HLS1_ARATH
ID HLS1_ARATH Reviewed; 403 AA.
AC Q42381;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Probable N-acetyltransferase HLS1;
DE EC=2.3.1.-;
DE AltName: Full=Protein CONSTITUTIVE PHOTOMORPHOGENIC 3;
DE AltName: Full=Protein HOOKLESS 1;
DE AltName: Full=Protein UNUSUAL SUGAR RESPONSE 2;
GN Name=HLS1; Synonyms=COP3, UNS2; OrderedLocusNames=At4g37580;
GN ORFNames=F19F18.70;
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 / MRNA], INDUCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LEU-327 AND GLU-346.
RC STRAIN=cv. Columbia;
RX PubMed=8612271; DOI=10.1016/s0092-8674(00)81095-8;
RA Lehman A., Black R., Ecker J.R.;
RT "HOOKLESS1, an ethylene response gene, is required for differential cell
RT elongation in the Arabidopsis hypocotyl.";
RL Cell 85:183-194(1996).
RN [2]
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 [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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10409511; DOI=10.1242/dev.126.16.3661;
RA Raz V., Ecker J.R.;
RT "Regulation of differential growth in the apical hook of Arabidopsis.";
RL Development 126:3661-3668(1999).
RN [7]
RP FUNCTION.
RX PubMed=17071622; DOI=10.1093/pcp/pcl027;
RA Ohto M.A., Hayashi S., Sawa S., Hashimoto-Ohta A., Nakamura K.;
RT "Involvement of HLS1 in sugar and auxin signaling in Arabidopsis leaves.";
RL Plant Cell Physiol. 47:1603-1611(2006).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=18838801; DOI=10.1271/bbb.80348;
RA Hamaguchi A., Yamashino T., Koizumi N., Kiba T., Kojima M., Sakakibara H.,
RA Mizuno T.;
RT "A small subfamily of Arabidopsis RADIALIS-LIKE SANT/MYB genes: a link to
RT HOOKLESS1-mediated signal transduction during early morphogenesis.";
RL Biosci. Biotechnol. Biochem. 72:2687-2696(2008).
RN [9]
RP FUNCTION.
RX PubMed=22349459; DOI=10.1038/cr.2012.29;
RA An F., Zhang X., Zhu Z., Ji Y., He W., Jiang Z., Li M., Guo H.;
RT "Coordinated regulation of apical hook development by gibberellins and
RT ethylene in etiolated Arabidopsis seedlings.";
RL Cell Res. 22:915-927(2012).
CC -!- FUNCTION: Ethylene-responsive N-acetyltransferase required for
CC differential cell elongation in the hypocotyl. Regulates apical hook
CC formation of dark-grown seedlings. May control differential cell growth
CC by regulating auxin activity. May be involved in negative feedback
CC regulation of auxin homeostasis through the control of GH3-like genes.
CC Modulates de novo shoot organogenesis. {ECO:0000269|PubMed:17071622,
CC ECO:0000269|PubMed:22349459}.
CC -!- INTERACTION:
CC Q42381; Q9SAI2: CAF1-6; NbExp=4; IntAct=EBI-15207218, EBI-4465274;
CC -!- INDUCTION: By ethylene. {ECO:0000269|PubMed:8612271}.
CC -!- DISRUPTION PHENOTYPE: Unable to develop apical hook in the dark.
CC Reduced length of dark-grown hypocotyls and reduced leaf initiation
CC rate in light-grown seedlings. {ECO:0000269|PubMed:10409511,
CC ECO:0000269|PubMed:18838801, ECO:0000269|PubMed:8612271}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U50399; AAB03773.1; -; mRNA.
DR EMBL; U50400; AAB03774.1; -; Genomic_DNA.
DR EMBL; AL035605; CAB38297.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80423.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86813.1; -; Genomic_DNA.
DR EMBL; AK175660; BAD43423.1; -; mRNA.
DR EMBL; AK176117; BAD43880.1; -; mRNA.
DR EMBL; BT026435; ABH04542.1; -; mRNA.
DR PIR; S71236; S71236.
DR RefSeq; NP_195474.1; NM_119922.5.
DR AlphaFoldDB; Q42381; -.
DR BioGRID; 15194; 3.
DR IntAct; Q42381; 3.
DR STRING; 3702.AT4G37580.1; -.
DR PaxDb; Q42381; -.
DR PRIDE; Q42381; -.
DR ProteomicsDB; 230351; -.
DR EnsemblPlants; AT4G37580.1; AT4G37580.1; AT4G37580.
DR GeneID; 829913; -.
DR Gramene; AT4G37580.1; AT4G37580.1; AT4G37580.
DR KEGG; ath:AT4G37580; -.
DR Araport; AT4G37580; -.
DR TAIR; locus:2005512; AT4G37580.
DR eggNOG; ENOG502QQCN; Eukaryota.
DR HOGENOM; CLU_057213_0_0_1; -.
DR InParanoid; Q42381; -.
DR OMA; HKCGYSK; -.
DR OrthoDB; 567615at2759; -.
DR PhylomeDB; Q42381; -.
DR PRO; PR:Q42381; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42381; baseline and differential.
DR Genevisible; Q42381; AT.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Growth regulation; Reference proteome; Transferase.
FT CHAIN 1..403
FT /note="Probable N-acetyltransferase HLS1"
FT /id="PRO_0000423403"
FT DOMAIN 2..177
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT MUTAGEN 327
FT /note="L->W: In hls1-6; strong allele."
FT /evidence="ECO:0000269|PubMed:8612271"
FT MUTAGEN 346
FT /note="E->K: In hls1-1 and hls4-1; strong allele."
FT /evidence="ECO:0000269|PubMed:8612271"
SQ SEQUENCE 403 AA; 44934 MW; E2A9DD0C2FA2DFE8 CRC64;
MTVVREYDPT RDLVGVEDVE RRCEVGPSGK LSLFTDLLGD PICRIRHSPS YLMLVAEMGT
EKKEIVGMIR GCIKTVTCGQ KLDLNHKSQN DVVKPLYTKL AYVLGLRVSP FHRRQGIGFK
LVKMMEEWFR QNGAEYSYIA TENDNQASVN LFTGKCGYSE FRTPSILVNP VYAHRVNVSR
RVTVIKLEPV DAETLYRIRF STTEFFPRDI DSVLNNKLSL GTFVAVPRGS CYGSGSGSWP
GSAKFLEYPP ESWAVLSVWN CKDSFLLEVR GASRLRRVVA KTTRVVDKTL PFLKLPSIPS
VFEPFGLHFM YGIGGEGPRA VKMVKSLCAH AHNLAKAGGC GVVAAEVAGE DPLRRGIPHW
KVLSCDEDLW CIKRLGDDYS DGVVGDWTKS PPGVSIFVDP REF
