Reviewed, UniProtKB/Swiss-Prot P38418 (LOX2_ARATH)

Names and origin

Protein names

Recommended name:
    Lipoxygenase 2, chloroplastic
      Short name=AtLOX2
    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 › malvids › 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	13S-lipoxygenase that can use linolenic acid as substrates. 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. Required for the wound-induced synthesis of jasmonic acid (JA) in leaves. Ref.6 Ref.25
Catalytic activity	Linoleate + O2 = (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.
Subunit structure	Interacts with EIF4E2. Ref.8
Subcellular location	Plastid › chloroplast. Cytoplasm. Note: The unprocessed form is cytoplasmic whereas the cleaved form is chloroplastic. Ref.6 Ref.8 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.24
Tissue specificity	In leaves and inflorescences but not abundant in seeds, roots and stems. Ref.21
Developmental stage	Expression is sharply reduced in leaves during leaf senescence. Ref.11
Induction	By methyl jasmonate (MeJA) and wounding, probably through nitric oxide-mediated (NO) induction. Slightly locally induced upon herbivors infestation such as aphids (Myzus persicae and Brevicoryne brassicae), or caterpillar (Spodoptera exigua). Induced by leaf-volatiles generated by herbivors-mediated wounding such as (E)-2-hexenal, (Z)-3-hexenal, (Z)-3-hexenol or allo-ocimene (2,6-dimethyl-2,4,6-octatriene). Increased levels by bacterial pathogens (e.g. Pseudomonas viridiflava and P. syringae pv. tomato). Repressed by WRKY62. Ref.7 Ref.9 Ref.10 Ref.15 Ref.17 Ref.19 Ref.20 Ref.23
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 Cytoplasm Plastid
Domain	Transit peptide
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	jasmonic acid biosynthetic process Ref.6 Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to bacterium Ref.20 Inferred from expression pattern. Source: UniProtKB response to fungus Inferred from expression pattern. Source: TAIR response to herbivore Ref.9 Ref.23 Inferred from expression pattern. Source: UniProtKB response to jasmonic acid stimulus Inferred from expression pattern. Source: TAIR response to wounding Ref.9 Inferred from expression pattern. Source: UniProtKB
Cellular component	chloroplast envelope Ref.12 Inferred from direct assay. Source: TAIR chloroplast stroma Ref.18 Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Ref.14 Ref.16 Inferred from direct assay. Source: TAIR
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW lipoxygenase activity Ref.6 Ref.25 Inferred from direct assay. Source: UniProtKB protein binding Ref.8 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 – 56	56	Chloroplast Potential
	Chain	57 – 896	840	Lipoxygenase 2, chloroplastic		PRO_0000018326
Regions
	Domain	79 – 199	121	PLAT
	Domain	202 – 896	695	Lipoxygenase
	Region	175 – 232	58	EIF4E2 binding
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	119 – 125	7	ITVEDYA → EYTFFFL in BAC43666. Ref.4
	Sequence conflict	613	1	W → C in AAL32689. Ref.3
	Sequence conflict	646	1	L → V in BAF01939. Ref.5
	Sequence conflict	731	1	L → F in BAF01939. Ref.5

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.
[4]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-125. Strain: cv. Columbia.
[5]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 454-896. Strain: cv. Columbia.
[6]	"A chloroplast lipoxygenase is required for wound-induced jasmonic acid accumulation in Arabidopsis." Bell E., Creelman R.A., Mullet J.E. Proc. Natl. Acad. Sci. U.S.A. 92:8675-8679(1995) [PubMed: 7567995] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Involvement of phospholipase D in wound-induced accumulation of jasmonic acid in arabidopsis." Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X. Plant Cell 12:2237-2246(2000) [PubMed: 11090221] [Abstract] Cited for: INDUCTION BY WOUNDING.
[8]	"Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein." Freire M.A., Tourneur C., Granier F., Camonis J., El Amrani A., Browning K.S., Robaglia C. Plant Mol. Biol. 44:129-140(2000) [PubMed: 11117257] [Abstract] Cited for: INTERACTION WITH EIF4E2, SUBCELLULAR LOCATION.
[9]	"Molecular responses to aphid feeding in Arabidopsis in relation to plant defense pathways." Moran P.J., Thompson G.A. Plant Physiol. 125:1074-1085(2001) [PubMed: 11161062] [Abstract] Cited for: INDUCTION BY APHIDS AND WOUNDING.
[10]	"Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis." Jensen A.B., Raventos D., Mundy J. Plant J. 29:595-606(2002) [PubMed: 11874572] [Abstract] Cited for: INDUCTION BY JASMONATE.
[11]	"Evidence supporting a role of jasmonic acid in Arabidopsis leaf senescence." He Y., Fukushige H., Hildebrand D.F., Gan S. Plant Physiol. 128:876-884(2002) [PubMed: 11891244] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[12]	"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis." Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S. J. Proteome Res. 2:413-425(2003) [PubMed: 12938931] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions." Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S. Curr. Biol. 14:354-362(2004) [PubMed: 15028209] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy." Peltier J.-B., Ytterberg A.J., Sun Q., van Wijk K.J. J. Biol. Chem. 279:49367-49383(2004) [PubMed: 15322131] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Nitric oxide is induced by wounding and influences jasmonic acid signaling in Arabidopsis thaliana." Huang X., Stettmaier K., Michel C., Hutzler P., Mueller M.J., Durner J. Planta 218:938-946(2004) [PubMed: 14716563] [Abstract] Cited for: INDUCTION BY NITRIC OXIDE.
[16]	"In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database." Friso G., Giacomelli L., Ytterberg A.J., Peltier J.-B., Rudella A., Sun Q., van Wijk K.J. Plant Cell 16:478-499(2004) [PubMed: 14729914] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Volatile C6-aldehydes and allo-ocimene activate defense genes and induce resistance against Botrytis cinerea in Arabidopsis thaliana." Kishimoto K., Matsui K., Ozawa R., Takabayashi J. Plant Cell Physiol. 46:1093-1102(2005) [PubMed: 15879447] [Abstract] Cited for: INDUCTION BY LEAF VOLATILES.
[18]	"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts." Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J. Mol. Cell. Proteomics 5:114-133(2006) [PubMed: 16207701] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Transcriptional responses of Arabidopsis thaliana ecotypes with different glucosinolate profiles after attack by polyphagous Myzus persicae and oligophagous Brevicoryne brassicae." Kusnierczyk A., Winge P., Midelfart H., Armbruster W.S., Rossiter J.T., Bones A.M. J. Exp. Bot. 58:2537-2552(2007) [PubMed: 17545220] [Abstract] Cited for: INDUCTION BY MYZUS PERSICAE AND BREVICORYNE BRASSICAE.
[20]	"The role of pectate lyase and the jasmonic acid defense response in Pseudomonas viridiflava virulence." Jakob K., Kniskern J.M., Bergelson J. Mol. Plant Microbe Interact. 20:146-158(2007) [PubMed: 17313166] [Abstract] Cited for: INDUCTION BY BACTERIAL PATHOGENS.
[21]	"Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade." Vellosillo T., Martinez M., Lopez M.A., Vicente J., Cascon T., Dolan L., Hamberg M., Castresana C. Plant Cell 19:831-846(2007) [PubMed: 17369372] [Abstract] Cited for: TISSUE SPECIFICITY.
[22]	"WRKY62 transcription factor acts downstream of cytosolic NPR1 and negatively regulates jasmonate-responsive gene expression." Mao P., Duan M., Wei C., Li Y. Plant Cell Physiol. 48:833-842(2007) [PubMed: 17510065] [Abstract] Cited for: REPRESSION BY WRKY62.
[23]	"Caterpillar saliva interferes with induced Arabidopsis thaliana defence responses via the systemic acquired resistance pathway." Weech M.-H., Chapleau M., Pan L., Ide C., Bede J.C. J. Exp. Bot. 59:2437-2448(2008) [PubMed: 18487634] [Abstract] Cited for: INDUCTION BY CATERPILLAR.
[24]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed: 18431481] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]	"Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana." Bannenberg G., Martinez M., Hamberg M., Castresana C. Lipids 44:85-95(2009) [PubMed: 18949503] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L23968 mRNA. Translation: AAA32749.1. AL138649 Genomic DNA. Translation: CAB72152.1. Sequence problems. AY062611 mRNA. Translation: AAL32689.1. AK119093 mRNA. Translation: BAC43666.1. AK222075 mRNA. Translation: BAD94917.1. AK230124 mRNA. Translation: BAF01939.1.
IPI	IPI00548522.
PIR	JQ2391. T47454.
RefSeq	NP_566875.1.
UniGene	At.22079
3D structure databases
SMR	P38418. Positions 96-896.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38418. 4 interactions.
STRING	P38418.
2-D gel databases
SWISS-2DPAGE	P38418.
Proteomic databases
PRIDE	P38418.
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.
Phylogenomic databases
eggNOG	euNOG05471.
HOGENOM	HBG749429.
InParanoid	P38418.
OMA	DTYNDLG.
PhylomeDB	P38418.
Enzyme and pathway databases
BRENDA	1.13.11.12. 302.
Gene expression databases
ArrayExpress	P38418.
Genevestigator	P38418.
GermOnline	AT3G45140. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008976. Lipase_LipOase. IPR000907. LipOase. IPR013819. LipOase_C. IPR020834. LipOase_CS. IPR020833. LipOase_Fe_BS. 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

LOX2_ARATH

Accession

Primary (citable) accession number: P38418
Secondary accession number(s): Q0WLR8 , Q56WG6, Q8GW45, Q8W4E4, Q9M1U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	February 9, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)