GH317_ARATH
ID GH317_ARATH Reviewed; 609 AA.
AC Q9FZ87;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.17;
DE EC=6.3.2.-;
DE AltName: Full=Auxin-responsive GH3-like protein 17;
DE Short=AtGH3-17;
GN Name=GH3.17; OrderedLocusNames=At1g28130;
GN ORFNames=F13K9.22, F3H9.21, F3H9_19;
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=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 [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 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 [5]
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. Appears to favor Glu over
CC Asp while the other GH3 favor Asp over Glu. 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:15659623}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FZ87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FZ87-2; Sequence=VSP_015094;
CC -!- INDUCTION: Not induced by auxin. {ECO:0000269|PubMed:15659623}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {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; AC021044; AAF98442.1; -; Genomic_DNA.
DR EMBL; AC069471; AAG51481.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30921.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30922.1; -; Genomic_DNA.
DR EMBL; AY052283; AAK96476.1; -; mRNA.
DR EMBL; AY113067; AAM47375.1; -; mRNA.
DR PIR; B86407; B86407.
DR RefSeq; NP_174134.1; NM_102578.4. [Q9FZ87-1]
DR RefSeq; NP_849718.1; NM_179387.2. [Q9FZ87-2]
DR AlphaFoldDB; Q9FZ87; -.
DR SMR; Q9FZ87; -.
DR BioGRID; 24941; 1.
DR STRING; 3702.AT1G28130.1; -.
DR PaxDb; Q9FZ87; -.
DR PRIDE; Q9FZ87; -.
DR ProteomicsDB; 224790; -. [Q9FZ87-1]
DR EnsemblPlants; AT1G28130.1; AT1G28130.1; AT1G28130. [Q9FZ87-1]
DR EnsemblPlants; AT1G28130.2; AT1G28130.2; AT1G28130. [Q9FZ87-2]
DR GeneID; 839706; -.
DR Gramene; AT1G28130.1; AT1G28130.1; AT1G28130. [Q9FZ87-1]
DR Gramene; AT1G28130.2; AT1G28130.2; AT1G28130. [Q9FZ87-2]
DR KEGG; ath:AT1G28130; -.
DR Araport; AT1G28130; -.
DR TAIR; locus:2010484; AT1G28130.
DR eggNOG; ENOG502QPMU; Eukaryota.
DR HOGENOM; CLU_016249_2_1_1; -.
DR InParanoid; Q9FZ87; -.
DR OMA; PACDPHD; -.
DR PhylomeDB; Q9FZ87; -.
DR BioCyc; ARA:AT1G28130-MON; -.
DR BioCyc; MetaCyc:AT1G28130-MON; -.
DR PRO; PR:Q9FZ87; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ87; baseline and differential.
DR Genevisible; Q9FZ87; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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..609
FT /note="Indole-3-acetic acid-amido synthetase GH3.17"
FT /id="PRO_0000203577"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_015094"
SQ SEQUENCE 609 AA; 68864 MW; 1CD031FC5AB14042 CRC64;
MIPSYDPNDT EAGLKLLEDL TTNAEAIQQQ VLHQILSQNS GTQYLRAFLD GEADKNQQSF
KNKVPVVNYD DVKPFIQRIA DGESSDIVSA QPITELLTSS GTSAGKPKLM PSTAEELERK
TFFYSMLVPI MNKYVDGLDE GKGMYLLFIK PEIKTPSGLM ARPVLTSYYK SQHFRNRPFN
KYNVYTSPDQ TILCQDSKQS MYCQLLCGLV QRSHVLRVGA VFASAFLRAV KFLEDHYKEL
CADIRTGTVT SWITDSSCRD SVLSILNGPN QELADEIESE CAEKSWEGIL RRIWPKAKYV
EVIVTGSMAQ YIPTLEFYSG GLPLVSTMYA SSECYFGINL NPLCDPADVS YTLLPNMAYF
EFLPVDDKSH EEIHFATHSN TDDDDDALKE DLIVNLVNVE VGQYYEIVIT TFTGLYRYRV
GDILKVTGFH NKAPQFRFVQ RRNVVLSIDT DKTSEEDLLN AVTQAKLNHL QHPSSLLLTE
YTSYADTSSI PGHYVLFWEL KPRHSNDPPK LDDKTMEDCC SEVEDCLDYV YRRCRNRDKS
IGPLEIRVVS LGTFDSLMDF CVSQGSSLNQ YKTPRCVKSG GALEILDSRV IGRFFSKRVP
QWEPLGLDS
