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UniProtKB/Swiss-Prot entry Q949P1


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

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Entry information
Entry name ABAH1_ARATH
Primary accession number Q949P1
Secondary accession number O65624
Integrated into Swiss-Prot on May 29, 2007
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 51)
Name and origin of the protein
Protein name Abscisic acid 8'-hydroxylase 1
Synonyms ABA 8'-hydroxylase 1
EC 1.14.13.93
Cytochrome P450 707A1
Gene name
Name: CYP707A1
OrderedLocusNames: At4g19230
ORFNames: T18B16.200
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1104/pp.103.037614; PubMed=15064374 [NCBI, ExPASy, EBI, Israel, Japan]
Saito S., Hirai N., Matsumoto C., Ohigashi H., Ohta D., Sakata K., Mizutani M.;
"Arabidopsis CYP707As encode (+)-abscisic acid 8'-hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid.";
Plant Physiol. 134:1439-1449(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
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).
[5]
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).
[6]
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
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
AB122149; BAD16629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL021687; CAA16713.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161550; CAB78925.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY050980; AAK93657.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY091446; AAM14385.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04444; T04444.
RefSeq NP_567581.1; -.
UniGene At.1930
3D structure databases
HSSP P33006; 1CPT. [HSSP ENTRY / PDB]
ModBase Q949P1.
Enzyme and pathway databases
BioCyc MetaCyc:AT4G19230-MON; -.
Organism-specific databases
GeneFarm 1251; 94.
TAIR At4g19230; -.
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.
BLOCKS Q949P1.
Genome annotation databases
GeneID 827663; -.
GenomeReviews CT486007_GR; AT4G19230.
KEGG ath:AT4G19230; -.
NMPDR fig|3702.1.peg.19741; -.
Other
ProtoNet Q949P1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; 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   467  467     Abscisic acid 8'-hydroxylase 1. PRO_0000288639
TRANSMEM   5    24  20     Potential. 
METAL   411   411        Iron (heme axial ligand) (By similarity). 
Sequence information
Length: 467 AA [This is the length of the unprocessed precursor] Molecular weight: 53037 Da [This is the MW of the unprocessed precursor] CRC64: 2F4230446536D955 [This is a checksum on the sequence]
        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 

Q949P1 in FASTA format

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