LOCUS NP_000373 485 aa linear PRI 22-OCT-2008
DEFINITION aldehyde dehydrogenase 3A2 isoform 2 [Homo sapiens].
ACCESSION NP_000373
VERSION NP_000373.1 GI:4557303
DBSOURCE REFSEQ: accession NM_000382.2
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 485)
AUTHORS Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
David,S.P., Niaura,R. and Lerman,C.
TITLE Molecular genetics of successful smoking cessation: convergent
genome-wide association study results
JOURNAL Arch. Gen. Psychiatry 65 (6), 683-693 (2008)
PUBMED 18519826
REMARK GeneRIF: Observational study and clinical trial of gene-disease
association, gene-environment interaction, and pharmacogenomic /
toxicogenomic. (HuGE Navigator)
REFERENCE 2 (residues 1 to 485)
AUTHORS Rizzo,W.B., Craft,D.A., Somer,T., Carney,G., Trafrova,J. and
Simon,M.
TITLE Abnormal fatty alcohol metabolism in cultured keratinocytes from
patients with Sjogren-Larsson syndrome
JOURNAL J. Lipid Res. 49 (2), 410-419 (2008)
PUBMED 17971613
REMARK GeneRIF: FALDH deficiency in keratinocytes from patients with
Sjogren-Larsson syndrome causes accumulation and diversion of fatty
alcohol into alternative biosynthetic pathways.
REFERENCE 3 (residues 1 to 485)
AUTHORS Jean-Francois,E., Low,J.Y., Gonzales,C.R. and Sarraf,D.
TITLE Sjogren-larsson syndrome and crystalline maculopathy associated
with a novel mutation
JOURNAL Arch. Ophthalmol. 125 (11), 1582-1583 (2007)
PUBMED 17998529
REMARK GeneRIF: Mutational analysis identified compound heterozygous
mutations in each allele of fatty aldehyde dehydrogenase gene,
confirming Sjogren-Larsson syndrome.
REFERENCE 4 (residues 1 to 485)
AUTHORS Lloyd,M.D., Boardman,K.D., Smith,A., van den Brink,D.M.,
Wanders,R.J. and Threadgill,M.D.
TITLE Characterisation of recombinant human fatty aldehyde dehydrogenase:
implications for Sjogren-Larsson syndrome
JOURNAL J Enzyme Inhib Med Chem 22 (5), 584-590 (2007)
PUBMED 18035827
REMARK GeneRIF: A structural model of FALDH has been constructed, and
catalytically important residues have been proposed to be involved
in alcohol and aldehyde oxidation: Gln-120, Glu-207, Cys-241,
Phe-333, Tyr-410 and His-411.
REFERENCE 5 (residues 1 to 485)
AUTHORS Didona,B., Codispoti,A., Bertini,E., Rizzo,W.B., Carney,G.,
Zambruno,G., Dionisi-Vici,C., Paradisi,M., Pedicelli,C., Melino,G.
and Terrinoni,A.
TITLE Novel and recurrent ALDH3A2 mutations in Italian patients with
Sjogren-Larsson syndrome
JOURNAL J. Hum. Genet. 52 (10), 865-870 (2007)
PUBMED 17902024
REMARK GeneRIF: These results add to understanding of the genetic basis of
Sjogren-Larsson syndrome.
REFERENCE 6 (residues 1 to 485)
AUTHORS Chang,C. and Yoshida,A.
TITLE Human fatty aldehyde dehydrogenase gene (ALDH10): organization and
tissue-dependent expression
JOURNAL Genomics 40 (1), 80-85 (1997)
PUBMED 9070922
REFERENCE 7 (residues 1 to 485)
AUTHORS Rogers,G.R., Markova,N.G., De Laurenzi,V., Rizzo,W.B. and
Compton,J.G.
