GH310_ARATH
ID GH310_ARATH Reviewed; 591 AA.
AC Q9ZNS2; E0Y432;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.10 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000305};
DE AltName: Full=Auxin-responsive GH3-like protein 10 {ECO:0000305};
DE AltName: Full=Protein DWARF IN LIGHT 2 {ECO:0000303|PubMed:14581632};
GN Name=GH3.10 {ECO:0000303|PubMed:14581632};
GN Synonyms=DFL2 {ECO:0000303|PubMed:14581632};
GN OrderedLocusNames=At4g03400 {ECO:0000312|Araport:AT4G03400};
GN ORFNames=F4C21.36 {ECO:0000312|EMBL:AAD14468.1},
GN F9H3.1 {ECO:0000312|EMBL:AAD11582.1};
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 [GENOMIC DNA].
RX PubMed=21037570; DOI=10.1038/ng.704;
RA Alcazar R., Garcia A.V., Kronholm I., de Meaux J., Koornneef M.,
RA Parker J.E., Reymond M.;
RT "Natural variation at strubbelig receptor kinase 3 drives immune-triggered
RT incompatibilities between Arabidopsis thaliana accessions.";
RL Nat. Genet. 42:1135-1139(2010).
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;
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 FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14581632; DOI=10.1093/pcp/pcg130;
RA Takase T., Nakazawa M., Ishikawa A., Manabe K., Matsui M.;
RT "DFL2, a new member of the Arabidopsis GH3 gene family, is involved in red
RT light-specific hypocotyl elongation.";
RL Plant Cell Physiol. 44:1071-1080(2003).
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 (By similarity). Involved in red light-
CC specific hypocotyl elongation. May act downstream of a red light signal
CC transduction and determine the degree of hypocotyl elongation
CC (PubMed:14581632). {ECO:0000250|UniProtKB:Q9LSQ4,
CC ECO:0000269|PubMed:14581632}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons and hypocotyls.
CC {ECO:0000269|PubMed:14581632}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
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DR EMBL; GU571158; ADM21185.1; -; Genomic_DNA.
DR EMBL; AC005275; AAD14468.1; -; Genomic_DNA.
DR EMBL; AF071527; AAD11582.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77825.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82314.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66984.1; -; Genomic_DNA.
DR EMBL; AY059941; AAL24423.1; -; mRNA.
DR EMBL; BT000061; AAN15380.1; -; mRNA.
DR PIR; B85043; B85043.
DR RefSeq; NP_001319858.1; NM_001340446.1.
DR RefSeq; NP_192249.1; NM_116578.3.
DR AlphaFoldDB; Q9ZNS2; -.
DR SMR; Q9ZNS2; -.
DR IntAct; Q9ZNS2; 2.
DR STRING; 3702.AT4G03400.1; -.
DR PaxDb; Q9ZNS2; -.
DR PRIDE; Q9ZNS2; -.
DR ProteomicsDB; 224789; -.
DR EnsemblPlants; AT4G03400.1; AT4G03400.1; AT4G03400.
DR EnsemblPlants; AT4G03400.2; AT4G03400.2; AT4G03400.
DR GeneID; 827938; -.
DR Gramene; AT4G03400.1; AT4G03400.1; AT4G03400.
DR Gramene; AT4G03400.2; AT4G03400.2; AT4G03400.
DR KEGG; ath:AT4G03400; -.
DR Araport; AT4G03400; -.
DR TAIR; locus:2125571; AT4G03400.
DR eggNOG; ENOG502QT0R; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9ZNS2; -.
DR OMA; IIGWFED; -.
DR OrthoDB; 374623at2759; -.
DR PhylomeDB; Q9ZNS2; -.
DR PRO; PR:Q9ZNS2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZNS2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0009416; P:response to light stimulus; IEP:TAIR.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 2: Evidence at transcript level;
KW Ligase; Reference proteome.
FT CHAIN 1..591
FT /note="Indole-3-acetic acid-amido synthetase GH3.10"
FT /id="PRO_0000439703"
FT CONFLICT 56
FT /note="D -> H (in Ref. 1; ADM21185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 66859 MW; 5A05BD36BF94E46A CRC64;
METVEAGHDD VIGWFEHVSE NACKVQSETL RRILELNSGV EYLRKWLGTV DVEKMDDYTL
ETLFTSLVPI VSHADLDPYI QRIADGETSP LLTQEPITVL SLSSGTTEGR QKYVPFTRHS
AQTTLQIFRL SAAYRSRFYP IREGGRILEF IYAGKEFKTL GGLTVGTATT HYYASEEFKT
KQETTKSFTC SPQEVISGGD FGQCTYCHLL LGLHYSSQVE FVASAFSYTI VQAFSFFEEI
WREICADIKE GNLSSRITLP KMRKAVLALI RPNPSLASHI EEICLELETN LGWFGLISKL
WPNAKFISSI MTGSMLPYLN KLRHYAGGLP LVSADYGSTE SWIGVNVDPH LPPEDVSFAV
IPTFSYFEFI PLYRRQNQSD ICIDGDFVED KPVPLSQVKL GQEYELVLTT FTGLYRYRLG
DVVEVTSFHK GTPKLSFIYR RKLILTINID KNTEKDLQRV VDKASQLLSR STRAEVVDFT
SHADVIARPG HYVIYWEIRG EADDKALEEC CREMDTAFVD YGYVVSRRMN SIGPLELRVV
ERGTFGKVAE RCVGKCGGLN QFKTPRCTTN SVMLDILNDS TIKRFRSSAY D
