Reviewed, UniProtKB/Swiss-Prot P38418 (LOXC_ARATH)

Names and origin

Protein names

Recommended name:
    Lipoxygenase, chloroplastic
    EC=1.13.11.12

Gene names

Name:	LOX2
Ordered Locus Names:	At3g45140
ORF Names:	T14D3.80

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	896 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure.
Catalytic activity	Linoleate + O(2) = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate.
Cofactor	Binds 1 iron ion per subunit. Iron is tightly bound By similarity.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Plastid › chloroplastPotential.
Tissue specificity	In leaves and inflorescences but not abundant in seeds, roots and stems.
Induction	By methyl jasmonate and wounding.
Sequence similarities	Belongs to the lipoxygenase family. Contains 1 lipoxygenase domain. Contains 1 PLAT domain.
Sequence caution	The sequence CAB72152.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro lipoxygenase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4E2	O04663	5	EBI-1770437,EBI-1770425

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 896		Lipoxygenase, chloroplastic		PRO_0000018326
Regions
	Domain	79 – 199	121	PLAT
	Domain	202 – 896	695	Lipoxygenase
Sites
	Metal binding	554	1	Iron; catalytic By similarity
	Metal binding	559	1	Iron; catalytic By similarity
	Metal binding	746	1	Iron; catalytic By similarity
	Metal binding	750	1	Iron; catalytic By similarity
	Metal binding	896	1	Iron; via carboxylate; catalytic By similarity
Experimental info
	Sequence conflict	613	1	W → C in AAL32689. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38418-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: F32822205C8F9F22	FASTA	896	102,046
	10 20 30 40 50 60 MYCRESLSSL QTLNVAKSLS SLFPKQSALI NPISAGRRNN LPRPNLRRRC KVTASRANIE 70 80 90 100 110 120 QEGNTVKEPI QNIKVKGYIT AQEEFLEGIT WSRGLDDIAD IRGRSLLVEL ISAKTDQRIT 130 140 150 160 170 180 VEDYAQRVWA EAPDEKYECE FEMPEDFGPV GAIKIQNQYH RQLFLKGVEL KLPGGSITFT 190 200 210 220 230 240 CESWVAPKSV DPTKRIFFSD KSYLPSQTPE PLKKYRKEEL ETLQGKNREE VGEFTKFERI 250 260 270 280 290 300 YDYDVYNDVG DPDNDPELAR PVIGGLTHPY PRRCKTGRKP CETDPSSEQR YGGEFYVPRD 310 320 330 340 350 360 EEFSTAKGTS FTGKAVLAAL PSIFPQIESV LLSPQEPFPH FKAIQNLFEE GIQLPKDAGL 370 380 390 400 410 420 LPLLPRIIKA LGEAQDDILQ FDAPVLINRD RFSWLRDDEF ARQTLAGLNP YSIQLVEEWP 430 440 450 460 470 480 LISKLDPAVY GDPTSLITWE IVEREVKGNM TVDEALKNKR LFVLDYHDLL LPYVNKVREL 490 500 510 520 530 540 NNTTLYASRT LFFLSDDSTL RPVAIELTCP PNINKPQWKQ VFTPGYDATS CWLWNLAKTH 550 560 570 580 590 600 AISHDAGYHQ LISHWLRTHA CTEPYIIAAN RQLSAMHPIY RLLHPHFRYT MEINARARQS 610 620 630 640 650 660 LVNGGGIIET CFWPGKYALE LSSAVYGKLW RFDQEGLPAD LIKRGLAEED KTAEHGVRLT 670 680 690 700 710 720 IPDYPFANDG LILWDAIKEW VTDYVKHYYP DEELITSDEE LQGWWSEVRN IGHGDKKDEP 730 740 750 760 770 780 WWPVLKTQDD LIGVVTTIAW VTSGHHAAVN FGQYGYGGYF PNRPTTTRIR MPTEDPTDEA 790 800 810 820 830 840 LKEFYESPEK VLLKTYPSQK QATLVMVTLD LLSTHSPDEE YIGEQQEASW ANEPVINAAF 850 860 870 880 890 ERFKGKLQYL EGVIDERNVN ITLKNRAGAG VVKYELLKPT SEHGVTGMGV PYSISI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of an Arabidopsis lipoxygenase gene responsive to methyl jasmonate and wounding." Bell E., Mullet J.E. Plant Physiol. 103:1133-1137(1993) [PubMed: 8290626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L23968 mRNA. Translation: AAA32749.1. AL138649 Genomic DNA. Translation: CAB72152.1. Sequence problems. AY062611 mRNA. Translation: AAL32689.1.
PIR	JQ2391. T47454.
RefSeq	NP_566875.1.
UniGene	At.22079
3D structure databases
HSSP	HSSP built from PDB template 2SBL based on UniProtKB P08170.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38418.
2-D gel databases
SWISS-2DPAGE	P38418.
Proteomic databases
ProMEX	P38418.
Genome annotation databases
GeneID	823650.
GenomeReviews	Gene locus AT3G45140 in contig BA000014_GR.
KEGG	ath:AT3G45140.
NMPDR	fig|3702.1.peg.15728.
Organism-specific databases
TAIR	At3g45140.
Gene expression databases
ArrayExpress	P38418.
GermOnline	AT3G45140. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000907. LipOase. IPR013819. LipOase_C. IPR001024. LipOase_LH2. IPR001246. LipOase_pln. [Graphical view]
Gene3D	G3DSA:2.60.60.20. Lipase_LipOase. 1 hit.
PANTHER	PTHR11771. LipOase. 1 hit.
Pfam	PF00305. Lipoxygenase. 1 hit. PF01477. PLAT. 1 hit. [Graphical view]
PRINTS	PR00087. LIPOXYGENASE. PR00468. PLTLPOXGNASE.
SMART	SM00308. LH2. 1 hit. [Graphical view]
PROSITE	PS00711. LIPOXYGENASE_1. 1 hit. PS00081. LIPOXYGENASE_2. 1 hit. PS51393. LIPOXYGENASE_3. 1 hit. PS50095. PLAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LOXC_ARATH

Accession

Primary (citable) accession number: P38418
Secondary accession number(s): Q8W4E4, Q9M1U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 25, 2008
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)