TITLE Genomic organization and expression of the human fatty aldehyde
dehydrogenase gene (FALDH)
JOURNAL Genomics 39 (2), 127-135 (1997)
PUBMED 9027499
REFERENCE 8 (residues 1 to 485)
AUTHORS De Laurenzi,V., Rogers,G.R., Hamrock,D.J., Marekov,L.N.,
Steinert,P.M., Compton,J.G., Markova,N. and Rizzo,W.B.
TITLE Sjogren-Larsson syndrome is caused by mutations in the fatty
aldehyde dehydrogenase gene
JOURNAL Nat. Genet. 12 (1), 52-57 (1996)
PUBMED 8528251
REFERENCE 9 (residues 1 to 485)
AUTHORS Rogers,G.R., Rizzo,W.B., Zlotogorski,A., Hashem,N., Lee,M.,
Compton,J.G. and Bale,S.J.
TITLE Genetic homogeneity in Sjogren-Larsson syndrome: linkage to
chromosome 17p in families of different non-Swedish ethnic origins
JOURNAL Am. J. Hum. Genet. 57 (5), 1123-1129 (1995)
PUBMED 7485163
REFERENCE 10 (residues 1 to 485)
AUTHORS Pigg,M., Jagell,S., Sillen,A., Weissenbach,J., Gustavson,K.H. and
Wadelius,C.
TITLE The Sjogren-Larsson syndrome gene is close to D17S805 as determined
by linkage analysis and allelic association
JOURNAL Nat. Genet. 8 (4), 361-364 (1994)
PUBMED 7894487
REMARK Erratum:[Nat Genet 1995 Apr;9(4):451]
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from U46689.1, L47162.1, BC002430.2
and AK123877.1.
Summary: Aldehyde dehydrogenase isozymes are thought to play a
major role in the detoxification of aldehydes generated by alcohol
metabolism and lipid peroxidation. This gene product catalyzes the
oxidation of long-chain aliphatic aldehydes to fatty acid.
Mutations in the gene cause Sjogren-Larsson syndrome. Alternatively
spliced transcript variants encoding different isoforms have been
found for this gene. [provided by RefSeq].
Transcript Variant: This variant (2) lacks an alternate segment in
the 3' coding region compared to variant 1. Isoform 2 has a shorter
and different C-terminus, compared to isoform 1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..485
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="17"
/map="17p11.2"
Protein 1..485
/product="aldehyde dehydrogenase 3A2 isoform 2"
/EC_number="1.2.1.3"
/note="aldehyde dehydrogenase 10; fatty aldehyde
dehydrogenase"
/calculated_mol_wt=54717
CDS 1..485
/gene="ALDH3A2"
/gene_synonym="SLS"
/gene_synonym="FALDH"
/gene_synonym="ALDH10"
/gene_synonym="FLJ20851"
/gene_synonym="DKFZp686E23276"
/coded_by="NM_000382.2:222..1679"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="CCDS:CCDS11210.1"
/db_xref="GeneID:224"
/db_xref="HGNC:403"
/db_xref="HPRD:07188"
/db_xref="MIM:609523"
ORIGIN
1 melevrrvrq aflsgrsrpl rfrlqqleal rrmvqerekd iltaiaadlc ksefnvysqe
61 vitvlgeidf mlenlpewvt akpvkknvlt mldeayiqpq plgvvliiga wnypfvltiq
121 pligaiaagn aviikpsels entakilakl lpqyldqdly ivinggveet tellkqrfdh
181 ifytgntavg kivmeaaakh ltpvtlelgg kspcyidkdc dldivcrrit wgkymncgqt
241 ciapdyilce aslqnqivwk iketvkefyg enikespdye riinlrhfkr ilsllegqki
301 afggetdeat ryiaptvltd vdpktkvmqe eifgpilpiv pvknvdeain finerekpla
361 lyvfshnhkl ikrmidetss ggvtgndvim hftlnsfpfg gvgssgmgay hgkhsfdtfs
421 hqrpcllksl kreganklry ppnsqskvdw gkffllkrfn keklgllllt flgivaavlv
481 kaeyy
//