Y74B2_ARATH
ID Y74B2_ARATH Reviewed; 384 AA.
AC B3LF83; Q8RXK9; Q9SUL4;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable inactive linolenate hydroperoxide lyase {ECO:0000305|PubMed:9701595};
DE AltName: Full=Cytochrome P450 74B2 {ECO:0000305};
DE AltName: Full=Hydroperoxide lyase 1 {ECO:0000303|PubMed:9701595};
GN Name=CYP74B2 {ECO:0000305}; Synonyms=HPL1 {ECO:0000303|PubMed:9701595};
GN OrderedLocusNames=At4g15440; ORFNames=dl3766w;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-384.
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 [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY WOUNDING.
RX PubMed=9701595; DOI=10.1104/pp.117.4.1393;
RA Bate N.J., Sivasankar S., Moxon C., Riley J.M., Thompson J.E.,
RA Rothstein S.J.;
RT "Molecular characterization of an Arabidopsis gene encoding hydroperoxide
RT lyase, a cytochrome P-450 that is wound inducible.";
RL Plant Physiol. 117:1393-1400(1998).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16258015; DOI=10.1104/pp.105.067249;
RA Duan H., Huang M.Y., Palacio K., Schuler M.A.;
RT "Variations in CYP74B2 (hydroperoxide lyase) gene expression differentially
RT affect hexenal signaling in the Columbia and Landsberg erecta ecotypes of
RT Arabidopsis.";
RL Plant Physiol. 139:1529-1544(2005).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers and siliques.
CC {ECO:0000269|PubMed:16258015, ECO:0000269|PubMed:9701595}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:9701595}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: In cv. Columbia, CYP74B2 (AC B3LF83) DNA sequence contains a
CC 10-bp deletion that leads to a shorter N-terminus compared to typical
CC other CYP74B subfamily members, and CYP74B2 is thought to be a non-
CC functional enzyme. Functional alleles, with full N-terminus are found
CC in cv. Landsberg erecta and cv. Wassilewskija (AC Q9ZSY9).
CC {ECO:0000269|PubMed:16258015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45989.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78586.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97339; CAB45989.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78586.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83604.1; -; Genomic_DNA.
DR EMBL; BT033071; ACE82594.1; -; mRNA.
DR EMBL; AY080827; AAL87304.1; -; mRNA.
DR PIR; D85170; D85170.
DR RefSeq; NP_193279.1; NM_117633.3.
DR AlphaFoldDB; B3LF83; -.
DR SMR; B3LF83; -.
DR STRING; 3702.AT4G15440.1; -.
DR PaxDb; B3LF83; -.
DR PRIDE; B3LF83; -.
DR ProteomicsDB; 242370; -.
DR DNASU; 827215; -.
DR EnsemblPlants; AT4G15440.1; AT4G15440.1; AT4G15440.
DR GeneID; 827215; -.
DR Gramene; AT4G15440.1; AT4G15440.1; AT4G15440.
DR KEGG; ath:AT4G15440; -.
DR Araport; AT4G15440; -.
DR TAIR; locus:2130145; AT4G15440.
DR eggNOG; ENOG502QQNS; Eukaryota.
DR HOGENOM; CLU_045757_0_0_1; -.
DR InParanoid; B3LF83; -.
DR OMA; DMRVCAY; -.
DR OrthoDB; 485250at2759; -.
DR PhylomeDB; B3LF83; -.
DR BioCyc; ARA:AT4G15440-MON; -.
DR BioCyc; ARA:MON-1583; -.
DR BioCyc; MetaCyc:MON-1583; -.
DR BRENDA; 4.2.1.92; 399.
DR PRO; PR:B3LF83; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; B3LF83; baseline and differential.
DR Genevisible; B3LF83; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..384
FT /note="Probable inactive linolenate hydroperoxide lyase"
FT /id="PRO_0000431454"
FT BINDING 346
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 384 AA; 42667 MW; 40F5451AB76BC79A CRC64;
MDLVDKRDVL IGDFRPSLGF YGGVRVGVYL DTTEPKHAKI KGFAMETLKR SSKVWLQELR
SNLNIFWGTI ESEISKNGAA SYIFPLQRCI FSFLCASLAG VDASVSPDIA ENGWKTINTW
LALQVIPTAK LGVVPQPLEE ILLHTWPYPS LLIAGNYKKL YNFIDENAGD CLRLGQEEFG
LTRDEAIQNL LFVLGFNAYG GFSVFLPSLI GRITGDNSGL QERIRTEVRR VCGSGSDLNF
KTVNEMELVK SVVYETLRFS PPVPLQFARA RKDFQISSHD AVFEVKKGEL LCGYQPLVMR
DANVFDEPEE FKPDRYVGET GSELLNYLYW SNGPQTGTPS ASNKQCAAKD IVTLTASLLV
ADLFLRYDTI TGDSGSIKAV VKAK
