455(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY HEAT STRESS, AND INTERACTION
RP WITH HSP90-1; DDB1A AND DDB1B.
RC STRAIN=cv. Columbia;
RX PubMed=25358503; DOI=10.14348/molcells.2014.0224;
RA Kim S.-H., Lee J.-H., Seo K.-I., Ryu B., Sung Y., Chung T., Deng X.W.,
RA Lee J.-H.;
RT "Characterization of a novel DWD protein that participates in heat stress
RT response in Arabidopsis.";
RL Mol. Cells 37:833-840(2014).
CC -!- FUNCTION: Probable substrate receptor of CRL4 E3 ligase complexes
CC acting as negative regulators of thermotolerance by disturbing the
CC action of HSP90-1 and by preventing the expression of heat-inducible
CC genes (e.g. HSP14.7, HSP21, At2g03020 and WRKY28).
CC {ECO:0000269|PubMed:25358503}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:25358503}.
CC -!- SUBUNIT: Probable component of CULLIN4 (CUL4) RING ligase (CRL4)
CC complexes (PubMed:25358503). Interacts with DDB1A and DDB1B
CC (PubMed:25358503). Associates with HSP90-1 (PubMed:25358503).
CC {ECO:0000269|PubMed:25358503}.
CC -!- INDUCTION: Accumulates in response to heat stress.
CC {ECO:0000269|PubMed:25358503}.
CC -!- DISRUPTION PHENOTYPE: Increased heat stress tolerance associated with
CC the accumulation of HSP14.7, HSP21, At2g03020 and WRKY28.
CC {ECO:0000269|PubMed:25358503}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; AC005917; AAD10153.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06893.1; -; Genomic_DNA.
DR EMBL; AF370506; AAK43883.1; -; mRNA.
DR EMBL; AY128814; AAM91214.1; -; mRNA.
DR PIR; A84578; A84578.
DR RefSeq; NP_179544.1; NM_127512.4.
DR AlphaFoldDB; Q9ZUN8; -.
DR SMR; Q9ZUN8; -.
DR STRING; 3702.AT2G19540.1; -.
DR PaxDb; Q9ZUN8; -.
DR PRIDE; Q9ZUN8; -.
DR ProteomicsDB; 191697; -.
DR EnsemblPlants; AT2G19540.1; AT2G19540.1; AT2G19540.
DR GeneID; 816473; -.
DR Gramene; AT2G19540.1; AT2G19540.1; AT2G19540.
DR KEGG; ath:AT2G19540; -.
DR Araport; AT2G19540; -.
DR TAIR; locus:2050388; AT2G19540.
DR eggNOG; KOG0302; Eukaryota.
DR HOGENOM; CLU_025272_2_1_1; -.
DR InParanoid; Q9ZUN8; -.
DR OMA; DWSPLQP; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q9ZUN8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUN8; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:1900035; P:negative regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Stress response; Ubl conjugation pathway;
KW WD repeat.
FT CHAIN 1..469
FT /note="Protein HEAT STRESS TOLERANT DWD 1"
FT /id="PRO_0000452651"
FT REPEAT 157..197
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 221..261
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 267..307
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 311..351
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 358..398
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 425..464
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51404 MW; E46747B4CC097710 CRC64;
MGRNVKTKAK RKNKKKAEAS SSEIPSIPTR VWQPGVDTLE DGEELQCDPS AYNSLHGFHV
GWPCLSFDIL GDKLGLNRTE FPHTLYMVAG TQAEKAAHNS IGLFKITNVS GKRRDVVPKT
FGNGEDEDED DEDDSDSDDD DGDEASKTPN IQVRRVAHHG CVNRIRAMPQ NSHICVSWAD
SGHVQVWDMS SHLNALAESE TEGKDGTSPV LNQAPLVNFS GHKDEGYAID WSPATAGRLL
SGDCKSMIHL WEPASGSWAV DPIPFAGHTA SVEDLQWSPA EENVFASCSV DGSVAVWDIR
LGKSPALSFK AHNADVNVIS WNRLASCMLA SGSDDGTFSI RDLRLIKGGD AVVAHFEYHK
HPITSIEWSA HEASTLAVTS GDNQLTIWDL SLEKDEEEEA EFNAQTKELV NTPQDLPPQL
LFVHQGQKDL KELHWHNQIP GMIISTAGDG FNILMPYNIQ NTLPSELPA
