GH38_ORYSI
ID GH38_ORYSI Reviewed; 605 AA.
AC A3BLS0; A2YN96; Q7XIN9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Indole-3-acetic acid-amido synthetase GH3.8 {ECO:0000305};
DE EC=6.3.2.- {ECO:0000305|PubMed:18192436};
DE AltName: Full=Auxin-responsive GH3-like protein 8 {ECO:0000303|PubMed:15856348};
DE Short=OsGH3-8 {ECO:0000303|PubMed:15856348};
GN Name=GH3.8; Synonyms=GH3-8 {ECO:0000303|PubMed:18192436};
GN ORFNames=OsI_025789;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16146529; DOI=10.1111/j.1365-313x.2005.02504.x;
RA Prasad K., Parameswaran S., Vijayraghavan U.;
RT "OsMADS1, a rice MADS-box factor, controls differentiation of specific cell
RT types in the lemma and palea and is an early-acting regulator of inner
RT floral organs.";
RL Plant J. 43:915-928(2005).
RN [3]
RP TISSUE SPECIFICITY, INDUCTION, AND NOMENCLATURE.
RX PubMed=15856348; DOI=10.1007/s10142-005-0142-5;
RA Jain M., Kaur N., Tyagi A.K., Khurana J.P.;
RT "The auxin-responsive GH3 gene family in rice (Oryza sativa).";
RL Funct. Integr. Genomics 6:36-46(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18192436; DOI=10.1105/tpc.107.055657;
RA Ding X., Cao Y., Huang L., Zhao J., Xu C., Li X., Wang S.;
RT "Activation of the indole-3-acetic acid-amido synthetase GH3-8 suppresses
RT expansin expression and promotes salicylate- and jasmonate-independent
RT basal immunity in rice.";
RL Plant Cell 20:228-240(2008).
RN [5]
RP FUNCTION, AND INDUCTION BY AUXIN.
RX PubMed=22016342; DOI=10.1093/pcp/pcr142;
RA Yadav S.R., Khanday I., Majhi B.B., Veluthambi K., Vijayraghavan U.;
RT "Auxin-responsive OsMGH3, a common downstream target of OsMADS1 and
RT OsMADS6, controls rice floret fertility.";
RL Plant Cell Physiol. 52:2123-2135(2011).
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 excessive free auxin (PubMed:18192436). Produces more IAA-
CC Asp levels than IAA-Ala levels in vitro (PubMed:18192436). May
CC participate in the activation of disease resistance by preventing the
CC accumulation of free IAA, which reduces the expression of a group of
CC auxin-responsive genes encoding expansins that control cell wall
CC loosening and expansion (PubMed:18192436). Contributes to late events
CC in stamen and carpel differentiation, and influences floret fertility
CC (PubMed:22016342). {ECO:0000269|PubMed:18192436,
CC ECO:0000269|PubMed:22016342}.
CC -!- TISSUE SPECIFICITY: Expressed in the inner floral organs (lodicules,
CC stamens and carpels) and at lower levels in lemmas and paleas.
CC {ECO:0000269|PubMed:15856348, ECO:0000269|PubMed:16146529}.
CC -!- DEVELOPMENTAL STAGE: Expressed at early stage of flower development in
CC floral meristem and at later stage in lemma, palea and carpel
CC primordia. {ECO:0000269|PubMed:16146529}.
CC -!- INDUCTION: Induced by auxin. {ECO:0000269|PubMed:15856348,
CC ECO:0000269|PubMed:22016342}.
CC -!- DISRUPTION PHENOTYPE: Slight increase in disease susceptibility to
CC Xanthomonas oryzae pv oryzae. {ECO:0000269|PubMed:18192436}.
CC -!- MISCELLANEOUS: Plants overexpressing GH3-8 exhibit enhanced disease
CC resistance to Xanthomonas oryzae pv oryzae (PubMed:18192436). Plants
CC overexpressing GH3-8 exhibit abnormal morphology and dwarf phenotype
CC (PubMed:18192436, PubMed:22016342). Plants silencing GH3-8 produce
CC mostly non-viable pollen grains (PubMed:22016342).
CC {ECO:0000269|PubMed:18192436, ECO:0000269|PubMed:22016342}.
CC -!- SIMILARITY: Belongs to the IAA-amido conjugating enzyme family.
CC {ECO:0000305}.
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DR EMBL; CM000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A3BLS0; -.
DR SMR; A3BLS0; -.
DR STRING; 39946.A3BLS0; -.
DR EnsemblPlants; BGIOSGA023979-TA; BGIOSGA023979-PA; BGIOSGA023979.
DR Gramene; BGIOSGA023979-TA; BGIOSGA023979-PA; BGIOSGA023979.
DR HOGENOM; CLU_016249_2_1_1; -.
DR OMA; EGFFAIQ; -.
DR Proteomes; UP000007015; Chromosome 7.
DR ExpressionAtlas; A3BLS0; differential.
DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
DR GO; GO:0010279; F:indole-3-acetic acid amido synthetase activity; IDA:UniProtKB.
DR GO; GO:0010252; P:auxin homeostasis; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:UniProtKB.
DR InterPro; IPR004993; GH3.
DR PANTHER; PTHR31901; PTHR31901; 1.
DR Pfam; PF03321; GH3; 1.
PE 1: Evidence at protein level;
KW Ligase; Plant defense; Reference proteome.
FT CHAIN 1..605
FT /note="Indole-3-acetic acid-amido synthetase GH3.8"
FT /id="PRO_0000296247"
FT BINDING 115
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q0D4Z6"
FT BINDING 342..346
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q0D4Z6"
FT BINDING 365
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q0D4Z6"
FT BINDING 421
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q0D4Z6"
FT BINDING 440
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q0D4Z6"
SQ SEQUENCE 605 AA; 66932 MW; F8F8035441FFA3B2 CRC64;
MAVMTDVSTT GTALRTPAAG AVKEGDVEKL RFIDEMTTNV DAVQERVLGE ILGRNAGTEY
LTKCGLDGAT DRAAFRAKVP VVSYDDLQPY IQRIANGDRS PILSTHPVSE FLTSSGTSAG
ERKLMPTIMD ELDRRQLLYS LLMPVMNLYV PGLDKGKGLY FLFVKSETKT PGGLTARPVL
TSYYKSDHFK NRPYDPYHNY TSPTAAILCA DAFQSMYAQM VCGLCQRNDV LRLGAVFASG
LLRAIRFLQL NWEQLADDIE SGELTPRVTD PSVREAVAAI LLPDPELAKL IRAECSKGDW
AGIITRVWPN TKYLDVIVTG AMAQYIPTLE FYSGGLPMAC TMYASSECYF GLNLRPMCDP
SEVSYTIMPN MGYFEFLPVD ETGAASGDAT QLVDLARVEV GREYELVITT YAGLNRYRVG
DVLRVTGFHN AAPQFRFVRR KNVLLSIESD KTDEAELQRA VERASALLRP HGASVVEYTS
QACTKRIPGH YVIYWELLTK GAGATVVDAD TLGRCCLEME EALNTVYRQS RVADGSIGPL
EIRVVRPGTF EELMDYAISR GASINQYKVP RCVTFPPIVE LLDSRVVSSH FSPALPHWTP
ARRSE
