YUC4_ARATH
ID YUC4_ARATH Reviewed; 411 AA.
AC Q9LFM5; Q3E9I6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA4;
DE EC=1.14.13.168;
DE AltName: Full=Flavin-containing monooxygenase YUCCA4;
GN Name=YUC4; Synonyms=THREAD, YUCCA4; OrderedLocusNames=At5g11320;
GN ORFNames=F2I11_210;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16818609; DOI=10.1101/gad.1415106;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
RT formation of floral organs and vascular tissues in Arabidopsis.";
RL Genes Dev. 20:1790-1799(2006).
RN [4]
RP INDUCTION BY STY1.
RX PubMed=16740145; DOI=10.1111/j.1365-313x.2006.02775.x;
RA Sohlberg J.J., Myrenaas M., Kuusk S., Lagercrantz U., Kowalczyk M.,
RA Sandberg G., Sundberg E.;
RT "STY1 regulates auxin homeostasis and affects apical-basal patterning of
RT the Arabidopsis gynoecium.";
RL Plant J. 47:112-123(2006).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17704214; DOI=10.1105/tpc.107.053009;
RA Cheng Y., Dai X., Zhao Y.;
RT "Auxin synthesized by the YUCCA flavin monooxygenases is essential for
RT embryogenesis and leaf formation in Arabidopsis.";
RL Plant Cell 19:2430-2439(2007).
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 50:902-910(2007).
RN [7]
RP INDUCTION BY LEC2.
RX PubMed=18287041; DOI=10.1073/pnas.0712364105;
RA Stone S.L., Braybrook S.A., Paula S.L., Kwong L.W., Meuser J.,
RA Pelletier J., Hsieh T.-F., Fischer R.L., Goldberg R.B., Harada J.J.;
RT "Arabidopsis LEAFY COTYLEDON2 induces maturation traits and auxin activity:
RT implications for somatic embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3151-3156(2008).
RN [8]
RP INDUCTION BY NGA3.
RX PubMed=19435937; DOI=10.1105/tpc.109.065508;
RA Trigueros M., Navarrete-Gomez M., Sato S., Christensen S.K., Pelaz S.,
RA Weigel D., Yanofsky M.F., Ferrandiz C.;
RT "The NGATHA genes direct style development in the Arabidopsis gynoecium.";
RL Plant Cell 21:1394-1409(2009).
RN [9]
RP INDUCTION BY STY1.
RX PubMed=20154152; DOI=10.1105/tpc.108.064816;
RA Eklund D.M., Staaldal V., Valsecchi I., Cierlik I., Eriksson C.,
RA Hiratsu K., Ohme-Takagi M., Sundstroem J.F., Thelander M., Ezcurra I.,
RA Sundberg E.;
RT "The Arabidopsis thaliana STYLISH1 protein acts as a transcriptional
RT activator regulating auxin biosynthesis.";
RL Plant Cell 22:349-363(2010).
RN [10]
RP FUNCTION.
RX PubMed=22025721; DOI=10.1073/pnas.1108436108;
RA Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y., Kasahara H.,
RA Kamiya Y., Chory J., Zhao Y.;
RT "Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
RT AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=22233288; DOI=10.1111/j.1365-313x.2011.04866.x;
RA Kriechbaumer V., Wang P., Hawes C., Abell B.M.;
RT "Alternative splicing of the auxin biosynthesis gene YUCCA4 determines its
RT subcellular compartmentation.";
RL Plant J. 70:292-302(2012).
CC -!- FUNCTION: Involved in auxin biosynthesis. Both isoforms are
CC catalitically active. Involved during embryogenesis and seedling
CC development. Required for the formation of floral organs and vascular
CC tissues. Belongs to the set of redundant YUCCA genes probably
CC responsible for auxin biosynthesis in shoots.
CC {ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:17704214,
CC ECO:0000269|PubMed:22025721, ECO:0000269|PubMed:22233288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.168;
CC Evidence={ECO:0000269|PubMed:22233288};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane;
CC Single-pass membrane protein; Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LFM5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LFM5-2; Sequence=VSP_039987, VSP_039988;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, buds and
CC siliques. Detected in the apical gynoecium and in the developing
CC ovules. {ECO:0000269|PubMed:16818609, ECO:0000269|PubMed:22233288}.
