Reviewed, UniProtKB/Swiss-Prot Q949P1 (ABAH1_ARATH)

Names and origin

Protein names

Recommended name:
    Abscisic acid 8'-hydroxylase 1
      Short name=ABA 8'-hydroxylase 1
    EC=1.14.13.93
Alternative name(s):
    Cytochrome P450 707A1

Gene names

Name:	CYP707A1
Ordered Locus Names:	At4g19230
ORF Names:	T18B16.200

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	467 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the oxidative degradation of abscisic acid. Plays an important role in determining abscisic acid levels in dry seeds and in the control of postgermination growth. Ref.1 Ref.4 Ref.5
Catalytic activity	+-abscisate + NADPH + O2 = 8'-hydroxyabscisate + NADP+ + H2O.
Cofactor	Heme group By similarity.
Pathway	Plant hormone degradation; abscisic acid degradation.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Mainly expressed in flowers, siliques, roots and stems. Lower expression in rosette leaves and dry seeds. Expressed in vascular tissues of embryo during the seed development. Ref.1 Ref.4 Ref.5
Developmental stage	Expressed predominantly during mid-maturation of seed and down-regulated during late maturation. Up-regulated 12 hours after seed imbibition. Ref.4 Ref.5
Induction	By abscisic acid treatment, salt or osmotic stresses, and by dehydration and rehydration. Expression regulated by phytochrome B. Ref.1 Ref.4 Ref.6
Disruption phenotype	Plants show a reduced germination. Ref.5
Sequence similarities	Belongs to the cytochrome P450 family.
Sequence caution	The sequence CAA16713.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78925.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	abscisic acid metabolic process Ref.5 Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW release of seed from dormancy Inferred from mutant phenotype. Source: TAIR response to red or far red light Ref.6 Inferred from expression pattern. Source: TAIR response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	(+)-abscisic acid 8'-hydroxylase activity Ref.1 Inferred from direct assay. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q949P1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	Abscisic acid 8'-hydroxylase 1		PRO_0000288639
Regions
	Transmembrane	5 – 24	20	Potential
Sites
	Metal binding	411	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 2F4230446536D955	FASTA	467	53,037
	10 20 30 40 50 60 MDISALFLTL FAGSLFLYFL RCLISQRRFG SSKLPLPPGT MGWPYVGETF QLYSQDPNVF 70 80 90 100 110 120 FQSKQKRYGS VFKTHVLGCP CVMISSPEAA KFVLVTKSHL FKPTFPASKE RMLGKQAIFF 130 140 150 160 170 180 HQGDYHAKLR KLVLRAFMPE SIRNMVPDIE SIAQDSLRSW EGTMINTYQE MKTYTFNVAL 190 200 210 220 230 240 LSIFGKDEVL YREDLKRCYY ILEKGYNSMP VNLPGTLFHK SMKARKELSQ ILARILSERR 250 260 270 280 290 300 QNGSSHNDLL GSFMGDKEEL TDEQIADNII GVIFAARDTT ASVMSWILKY LAENPNVLEA 310 320 330 340 350 360 VTEEQMAIRK DKEEGESLTW GDTKKMPLTS RVIQETLRVA SILSFTFREA VEDVEYEGYL 370 380 390 400 410 420 IPKGWKVLPL FRNIHHSADI FSNPGKFDPS RFEVAPKPNT FMPFGNGTHS CPGNELAKLE 430 440 450 460 MSIMIHHLTT KYSWSIVGAS DGIQYGPFAL PQNGLPIVLA RKPEIEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid." Saito S., Hirai N., Matsumoto C., Ohigashi H., Ohta D., Sakata K., Mizutani M. Plant Physiol. 134:1439-1449(2004) [PubMed: 15064374] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[2]	"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.
[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]	"The Arabidopsis cytochrome P450 CYP707A encodes ABA 8'-hydroxylases: key enzymes in ABA catabolism." Kushiro T., Okamoto M., Nakabayashi K., Yamagishi K., Kitamura S., Asami T., Hirai N., Koshiba T., Kamiya Y., Nambara E. EMBO J. 23:1647-1656(2004) [PubMed: 15044947] [Abstract] Cited for: IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
[5]	"CYP707A1 and CYP707A2, which encode abscisic acid 8'-hydroxylases, are indispensable for proper control of seed dormancy and germination in Arabidopsis." Okamoto M., Kuwahara A., Seo M., Kushiro T., Asami T., Hirai N., Kamiya Y., Koshiba T., Nambara E. Plant Physiol. 141:97-107(2006) [PubMed: 16543410] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]	"Regulation of hormone metabolism in Arabidopsis seeds: phytochrome regulation of abscisic acid metabolism and abscisic acid regulation of gibberellin metabolism." Seo M., Hanada A., Kuwahara A., Endo A., Okamoto M., Yamauchi Y., North H., Marion-Poll A., Sun T.P., Koshiba T., Kamiya Y., Yamaguchi S., Nambara E. Plant J. 48:354-366(2006) [PubMed: 17010113] [Abstract] Cited for: INDUCTION BY PHYTOCHROME B.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB122149 mRNA. Translation: BAD16629.1. AL021687 Genomic DNA. Translation: CAA16713.1. Sequence problems. AL161550 Genomic DNA. Translation: CAB78925.1. Sequence problems. AY050980 mRNA. Translation: AAK93657.1. AY091446 mRNA. Translation: AAM14385.1.
IPI	IPI00519786.
PIR	T04444.
RefSeq	NP_567581.1.
UniGene	At.1930
3D structure databases
HSSP	HSSP built from PDB template 1CPT based on UniProtKB P33006.
ModBase	Search...
Protein-protein interaction databases
STRING	Q949P1.
Genome annotation databases
GeneID	827663.
GenomeReviews	Gene locus AT4G19230 in contig CT486007_GR.
KEGG	ath:AT4G19230.
NMPDR	fig|3702.1.peg.19741.
Organism-specific databases
GeneFarm	1251. 94.
TAIR	At4g19230.
Enzyme and pathway databases
BioCyc	MetaCyc:AT4G19230-MON.
BRENDA	1.14.13.93. 302.
Gene expression databases
Genevestigator	Q949P1.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ABAH1_ARATH

Accession

Primary (citable) accession number: Q949P1
Secondary accession number(s): O65624

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	December 1, 2001
Last modified:	October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)