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UniProtKB/Swiss-Prot entry O81077


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ABAH2_ARATH
Primary accession number O81077
Secondary accession numbers None
Integrated into Swiss-Prot on May 29, 2007
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 56)
Name and origin of the protein
Protein name Abscisic acid 8'-hydroxylase 2
Synonyms ABA 8'-hydroxylase 2
EC 1.14.13.93
Cytochrome P450 707A2
Gene name
Name: CYP707A2
OrderedLocusNames: At2g29090
ORFNames: T9I4.17
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[3]
IDENTIFICATION, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
DOI=10.1038/sj.emboj.7600121; PubMed=15044947 [NCBI, ExPASy, EBI, Israel, Japan]
Kushiro T., Okamoto M., Nakabayashi K., Yamagishi K., Kitamura S., Asami T., Hirai N., Koshiba T., Kamiya Y., Nambara E.;
"The Arabidopsis cytochrome P450 CYP707A encodes ABA 8'-hydroxylases: key enzymes in ABA catabolism.";
EMBO J. 23:1647-1656(2004).
[4]
FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.106.079475; PubMed=16543410 [NCBI, ExPASy, EBI, Israel, Japan]
Okamoto M., Kuwahara A., Seo M., Kushiro T., Asami T., Hirai N., Kamiya Y., Koshiba T., Nambara E.;
"CYP707A1 and CYP707A2, which encode abscisic acid 8'-hydroxylases, are indispensable for proper control of seed dormancy and germination in Arabidopsis.";
Plant Physiol. 141:97-107(2006).
[5]
INDUCTION BY PHYTOCHROME B.
DOI=10.1111/j.1365-313X.2006.02881.x; PubMed=17010113 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Regulation of hormone metabolism in Arabidopsis seeds: phytochrome regulation of abscisic acid metabolism and abscisic acid regulation of gibberellin metabolism.";
Plant J. 48:354-366(2006).
Comments
  • FUNCTION: Involved in the oxidative degradation of abscisic acid, but not in the isomerization of the produced 8'-hydroxyabscisic acid (8'-OH-ABA) to (-)-phaseic acid (PA). Involved in the control of seed dormancy and germination.
  • 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 dry seeds. Lower expression in rosette leaves, flowers, siliques and stems. Not expressed in roots. Expressed in both endosperm and vascular tissues of embryo during the seed development and in cortex and endodermis in germinating embryo.
  • DEVELOPMENTAL STAGE: Up-regulated from late-maturation to mature dry seed. Up-regulated immediately after seed imbibition, reaching a maximum at 6 hours and decreasing therafter.
  • INDUCTION: By abscisic acid, dehydration and rehydration. Expression regulated by phytochrome B.
  • MISCELLANEOUS: Loss-of-function mutants cyp707a2-1 and cyp707a2-2 (T-DNA insertion) show a hyperdormancy phenotype.
  • SIMILARITY: Belongs to the cytochrome P450 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC005315; AAC33235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK230466; BAF02260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T02739; T02739.
RefSeq NP_180473.1; -.
UniGene At.50108
3D structure databases
ModBase O81077.
Enzyme and pathway databases
BioCyc MetaCyc:AT2G29090-MON; -.
Organism-specific databases
GeneFarm 1252; 94.
TAIR At2g29090; -.
Gene expression databases
ArrayExpress O81077; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0010295; Molecular function: (+)-abscisic acid 8'-hydroxylase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009687; Biological process: abscisic acid metabolic process (inferred from mutant phenotype from TAIR).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0048838; Biological process: release of seed from dormancy (inferred from mutant phenotype from TAIR).
GO:0010114; Biological process: response to red light (inferred from expression pattern from TAIR).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00463; EP450I.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
Genome annotation databases
GeneID 817457; -.
GenomeReviews CT485783_GR; AT2G29090.
KEGG ath:AT2G29090; -.
NMPDR fig|3702.1.peg.9956; -.
Other
ProtoNet O81077.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Stress response; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   482  482     Abscisic acid 8'-hydroxylase 2. PRO_0000288640
TRANSMEM   20    40  21     Potential. 
COMPBIAS   4     9  6     Poly-Ser. 
METAL   431   431        Iron (heme axial ligand) (By similarity). 
Sequence information
Length: 482 AA [This is the length of the unprocessed precursor] Molecular weight: 55176 Da [This is the MW of the unprocessed precursor] CRC64: AB6A07AB2778DD3B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQISSSSSSN FFSSLYADEP ALITLTIVVV VVVLLFKWWL HWKEQRLRLP PGSMGLPYIG 

        70         80         90        100        110        120 
ETLRLYTENP NSFFATRQNK YGDIFKTHIL GCPCVMISSP EAARMVLVSK AHLFKPTYPP 

       130        140        150        160        170        180 
SKERMIGPEA LFFHQGPYHS TLKRLVQSSF MPSALRPTVS HIELLVLQTL SSWTSQKSIN 

       190        200        210        220        230        240 
TLEYMKRYAF DVAIMSAFGD KEEPTTIDVI KLLYQRLERG YNSMPLDLPG TLFHKSMKAR 

       250        260        270        280        290        300 
IELSEELRKV IEKRRENGRE EGGLLGVLLG AKDQKRNGLS DSQIADNIIG VIFAATDTTA 

       310        320        330        340        350        360 
SVLTWLLKYL HDHPNLLQEV SREQFSIRQK IKKENRRISW EDTRKMPLTT RVIQETLRAA 

       370        380        390        400        410        420 
SVLSFTFREA VQDVEYDGYL IPKGWKVLPL FRRIHHSSEF FPDPEKFDPS RFEVAPKPYT 

       430        440        450        460        470        480 
YMPFGNGVHS CPGSELAKLE MLILLHHLTT SFRWEVIGDE EGIQYGPFPV PKKGLPIRVT 


PI 

O81077 in FASTA format

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