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UniProtKB/Swiss-Prot entry Q56YU0


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

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Entry information
Entry name AL2C4_ARATH
Primary accession number Q56YU0
Secondary accession number Q9LV57
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 31, 2006 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 21)
Name and origin of the protein
Protein name Aldehyde dehydrogenase family 2 member C4
Synonyms EC 1.2.1.3
ALDH1a
Protein REDUCED EPIDERMAL FLUORESCENCE 1
Gene name
Name: ALDH2C4
Synonyms: REF1
OrderedLocusNames: At3g24503
ORFNames: MOB24.3
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
DOI=10.1023/A:1014870429630; PubMed=11999848 [NCBI, ExPASy, EBI, Israel, Japan]
Skibbe D.S., Liu F., Wen T.-J., Yandeau M.D., Cui X., Cao J., Simmons C.R., Schnable P.S.;
"Characterization of the aldehyde dehydrogenase gene families of Zea mays and Arabidopsis.";
Plant Mol. Biol. 48:751-764(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/7.3.217; PubMed=10907853 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones.";
DNA Res. 7:217-221(2000).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-501.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND MUTAGENESIS OF GLY-152 AND GLY-416.
DOI=10.1105/tpc.017509; PubMed=14729911 [NCBI, ExPASy, EBI, Israel, Japan]
Nair R.B., Bastress K.L., Ruegger M.O., Denault J.W., Chapple C.;
"The Arabidopsis thaliana REDUCED EPIDERMAL FLUORESCENCE1 gene encodes an aldehyde dehydrogenase involved in ferulic acid and sinapic acid biosynthesis.";
Plant Cell 16:544-554(2004).
[6]
NOMENCLATURE.
DOI=10.1016/j.tplants.2004.06.004; PubMed=15358267 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
"The ALDH gene superfamily of Arabidopsis.";
Trends Plant Sci. 9:371-377(2004).
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
AF349448; AAM27004.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020746; BAB01998.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056398; AAL08254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK221230; BAD93825.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_566749.1; -.
UniGene At.22894
3D structure databases
HSSP P05091; 1O04. [HSSP ENTRY / PDB]
ModBase Q56YU0.
Organism-specific databases
TAIR At3g24503; -.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS Q56YU0.
Proteomic databases
ProMEX Q56YU0; -.
Genome annotation databases
GeneID 822042; -.
GenomeReviews BA000014_GR; AT3G24503.
KEGG ath:AT3G24503; -.
NMPDR fig|3702.1.peg.14712; -.
Other
ProtoNet Q56YU0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   501  501     Aldehyde dehydrogenase family 2 member C4. PRO_0000256058
NP_BIND   245   250  6     NAD (By similarity). 
ACT_SITE   268   268        Proton acceptor (By similarity). 
ACT_SITE   302   302        Nucleophile (By similarity). 
SITE   169   169  1     Transition state stabilizer (By similarity). 
MUTAGEN   152   152        G->E: In ref1-7; reduced activity on sinapaldehyde. 
MUTAGEN   416   416        G->R: In ref1-6; reduced activity on sinapaldehyde. 
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 54360 Da [This is the MW of the unprocessed precursor] CRC64: 3E93A166B1D3ECF6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MENGKCNGAT TVKLPEIKFT KLFINGQFID AASGKTFETI DPRNGEVIAT IAEGDKEDVD 

        70         80         90        100        110        120 
LAVNAARYAF DHGPWPRMTG FERAKLINKF ADLIEENIEE LAKLDAVDGG KLFQLGKYAD 

       130        140        150        160        170        180 
IPATAGHFRY NAGAADKIHG ETLKMTRQSL FGYTLKEPIG VVGNIIPWNF PSIMFATKVA 

       190        200        210        220        230        240 
PAMAAGCTMV VKPAEQTSLS ALFYAHLSKE AGIPDGVLNI VTGFGSTAGA AIASHMDVDK 

       250        260        270        280        290        300 
VSFTGSTDVG RKIMQAAAAS NLKKVSLELG GKSPLLIFND ADIDKAADLA LLGCFYNKGE 

       310        320        330        340        350        360 
ICVASSRVFV QEGIYDKVVE KLVEKAKDWT VGDPFDSTAR QGPQVDKRQF EKILSYIEHG 

       370        380        390        400        410        420 
KNEGATLLTG GKAIGDKGYF IQPTIFADVT EDMKIYQDEI FGPVMSLMKF KTVEEGIKCA 

       430        440        450        460        470        480 
NNTKYGLAAG ILSQDIDLIN TVSRSIKAGI IWVNCYFGFD LDCPYGGYKM SGNCRESGMD 

       490        500 
ALDNYLQTKS VVMPLHNSPW M 

Q56YU0 in FASTA format

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