ID   LOXC_ARATH              Reviewed;         896 AA.
AC   P38418; Q8W4E4; Q9M1U5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 79.
DE   RecName: Full=Lipoxygenase, chloroplastic;
DE            EC=1.13.11.12;
DE   Flags: Precursor;
GN   Name=LOX2; OrderedLocusNames=At3g45140; ORFNames=T14D3.80;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94120003; PubMed=8290626; DOI=10.1104/pp.103.4.1133;
RA   Bell E., Mullet J.E.;
RT   "Characterization of an Arabidopsis lipoxygenase gene responsive to
RT   methyl jasmonate and wounding.";
RL   Plant Physiol. 103:1133-1137(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Plant lipoxygenase may be involved in a number of
CC       diverse aspects of plant physiology including growth and
CC       development, pest resistance, and senescence or responses to
CC       wounding. It catalyzes the hydroperoxidation of lipids, containing
CC       a cis,cis-1,4-pentadiene structure.
CC   -!- CATALYTIC ACTIVITY: Linoleate + O(2) = (9Z,11E)-(13S)-13-
CC       hydroperoxyoctadeca-9,11-dienoate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit. Iron is tightly bound (By
CC       similarity).
CC   -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC   -!- INTERACTION:
CC       O04663:EIF4E2; NbExp=5; IntAct=EBI-1770437, EBI-1770425;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (Potential).
CC   -!- TISSUE SPECIFICITY: In leaves and inflorescences but not abundant
CC       in seeds, roots and stems.
CC   -!- INDUCTION: By methyl jasmonate and wounding.
CC   -!- SIMILARITY: Belongs to the lipoxygenase family.
CC   -!- SIMILARITY: Contains 1 lipoxygenase domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB72152.1; Type=Erroneous gene model prediction;
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DR   EMBL; L23968; AAA32749.1; -; mRNA.
DR   EMBL; AL138649; CAB72152.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY062611; AAL32689.1; -; mRNA.
DR   PIR; JQ2391; JQ2391.
DR   PIR; T47454; T47454.
DR   RefSeq; NP_566875.1; -.
DR   UniGene; At.22079; -.
DR   HSSP; P08170; 2SBL.
DR   IntAct; P38418; -.
DR   SWISS-2DPAGE; P38418; -.
DR   ProMEX; P38418; -.
DR   GeneID; 823650; -.
DR   GenomeReviews; BA000014_GR; AT3G45140.
DR   KEGG; ath:AT3G45140; -.
DR   NMPDR; fig|3702.1.peg.15728; -.
DR   TAIR; At3g45140; -.
DR   ArrayExpress; P38418; -.
DR   GermOnline; AT3G45140; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016165; F:lipoxygenase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000907; LipOase.
DR   InterPro; IPR013819; LipOase_C.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR001246; LipOase_pln.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   PANTHER; PTHR11771; LipOase; 1.
DR   Pfam; PF00305; Lipoxygenase; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   PRINTS; PR00087; LIPOXYGENASE.
DR   PRINTS; PR00468; PLTLPOXGNASE.
DR   SMART; SM00308; LH2; 1.
DR   PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR   PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR   PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR   PROSITE; PS50095; PLAT; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Complete proteome; Dioxygenase; Fatty acid biosynthesis;
KW   Iron; Lipid synthesis; Metal-binding; Oxidoreductase;
KW   Oxylipin biosynthesis; Plastid; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   CHAIN         ?    896       Lipoxygenase, chloroplastic.
FT                                /FTId=PRO_0000018326.
FT   DOMAIN       79    199       PLAT.
FT   DOMAIN      202    896       Lipoxygenase.
FT   METAL       554    554       Iron; catalytic (By similarity).
FT   METAL       559    559       Iron; catalytic (By similarity).
FT   METAL       746    746       Iron; catalytic (By similarity).
FT   METAL       750    750       Iron; catalytic (By similarity).
FT   METAL       896    896       Iron; via carboxylate; catalytic (By
FT                                similarity).
FT   CONFLICT    613    613       W -> C (in Ref. 3; AAL32689).
SQ   SEQUENCE   896 AA;  102046 MW;  F32822205C8F9F22 CRC64;
     MYCRESLSSL QTLNVAKSLS SLFPKQSALI NPISAGRRNN LPRPNLRRRC KVTASRANIE
     QEGNTVKEPI QNIKVKGYIT AQEEFLEGIT WSRGLDDIAD IRGRSLLVEL ISAKTDQRIT
     VEDYAQRVWA EAPDEKYECE FEMPEDFGPV GAIKIQNQYH RQLFLKGVEL KLPGGSITFT
     CESWVAPKSV DPTKRIFFSD KSYLPSQTPE PLKKYRKEEL ETLQGKNREE VGEFTKFERI
     YDYDVYNDVG DPDNDPELAR PVIGGLTHPY PRRCKTGRKP CETDPSSEQR YGGEFYVPRD
     EEFSTAKGTS FTGKAVLAAL PSIFPQIESV LLSPQEPFPH FKAIQNLFEE GIQLPKDAGL
     LPLLPRIIKA LGEAQDDILQ FDAPVLINRD RFSWLRDDEF ARQTLAGLNP YSIQLVEEWP
     LISKLDPAVY GDPTSLITWE IVEREVKGNM TVDEALKNKR LFVLDYHDLL LPYVNKVREL
     NNTTLYASRT LFFLSDDSTL RPVAIELTCP PNINKPQWKQ VFTPGYDATS CWLWNLAKTH
     AISHDAGYHQ LISHWLRTHA CTEPYIIAAN RQLSAMHPIY RLLHPHFRYT MEINARARQS
     LVNGGGIIET CFWPGKYALE LSSAVYGKLW RFDQEGLPAD LIKRGLAEED KTAEHGVRLT
     IPDYPFANDG LILWDAIKEW VTDYVKHYYP DEELITSDEE LQGWWSEVRN IGHGDKKDEP
     WWPVLKTQDD LIGVVTTIAW VTSGHHAAVN FGQYGYGGYF PNRPTTTRIR MPTEDPTDEA
     LKEFYESPEK VLLKTYPSQK QATLVMVTLD LLSTHSPDEE YIGEQQEASW ANEPVINAAF
     ERFKGKLQYL EGVIDERNVN ITLKNRAGAG VVKYELLKPT SEHGVTGMGV PYSISI
//