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P47740 (AL3A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty aldehyde dehydrogenase
EC=1.2.1.3
Alternative name(s):
Aldehyde dehydrogenase 3
Aldehyde dehydrogenase family 3 member A2
Gene names
Name:Aldh3a2
Synonyms:Ahd-3, Ahd3, Aldh3, Aldh4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid By similarity.

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular aldehyde metabolic process

Inferred from electronic annotation. Source: InterPro

central nervous system development

Inferred from electronic annotation. Source: Compara

epidermis development

Inferred from electronic annotation. Source: Compara

peripheral nervous system development

Inferred from electronic annotation. Source: Compara

phytol metabolic process

Inferred from electronic annotation. Source: Compara

sesquiterpenoid metabolic process

Inferred from electronic annotation. Source: Compara

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 17510064. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

peroxisome

Inferred from electronic annotation. Source: Compara

   Molecular_functionaldehyde dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: InterPro

long-chain-alcohol oxidase activity

Inferred from electronic annotation. Source: Compara

long-chain-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: Compara

medium-chain-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Fatty aldehyde dehydrogenase
PRO_0000056475

Regions

Topological domain1 – 463463Cytoplasmic
Transmembrane464 – 48017Helical; Potential
Nucleotide binding185 – 1906NAD Potential
Motif481 – 4844Prevents secretion from ER By similarity

Sites

Active site2071 By similarity
Active site2411 By similarity

Experimental info

Sequence conflict191P → L in AAB06232. Ref.1
Sequence conflict2291I → V in AAB06232. Ref.1
Sequence conflict4181T → A in AAB06232. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47740 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: DFC67C96C757832A

FASTA48453,971
        10         20         30         40         50         60 
MERQVLRLRQ AFRSGRSRPL RFRLQQLEAL RRMVQEREKE ILAAIAADLS KSELNAYSHE 

        70         80         90        100        110        120 
VITILGEIDF MLGNLPELAS ARPAKKNLLT MMDEAYVQPE PLGVVLIIGA WNYPFVLTMQ 

       130        140        150        160        170        180 
PLVGAIAAGN AAIVKPSELS ENTAKILAEL LPQYLDQDLY AIVNGGIPET TELLKQRFDH 

       190        200        210        220        230        240 
ILYTGNTAVG KIVMEAAAKH LTPVTLELGG KSPCYIDRDC DLDVACRRIA WGKYMNCGQT 

       250        260        270        280        290        300 
CIAPDYILCE ASLQNQIVQK IKETVKDFYG ENIKASPDYE RIINLRHFKR LQSLLKGQKI 

       310        320        330        340        350        360 
AFGGEMDEAT RYLAPTILTD VDPNSKVMQE EIFGPILPIV SVKNVDEAIN FINDREKPLA 

       370        380        390        400        410        420 
LYVFSRNNKL IKRVIDETSS GGVTGNDVIM HFTVNSLPFG GVGASGMGAY HGKYSFDTFS 

       430        440        450        460        470        480 
HQRPCLLKGL KGESVNKLRY PPNSESKVSW AKFFLLKQFN KGRLGMLLFV CLVAVAAVIV 


KDQL

« Hide

References

« Hide 'large scale' references
[1]"Mouse microsomal class 3 aldehyde dehydrogenase: AHD3 cDNA sequence, inducibility by dioxin and clofibrate, and genetic mapping."
Vasiliou V., Kozak C.A., Lindahl R., Nebert D.W.
DNA Cell Biol. 15:235-245(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head, Spinal cord, Stomach and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U14390 mRNA. Translation: AAB06232.1.
AK079639 mRNA. Translation: BAC37712.1.
AK140932 mRNA. Translation: BAE24523.1.
AK159246 mRNA. Translation: BAE34928.1.
AK163040 mRNA. Translation: BAE37166.1.
AK169157 mRNA. Translation: BAE40936.1.
AK170195 mRNA. Translation: BAE41628.1.
AL672172 Genomic DNA. Translation: CAI24063.1.
BC003797 mRNA. Translation: AAH03797.1.
IPIIPI00874350.
RefSeqNP_031463.2. NM_007437.4.
UniGeneMm.398221.

3D structure databases

ProteinModelPortalP47740.
SMRP47740. Positions 1-443.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000067767.

PTM databases

PhosphoSiteP47740.

Proteomic databases

PaxDbP47740.
PRIDEP47740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074127; ENSMUSP00000073764; ENSMUSG00000010025.
GeneID11671.
KEGGmmu:11671.

Organism-specific databases

CTD224.
MGIMGI:1353452. Aldh3a2.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00390000002825.
HOGENOMHOG000271515.
HOVERGENHBG050483.
KOK00128.

Gene expression databases

ArrayExpressP47740.
BgeeP47740.
CleanExMM_ALDH3A2.
GenevestigatorP47740.
GermOnlineENSMUSG00000010025. Mus musculus.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PANTHERPTHR11699:SF15. PTHR11699:SF15. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036492. ALDH. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH3A2. mouse.
NextBio279299.
SOURCESearch...

Entry information

Entry nameAL3A2_MOUSE
AccessionPrimary (citable) accession number: P47740
Secondary accession number(s): Q99L64
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents