Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H2A2 (AL8A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase family 8 member A1

EC=1.2.1.-
Alternative name(s):
Aldehyde dehydrogenase 12
Gene names
Name:ALDH8A1
Synonyms:ALDH12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts 9-cis-retinal to 9-cis-retinoic acid. Has lower activity towards 13-cis-retinal. Has much lower activity towards all-trans-retinal. Has highest activity with benzaldehyde and decanal (in vitro). Has a preference for NAD, but shows considerable activity with NADP (in vitro). Ref.1

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in adult kidney and liver. Detected at lower levels in fetal liver and kidney. Ref.1

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=17.5 µM for benzaldehyde Ref.1

KM=3.15 µM for 9-cis-retinal

pH dependence:

Optimum pH is 9.

Sequence caution

The sequence AAI14474.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2A2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H2A2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     284-337: Missing.
Note: Lacks enzymatic activity.
Isoform 3 (identifier: Q9H2A2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     148-160: AGLISPWNLPLYL → VPGYTCRTCRFVT
     161-487: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Isoform 4 (identifier: Q9H2A2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     148-197: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Aldehyde dehydrogenase family 8 member A1
PRO_0000312954

Regions

Nucleotide binding209 – 2157NAD Potential

Sites

Active site2531Proton acceptor By similarity
Active site2871Nucleophile By similarity
Site1551Transition state stabilizer By similarity

Natural variations

Alternative sequence148 – 19750Missing in isoform 4.
VSP_043279
Alternative sequence148 – 16013AGLIS…LPLYL → VPGYTCRTCRFVT in isoform 3.
VSP_039759
Alternative sequence161 – 487327Missing in isoform 3.
VSP_039760
Alternative sequence284 – 33754Missing in isoform 2.
VSP_029972
Natural variant4021F → S.
Corresponds to variant rs2294315 [ dbSNP | Ensembl ].
VAR_037618

Experimental info

Sequence conflict2521L → P in BAD96568. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3CC09F6A7CCC269F

FASTA48753,401
        10         20         30         40         50         60 
MAGTNALLML ENFIDGKFLP CSSYIDSYDP STGEVYCRVP NSGKDEIEAA VKAAREAFPS 

        70         80         90        100        110        120 
WSSRSPQERS RVLNQVADLL EQSLEEFAQA ESKDQGKTLA LARTMDIPRS VQNFRFFASS 

       130        140        150        160        170        180 
SLHHTSECTQ MDHLGCMHYT VRAPVGVAGL ISPWNLPLYL LTWKIAPAMA AGNTVIAKPS 

       190        200        210        220        230        240 
ELTSVTAWML CKLLDKAGVP PGVVNIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIT 

       250        260        270        280        290        300 
QLSAPHCKKL SLELGGKNPA IIFEDANLDE CIPATVRSSF ANQGEICLCT SRIFVQKSIY 

       310        320        330        340        350        360 
SEFLKRFVEA TRKWKVGIPS DPLVSIGALI SKAHLEKVRS YVKRALAEGA QIWCGEGVDK 

       370        380        390        400        410        420 
LSLPARNQAG YFMLPTVITD IKDESCCMTE EIFGPVTCVV PFDSEEEVIE RANNVKYGLA 

       430        440        450        460        470        480 
ATVWSSNVGR VHRVAKKLQS GLVWTNCWLI RELNLPFGGM KSSGIGREGA KDSYDFFTEI 


KTITVKH 

« Hide

Isoform 2 [UniParc].

Checksum: 9777AFD28CE20C14
Show »

FASTA43347,325
Isoform 3 [UniParc].

Checksum: C94538B542A8ECAD
Show »

FASTA16017,809
Isoform 4 [UniParc].

Checksum: 9544E73B210BABD6
Show »

FASTA43748,036

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ortholog, ALDH12."
Lin M., Napoli J.L.
J. Biol. Chem. 275:40106-40112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Kidney and Liver.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Liver.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 3).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303134 mRNA. Translation: AAG42417.1.
AK290784 mRNA. Translation: BAF83473.1.
AK298325 mRNA. Translation: BAH12757.1.
AK222848 mRNA. Translation: BAD96568.1.
AL021939, AL445190 Genomic DNA. Translation: CAI20305.1.
AL021939, AL445190 Genomic DNA. Translation: CAI20306.1.
AL445190, AL021939 Genomic DNA. Translation: CAI95158.1.
AL445190, AL021939 Genomic DNA. Translation: CAI95159.1.
CH471051 Genomic DNA. Translation: EAW47985.1.
CH471051 Genomic DNA. Translation: EAW47986.1.
BC113862 mRNA. Translation: AAI13863.1.
BC114473 mRNA. Translation: AAI14474.1. Sequence problems.
CCDSCCDS5171.1. [Q9H2A2-1]
CCDS5172.1. [Q9H2A2-2]
CCDS55057.1. [Q9H2A2-4]
RefSeqNP_001180409.1. NM_001193480.1. [Q9H2A2-4]
NP_072090.1. NM_022568.3. [Q9H2A2-1]
NP_739577.1. NM_170771.2. [Q9H2A2-2]
UniGeneHs.486520.

3D structure databases

ProteinModelPortalQ9H2A2.
SMRQ9H2A2. Positions 12-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122204. 1 interaction.
STRING9606.ENSP00000265605.

PTM databases

PhosphoSiteQ9H2A2.

Polymorphism databases

DMDM74752601.

Proteomic databases

MaxQBQ9H2A2.
PaxDbQ9H2A2.
PRIDEQ9H2A2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265605; ENSP00000265605; ENSG00000118514. [Q9H2A2-1]
ENST00000349305; ENSP00000325473; ENSG00000118514. [Q9H2A2-3]
ENST00000367845; ENSP00000356819; ENSG00000118514. [Q9H2A2-2]
ENST00000367847; ENSP00000356821; ENSG00000118514. [Q9H2A2-4]
GeneID64577.
KEGGhsa:64577.
UCSCuc003qew.3. human. [Q9H2A2-1]
uc003qex.3. human. [Q9H2A2-2]
uc011ecx.2. human. [Q9H2A2-4]

Organism-specific databases

CTD64577.
GeneCardsGC06M135238.
HGNCHGNC:15471. ALDH8A1.
HPAHPA026292.
MIM606467. gene.
neXtProtNX_Q9H2A2.
PharmGKBPA24705.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidQ9H2A2.
OMAVKDESCC.
OrthoDBEOG7FV3Q2.
PhylomeDBQ9H2A2.
TreeFamTF314129.

Gene expression databases

ArrayExpressQ9H2A2.
BgeeQ9H2A2.
CleanExHS_ALDH8A1.
GenevestigatorQ9H2A2.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi64577.
NextBio66507.
PROQ9H2A2.
SOURCESearch...

Entry information

Entry nameAL8A1_HUMAN
AccessionPrimary (citable) accession number: Q9H2A2
Secondary accession number(s): B7Z521 expand/collapse secondary AC list , O60793, Q24JS9, Q53GT3, Q5TI80
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM