[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND VARIANTS SLS. DOI=10.1038/ng0196-52; PubMed=8528251 [NCBI, ExPASy, EBI, Israel, Japan] de Laurenzi V., Rogers G.R., Hamrock D.J., Marekov L.N., Steinert P.M., Compton J.G., Markova N., Rizzo W.B.; "Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene."; Nat. Genet. 12:52-57(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2). DOI=10.1006/geno.1996.4501; PubMed=9027499 [NCBI, ExPASy, EBI, Israel, Japan] Rogers G.R., Markova N.G., De Laurenzi V., Rizzo W.B., Compton J.G.; "Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH)."; Genomics 39:127-135(1997).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; DOI=10.1006/geno.1996.4547; PubMed=9070922 [NCBI, ExPASy, EBI, Israel, Japan] Chang C., Yoshida A.; "Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression."; Genomics 40:80-85(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	VARIANT SLS SER-315. DOI=10.1007/s004390050490; PubMed=9254849 [NCBI, ExPASy, EBI, Israel, Japan] Sillen A., Jagell S., Wadelius C.; "A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden."; Hum. Genet. 100:201-203(1997).
[6]	VARIANTS SLS ARG-106; TRP-226; ASN-245; SER-315; LEU-365 AND ARG-412. DOI=10.1002/(SICI)1098-1004(1998)12:6<377::AID-HUMU3>3.0.CO;2-I; PubMed=9829906 [NCBI, ExPASy, EBI, Israel, Japan] Sillen A., Anton-Lamprecht I., Braun-Quentin C., Kraus C.S., Sayli B.S., Ayuso C., Jagell S., Kuester W., Wadelius C.; "Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome."; Hum. Mutat. 12:377-384(1998).
[7]	VARIANTS SLS PHE-45; ASP-64; ARG-106; LEU-114; LEU-121; ARG-184; MET-184; ALA-185; CYS-228; TYR-237; ASN-245; ASN-266; ASN-279; SER-315; ILE-328; LEU-365; ARG-406; TYR-411; ASN-415; SER-419; HIS-423 AND GLU-447. DOI=10.1086/302681; PubMed=10577908 [NCBI, ExPASy, EBI, Israel, Japan] Rizzo W.B., Carney G., Lin Z.; "The molecular basis of Sjoegren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene."; Am. J. Hum. Genet. 65:1547-1560(1999).
[8]	VARIANT SLS SER-386. DOI=10.1046/j.1523-1747.2000.00960-5.x; PubMed=10792573 [NCBI, ExPASy, EBI, Israel, Japan] Aoki N., Suzuki H., Ito K., Ito M.; "A novel point mutation of the FALDH gene in a Japanese family with Sjoegren-Larsson syndrome."; J. Invest. Dermatol. 114:1065-1066(2000).

Comments

FUNCTION: Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length.
CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID P51648-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID P51648-2

Features which should be applied to build the isoform sequence: VSP_001283.
DISEASE: Defects in ALDH3A2 are the cause of Sjoegren-Larsson syndrome (SLS) [MIM:270200]. SLS is an autosomal recessive neurocutaneous disorder characterized by a combination of severe mental retardation, spastic di- or tetraplegia and congenital ichthyosis (increased keratinization). Ichthyosis is usually evident at birth, neurologic symptoms appear in the first or second year of life. Most patients have an IQ of less than 60. Additional clinical features include glistening white spots on the retina, seizures, short stature and speech defects.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ALDH3A2";.

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

L47162; AAB01003.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75296; AAC50966.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75286; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75287; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75288; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75289; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75290; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75291; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75292; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75293; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75294; AAC50966.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75295; AAC50965.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75286; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75287; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75288; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75289; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75290; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75291; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75292; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75293; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U75294; AAC50965.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U46689; AAC51121.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002430; AAH02430.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_000373.1; -.
NP_001026976.1; -.

UniGene

Hs.499886

3D structure databases

HSSP

P11883; 1AD3. [HSSP ENTRY / PDB]

ModBase

P51648.

Protein-protein interaction databases

IntAct

P51648; -.

Organism-specific databases

H-InvDB

HIX0009873; -.
HIX0013620; -.

HGNC:403; ALDH3A2.

HPA014769; -.

270200; phenotype. [NCBI / EBI]
609523; gene. [NCBI / EBI]

Orphanet

816; Sjoegren-Larsson syndrome.

PharmGKB

PA24698; -.

GeneCards

P51648.

Gene expression databases

ArrayExpress

P51648; -.

CleanEx

HS_ALDH3A2; -.

GermOnline

ENSG00000072210; Homo sapiens.

Ontologies

GO:0004028;	Molecular function: 3-chloroallyl aldehyde dehydrogenase activity (traceable author statement from ProtInc).
GO:0007417;	Biological process: central nervous system development (traceable author statement from ProtInc).
GO:0008544;	Biological process: epidermis development (traceable author statement from ProtInc).
GO:0006629;	Biological process: lipid metabolic process (traceable author statement from ProtInc).
GO:0007422;	Biological process: peripheral nervous system development (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR012394; Ald_DHase_NAD(P).
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF15; ALDH; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036492; ALDH; 1.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

P51648.

Genome annotation databases

Ensembl

ENSG00000072210; Homo sapiens. [Contig view]

GeneID

224; -.

KEGG

hsa:224; -.

Phylogenomic databases

HOVERGEN

P51648; -.

Other

DrugBank

DB00157; NADH.

SOURCE

ALDH3A2; Homo sapiens.

