Reviewed, UniProtKB/Swiss-Prot O49505 (NCED2_ARATH)

Names and origin

Protein names

Recommended name:
    9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic
      Short name=AtNCED2
    EC=1.13.11.51

Gene names

Name:	NCED2
Ordered Locus Names:	At4g18350
ORF Names:	F28J12.10

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

General annotation (Comments)

Function	Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Ref.3
Catalytic activity	A 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal. 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al. 9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al.
Subcellular location	Plastid › chloroplast stroma. Note: Partially bound to the thylakoid. Ref.4
Tissue specificity	Very low in all tissues. Expressed at the point of organ attachment and the abscission zones in the plant. Ref.4 Ref.5
Induction	Low induction by drought stress. Ref.4
Sequence similarities	Belongs to the carotenoid oxygenase family.

Ontologies

Keywords
Biological process	Abscisic acid biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	abscisic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Ref.4 Inferred from direct assay. Source: TAIR chloroplast thylakoid membrane Ref.4 Inferred from direct assay. Source: TAIR
Molecular function	9-cis-epoxycarotenoid dioxygenase activity Ref.3 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 583		9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic		PRO_0000285990

Sequences

	Sequence		Length	Mass (Da)
	O49505-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: A138F93542E50852	FASTA	583	65,067
	10 20 30 40 50 60 MVSLLTMPMS GGIKTWPQAQ IDLGFRPIKR QPKVIKCTVQ IDVTELTKKR QLFTPRTTAT 70 80 90 100 110 120 PPQHNPLRLN IFQKAAAIAI DAAERALISH EQDSPLPKTA DPRVQIAGNY SPVPESSVRR 130 140 150 160 170 180 NLTVEGTIPD CIDGVYIRNG ANPMFEPTAG HHLFDGDGMV HAVKITNGSA SYACRFTKTE 190 200 210 220 230 240 RLVQEKRLGR PVFPKAIGEL HGHSGIARLM LFYARGLCGL INNQNGVGVA NAGLVYFNNR 250 260 270 280 290 300 LLAMSEDDLP YQLKITQTGD LQTVGRYDFD GQLKSAMIAH PKLDPVTKEL HALSYDVVKK 310 320 330 340 350 360 PYLKYFRFSP DGVKSPELEI PLETPTMIHD FAITENFVVI PDQQVVFKLG EMISGKSPVV 370 380 390 400 410 420 FDGEKVSRLG IMPKDATEAS QIIWVNSPET FCFHLWNAWE SPETEEIVVI GSCMSPADSI 430 440 450 460 470 480 FNERDESLRS VLSEIRINLR TRKTTRRSLL VNEDVNLEIG MVNRNRLGRK TRFAFLAIAY 490 500 510 520 530 540 PWPKVSGFAK VDLCTGEMKK YIYGGEKYGG EPFFLPGNSG NGEENEDDGY IFCHVHDEET 550 560 570 580 KTSELQIINA VNLKLEATIK LPSRVPYGFH GTFVDSNELV DQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Arabidopsis ORF clones." Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis." Iuchi S., Kobayashi M., Taji T., Naramoto M., Seki M., Kato T., Tabata S., Kakubari Y., Yamaguchi-Shinozaki K., Shinozaki K. Plant J. 27:325-333(2001) [PubMed: 11532178] [Abstract] Cited for: FUNCTION.
[4]	"Molecular characterization of the Arabidopsis 9-cis epoxycarotenoid dioxygenase gene family." Tan B.-C., Joseph L.M., Deng W.-T., Liu L., Li Q.-B., Cline K., McCarty D.R. Plant J. 35:44-56(2003) [PubMed: 12834401] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY DROUGHT STRESS.
[5]	"Functional analysis of Arabidopsis NCED6 and NCED9 genes indicates that ABA synthesized in the endosperm is involved in the induction of seed dormancy." Lefebvre V., North H., Frey A., Sotta B., Seo M., Okamoto M., Nambara E., Marion-Poll A. Plant J. 45:309-319(2006) [PubMed: 16412079] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL021710 Genomic DNA. Translation: CAA16715.1. AL161548 Genomic DNA. Translation: CAB78837.1. BT030365 mRNA. Translation: ABO38778.1.
IPI	IPI00523545.
PIR	T04531.
RefSeq	NP_193569.1.
UniGene	At.32916
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	827562.
GenomeReviews	Gene locus AT4G18350 in contig CT486007_GR.
KEGG	ath:AT4G18350.
NMPDR	fig|3702.1.peg.19634.
Organism-specific databases
TAIR	At4g18350.
Enzyme and pathway databases
BRENDA	1.13.11.51. 302.
Gene expression databases
ArrayExpress	O49505.
Family and domain databases
InterPro	IPR004294. Carotenoid_Oase. [Graphical view]
PANTHER	PTHR10543. Carotenoid_Oase. 1 hit.
Pfam	PF03055. RPE65. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCED2_ARATH

Accession

Primary (citable) accession number: O49505

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)