CC -!- DEVELOPMENTAL STAGE: Expression relatively broad during early stages of
CC embryogenesis and more restricted to apical region of the cotyledons in
CC the mature embryo. {ECO:0000269|PubMed:17704214}.
CC -!- INDUCTION: Positively regulated by LEC2, by NGA3 and by STY1.
CC {ECO:0000269|PubMed:16740145, ECO:0000269|PubMed:18287041,
CC ECO:0000269|PubMed:19435937, ECO:0000269|PubMed:20154152}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC the other members of the YUCCA family. {ECO:0000269|PubMed:16818609}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC Expressed only in flowers. Contains a transmembrane at positions 334
CC - 354. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AL360314; CAB96667.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91659.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91660.1; -; Genomic_DNA.
DR RefSeq; NP_196693.1; NM_121170.3. [Q9LFM5-1]
DR RefSeq; NP_850808.1; NM_180477.2. [Q9LFM5-2]
DR AlphaFoldDB; Q9LFM5; -.
DR SMR; Q9LFM5; -.
DR STRING; 3702.AT5G11320.1; -.
DR PaxDb; Q9LFM5; -.
DR PRIDE; Q9LFM5; -.
DR ProteomicsDB; 242922; -. [Q9LFM5-1]
DR EnsemblPlants; AT5G11320.1; AT5G11320.1; AT5G11320. [Q9LFM5-1]
DR EnsemblPlants; AT5G11320.2; AT5G11320.2; AT5G11320. [Q9LFM5-2]
DR GeneID; 831003; -.
DR Gramene; AT5G11320.1; AT5G11320.1; AT5G11320. [Q9LFM5-1]
DR Gramene; AT5G11320.2; AT5G11320.2; AT5G11320. [Q9LFM5-2]
DR KEGG; ath:AT5G11320; -.
DR Araport; AT5G11320; -.
DR TAIR; locus:2147962; AT5G11320.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_2_0_1; -.
DR InParanoid; Q9LFM5; -.
DR OMA; TWRHRTY; -.
DR PhylomeDB; Q9LFM5; -.
DR BRENDA; 1.14.13.168; 399.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q9LFM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFM5; baseline and differential.
DR Genevisible; Q9LFM5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IDA:TAIR.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0009851; P:auxin biosynthetic process; IDA:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin biosynthesis; Cytoplasm; Endoplasmic reticulum;
KW FAD; Flavoprotein; Membrane; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..411
FT /note="Probable indole-3-pyruvate monooxygenase YUCCA4"
FT /id="PRO_0000400071"
FT BINDING 21..26
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 183..188
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT VAR_SEQ 334..357
FT /note="ENSFFTKEGMPKTPFPNGWKGEKG -> VLLSIYYLSYSLSCYIYVNVYMYM
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039987"
FT VAR_SEQ 358..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039988"
SQ SEQUENCE 411 AA; 45406 MW; 957AE2299820DBE2 CRC64;
MGTCRESEPT QIFVPGPIIV GAGPSGLAVA ACLSNRGVPS VILERTDCLA SLWQKRTYDR
LKLHLPKHFC ELPLMPFPKN FPKYPSKQLF ISYVESYAAR FNIKPVFNQT VEKAEFDDAS
GLWNVKTQDG VYTSTWLVVA TGENAEPVFP NIPGLKKFTG PVVHTSAYKS GSAFANRKVL
VVGCGNSGME VSLDLCRYNA LPHMVVRNSV HVLPRDFFGL STFGIAMTLL KWFPLKLVDK
FLLLLANSTL GNTDLLGLRR PKTGPIELKN VTGKTPVLDV GAISLIRSGQ IKVTQAVKEI
TRNGAKFLNG KEIEFDSIIL ATGYKSNVPD WLKENSFFTK EGMPKTPFPN GWKGEKGLYT
VGFTRRGLSG TAYDAVKIAE DITDQWMKFN GPLSCRNICS SHIIHLHFNK S
