GH32_ARATH
ID GH32_ARATH Reviewed; 549 AA.
AC Q9SZT9; F4JS15; Q93Z39; Q9SLU3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.2;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 2;
DE Short=AtGH3-2;
DE AltName: Full=Protein YADOKARI 1;
GN Name=GH3.2; Synonyms=BRU6, CF4, YDK1; OrderedLocusNames=At4g37390;
GN ORFNames=F6G17.40;
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=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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 281-549 (ISOFORM 1).
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14756757; DOI=10.1046/j.1365-313x.2003.01973.x;
RA Takase T., Nakazawa M., Ishikawa A., Kawashima M., Ichikawa T.,
RA Takahashi N., Shimada H., Manabe K., Matsui M.;
RT "ydk1-D, an auxin-responsive GH3 mutant that is involved in hypocotyl and
RT root elongation.";
RL Plant J. 37:471-483(2004).
RN [6]
RP FUNCTION, CHARACTERIZATION, AND INDUCTION.
RX PubMed=15659623; DOI=10.1105/tpc.104.026690;
RA Staswick P.E., Serban B., Rowe M., Tiryaki I., Maldonado M.T.,
RA Maldonado M.C., Suza W.;
RT "Characterization of an Arabidopsis enzyme family that conjugates amino
RT acids to indole-3-acetic acid.";
RL Plant Cell 17:616-627(2005).
RN [7]
RP NOMENCLATURE.
RX PubMed=12036261; DOI=10.1023/a:1015207114117;
RA Hagen G., Guilfoyle T.J.;
RT "Auxin-responsive gene expression: genes, promoters and regulatory
RT factors.";
RL Plant Mol. Biol. 49:373-385(2002).
CC -!- FUNCTION: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino
CC acid conjugates, providing a mechanism for the plant to cope with the
CC presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp,
CC Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or no product
CC formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic
CC and butyric acid analogs of IAA, PAA and the synthetic auxin
CC naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin
CC herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be
CC used as substrates. {ECO:0000269|PubMed:14756757,
CC ECO:0000269|PubMed:15659623}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SZT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZT9-2; Sequence=VSP_042266;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, pollen, cotyledons, stipules,
CC true leaves, hypocotyls, and all parts of the roots except for the
CC primary root tips. {ECO:0000269|PubMed:14756757}.
CC -!- INDUCTION: By auxin. Down-regulated by blue and far red lights.
CC {ECO:0000269|PubMed:14756757, ECO:0000269|PubMed:15659623}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA87950.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB38206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035601; CAB38206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161591; CAB80404.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86787.1; -; Genomic_DNA.
DR EMBL; AY058161; AAL25575.1; -; mRNA.
DR EMBL; AB028224; BAA87950.1; ALT_FRAME; mRNA.
DR PIR; T04733; T04733.
DR PIR; T52435; T52435.
DR RefSeq; NP_195455.1; NM_119902.4. [Q9SZT9-2]
DR AlphaFoldDB; Q9SZT9; -.
DR SMR; Q9SZT9; -.
DR STRING; 3702.AT4G37390.1; -.
DR PaxDb; Q9SZT9; -.
DR PeptideAtlas; Q9SZT9; -.
DR PRIDE; Q9SZT9; -.
DR ProteomicsDB; 220748; -. [Q9SZT9-1]
DR EnsemblPlants; AT4G37390.1; AT4G37390.1; AT4G37390. [Q9SZT9-2]
DR GeneID; 829893; -.
DR Gramene; AT4G37390.1; AT4G37390.1; AT4G37390. [Q9SZT9-2]
DR KEGG; ath:AT4G37390; -.
DR Araport; AT4G37390; -.
DR TAIR; locus:2126362; AT4G37390.
DR eggNOG; ENOG502QPMW; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9SZT9; -.
DR OMA; EGFFAIQ; -.
DR OrthoDB; 374623at2759; -.
DR BioCyc; ARA:AT4G37390-MON; -.
DR PRO; PR:Q9SZT9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZT9; baseline and differential.
DR Genevisible; Q9SZT9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IBA:GO_Central.
DR GO; GO:0010279; F:indole-3-acetic acid amido synthetase activity; IDA:TAIR.
DR GO; GO:0010252; P:auxin homeostasis; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Ligase; Reference proteome.
FT CHAIN 1..549
FT /note="Indole-3-acetic acid-amido synthetase GH3.2"
FT /id="PRO_0000203571"
FT VAR_SEQ 540..549
FT /note="GDTCGTERYV -> EIRVVRNGTFEELMDYAISRGASINQYKVPRCVSFTPI
FT MELLDSRVVSAHFSPSLPHWSPERRR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042266"
FT CONFLICT 422
FT /note="L -> F (in Ref. 4; BAA87950)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="V -> G (in Ref. 3; AAL25575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 61827 MW; D2C807C4FD5145D4 CRC64;
MAVDSPLQSR MVSATTSEKD VKALKFIEEM TRNPDSVQEK VLGEILTRNS NTEYLKRFDL
DGVVDRKTFK SKVPVVTYED LKPEIQRISN GDCSPILSSH PITEFLTSSG TSAGERKLMP
TIEEDLDRRQ LLYSLLMPVM NLYVPGLDKG KGLYFLFVKS ESKTSGGLPA RPVLTSYYKS
DHFKRRPYDP YNVYTSPNEA ILCSDSSQSM YAQMLCGLLM RHEVLRLGAV FASGLLRAIS
FLQNNWKELA RDISTGTLSS RIFDPAIKNR MSKILTKPDQ ELAEFLVGVC SQENWEGIIT
KIWPNTKYLD VIVTGAMAQY IPTLEYYSGG LPMACTMYAS SESYFGINLK PMCKPSEVSY
TIMPNMAYFE FLPHNHDGDG AAEASLDETS LVELANVEVG KEYELVITTY AGLYRYRVGD
ILRVTGFHNS APQFKFIRRK NVLLSVESDK TDEAELQKAV ENASRLFAEQ GTRVIEYTSY
AETKTIPGHY VIYWELLGRD QSNALMSEEV MAKCCLEMEE SLNSVYRQSR VADKSIGPLG
DTCGTERYV