ProtoNet

P51648.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Ichthyosis; Membrane; Mental retardation; NAD; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 485`	`485`	`Fatty aldehyde dehydrogenase.`	`PRO_0000056473`
`TOPO_DOM`	`1 463`	`463`	`Cytoplasmic.`
`TRANSMEM`	`464 480`	`17`	`Potential.`
`NP_BIND`	`185 190`	`6`	`NAD (Potential).`
`ACT_SITE`	`207 207`		`By similarity.`
`ACT_SITE`	`241 241`		`By similarity.`
`VAR_SEQ`	`482 485`		`AEYY -> KYQAVLRRKALLIFLVVHRLRWSSKQR (in isoform 2).`	`VSP_001283`
`VARIANT`	`45 45`	`1`	`I -> F (in SLS; severe loss of activity).`	`VAR_017510`
`VARIANT`	`64 64`	`1`	`V -> D (in SLS; severe loss of activity).`	`VAR_017511`
`VARIANT`	`106 106`	`1`	`L -> R (in SLS; severe loss of activity).`	`VAR_002249`
`VARIANT`	`114 114`	`1`	`P -> L (in SLS; severe loss of activity).`	`VAR_017512`
`VARIANT`	`121 121`	`1`	`P -> L (in SLS; severe loss of activity).`	`VAR_017513`
`VARIANT`	`184 184`	`1`	`T -> M (in SLS; severe loss of activity).`	`VAR_017514`
`VARIANT`	`184 184`	`1`	`T -> R (in SLS; severe loss of activity).`	`VAR_017515`
`VARIANT`	`185 185`	`1`	`G -> A (in SLS; severe loss of activity).`	`VAR_017516`
`VARIANT`	`214 214`	`1`	`C -> Y (in SLS; 4% of activity).`	`VAR_002250`
`VARIANT`	`226 226`	`1`	`C -> W (in SLS).`	`VAR_002251`
`VARIANT`	`228 228`	`1`	`R -> C (in SLS; severe loss of activity).`	`VAR_017517`
`VARIANT`	`237 237`	`1`	`C -> Y (in SLS; severe loss of activity).`	`VAR_017518`
`VARIANT`	`245 245`	`1`	`D -> N (in SLS; severe loss of activity; originally thought to be a neutral polymorphism).`	`VAR_002252`
`VARIANT`	`266 266`	`1`	`K -> N (in SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability).`	`VAR_017519`
`VARIANT`	`279 279`	`1`	`Y -> N (in SLS; severe loss of activity).`	`VAR_017520`
`VARIANT`	`314 315`	`2`	`AP -> GAKSTVGA (in SLS; 8% of activity).`	`VAR_002253`
`VARIANT`	`315 315`	`1`	`P -> S (in SLS; common mutation in Europeans; severe loss of enzymatic activity).`	`VAR_002254`
`VARIANT`	`328 328`	`1`	`M -> I (in SLS).`	`VAR_017521`
`VARIANT`	`365 365`	`1`	`S -> L (in SLS; severe loss of activity).`	`VAR_002255`
`VARIANT`	`386 386`	`1`	`N -> S (in SLS).`	`VAR_017522`
`VARIANT`	`406 406`	`1`	`G -> R (in SLS).`	`VAR_017523`
`VARIANT`	`411 411`	`1`	`H -> Y (in SLS; severe loss of activity).`	`VAR_017524`
`VARIANT`	`412 412`	`1`	`G -> R (in SLS).`	`VAR_002256`
`VARIANT`	`415 415`	`1`	`S -> N (in SLS; severe loss of activity).`	`VAR_017525`
`VARIANT`	`419 419`	`1`	`F -> S (in SLS; severe loss of activity).`	`VAR_017526`
`VARIANT`	`423 423`	`1`	`R -> H (in SLS; severe loss of activity).`	`VAR_017527`
`VARIANT`	`447 447`	`1`	`K -> E (in SLS; severe loss of activity).`	`VAR_017528`

Sequence information

Length: 485 AA [This is the length of the unprocessed precursor]

Molecular weight: 54848 Da [This is the MW of the unprocessed precursor]

CRC64: 209601CB5803C7E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MELEVRRVRQ AFLSGRSRPL RFRLQQLEAL RRMVQEREKD ILTAIAADLC KSEFNVYSQE 

        70         80         90        100        110        120 
VITVLGEIDF MLENLPEWVT AKPVKKNVLT MLDEAYIQPQ PLGVVLIIGA WNYPFVLTIQ 

       130        140        150        160        170        180 
PLIGAIAAGN AVIIKPSELS ENTAKILAKL LPQYLDQDLY IVINGGVEET TELLKQRFDH 

       190        200        210        220        230        240 
IFYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDKDC DLDIVCRRIT WGKYMNCGQT 

       250        260        270        280        290        300 
CIAPDYILCE ASLQNQIVWK IKETVKEFYG ENIKESPDYE RIINLRHFKR ILSLLEGQKI 

       310        320        330        340        350        360 
AFGGETDEAT RYIAPTVLTD VDPKTKVMQE EIFGPILPIV PVKNVDEAIN FINEREKPLA 

       370        380        390        400        410        420 
LYVFSHNHKL IKRMIDETSS GGVTGNDVIM HFTLNSFPFG GVGSSGMGAY HGKHSFDTFS 

       430        440        450        460        470        480 
HQRPCLLKSL KREGANKLRY PPNSQSKVDW GKFFLLKRFN KEKLGLLLLT FLGIVAAVLV 


KAEYY

P51648 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools