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UniProtKB/Swiss-Prot entry Q0WSF1


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

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Entry information
Entry name AL221_ARATH
Primary accession number Q0WSF1
Secondary accession numbers Q70E95 Q9C837
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 20)
Name and origin of the protein
Protein name Aldehyde dehydrogenase 22A1 [Precursor]
Synonyms EC 1.2.1.3
Novel aldehyde dehydrogenase family 22 member A1
Gene name
Name: ALDH22A1
OrderedLocusNames: At3g66658
ORFNames: T8E24.4
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], TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1007/s11103-004-7796-6; PubMed=15830124 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
"Detailed expression analysis of selected genes of the aldehyde dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
Plant Mol. Biol. 57:315-322(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
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.
[4]
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
AJ584646; CAE48165.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC036106; AAG50992.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK227981; BAE99947.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_974242.1; -.
UniGene At.43176
3D structure databases
HSSP P11883; 1AD3. [HSSP ENTRY / PDB]
ModBase Q0WSF1.
Organism-specific databases
TAIR At3g66658; -.
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 Q0WSF1.
Genome annotation databases
GeneID 819849; -.
GenomeReviews BA000014_GR; AT3G66658.
NMPDR fig|3702.1.peg.12680; -.
Other
ProtoNet Q0WSF1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; NAD; Oxidoreductase; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    30  30     Potential. 
CHAIN   31   596  566     Aldehyde dehydrogenase 22A1. PRO_0000256069
NP_BIND   276   281  6     NAD (By similarity). 
ACT_SITE   298   298        Proton acceptor (By similarity). 
ACT_SITE   332   332        Nucleophile (By similarity). 
SITE   199   199  1     Transition state stabilizer (By similarity). 
CONFLICT   33    33        V -> A (in Ref. 3; BAE99947). 
Sequence information
Length: 596 AA [This is the length of the unprocessed precursor] Molecular weight: 66003 Da [This is the MW of the unprocessed precursor] CRC64: 25AC39BC26E4C1A8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPFWWPLIVL AFAYAICKFL LMLIPPNVPS IDVDASDVLA HGKDTEENSF IYIPPRGRSQ 

        70         80         90        100        110        120 
QSDKKVQCYE PATMKYLGYF PALSPTEVEE RVTLSRKAQK TWAQSSFKLR RQFLRILLKY 

       130        140        150        160        170        180 
IIEHQELICE VSSRDTGKTM VDASLGEIMT TCEKITWLLS EGERWLKPES RSSGRAMLHK 

       190        200        210        220        230        240 
VSRVEFHPLG VIGAIVPWNY PFHNIFNPML AAVFSGNGIV IKVSEHASWS GCFYFRIIQA 

       250        260        270        280        290        300 
ALAAVGAPEN LVDVITGFAE TGEALVSSVD KMIFVGSTAV GKMIMRNAAE TLTPVTLELG 

       310        320        330        340        350        360 
GKDAFIICED ADVSHVAQVA VRGTLQSSGQ NCAGAERFYV HKDIYTAFIG QVTKIVKSVS 

       370        380        390        400        410        420 
AGPPLTGRYD MGAICLQEHS EHLQSLVNDA LDKGAEIAVR GSFGHLGEDA VDQYFPPTVL 

       430        440        450        460        470        480 
INVNHNMKIM KEEAFGPIMP IMQFSTDEEV IKLANDSRYA LGCAVFSGSK HRAKQIASQI 

       490        500        510        520        530        540 
QCGVAAINDF ASNYMCQSLP FGGVKDSGFG RFAGIEGLRA CCLVKSVVED RFWPLIKTKI 

       550        560        570        580        590 
PKPIQYPVAE NAFEFQEALV ETLYGLNIWD RLRSLIDVLK FLTDQSSNVS RTRKSH 

Q0WSF1 in FASTA format

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