Seroatlas · Human Serome Atlas

ALDH8A1

2-aminomuconic semialdehyde dehydrogenase

Also known as: AL8A1_HUMAN, ALDH12

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession: Q9H2A2
Gene: ALDH8A1
Ensembl: ENSG00000118514
Chromosome: 6
Canonical length: 487 aa
Protein class: Enzymes, Metabolic proteins, Predicted intracellular proteins
Subcellular location: Nucleoplasm,Centrosome

OverviewNCBI Gene

This gene encodes a member of the aldehyde dehydrogenase family of proteins. The encoded protein has been implicated in the synthesis of 9-cis-retinoic acid and in the breakdown of the amino acid tryptophan. This enzyme converts 9-cis-retinal into the retinoid X receptor ligand 9-cis-retinoic acid, and has approximately 40-fold higher activity with 9-cis-retinal than with all-trans-retinal. In addition, this enzyme has been shown to catalyze the conversion of 2-aminomuconic semialdehyde to 2-aminomuconate in the kynurenine pathway of tryptophan catabolism. [provided by RefSeq, Jul 2018]

Canonical amino-acid sequenceUniProt

487 residues, UniProt reviewed canonical sequence.

>Q9H2A2|ALDH8A1
     1  MAGTNALLML ENFIDGKFLP CSSYIDSYDP STGEVYCRVP NSGKDEIEAA VKAAREAFPS
    61  WSSRSPQERS RVLNQVADLL EQSLEEFAQA ESKDQGKTLA LARTMDIPRS VQNFRFFASS
   121  SLHHTSECTQ MDHLGCMHYT VRAPVGVAGL ISPWNLPLYL LTWKIAPAMA AGNTVIAKPS
   181  ELTSVTAWML CKLLDKAGVP PGVVNIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIT
   241  QLSAPHCKKL SLELGGKNPA IIFEDANLDE CIPATVRSSF ANQGEICLCT SRIFVQKSIY
   301  SEFLKRFVEA TRKWKVGIPS DPLVSIGALI SKAHLEKVRS YVKRALAEGA QIWCGEGVDK
   361  LSLPARNQAG YFMLPTVITD IKDESCCMTE EIFGPVTCVV PFDSEEEVIE RANNVKYGLA
   421  ATVWSSNVGR VHRVAKKLQS GLVWTNCWLI RELNLPFGGM KSSGIGREGA KDSYDFFTEI
   481  KTITVKH

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ALDH8A1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability: Intracellular
Secreted: No
Transmembrane segments: 0
Mean surface accessibility (rSASA): 0.21
Highest tissue expression: 231 nTPM

Expression across tissuesHPA

Tissue

liver: 231 nTPM
kidney: 67 nTPM
cerebellum: 6.2 nTPM
hippocampal formation: 4.8 nTPM
cerebral cortex: 3.8 nTPM
midbrain: 3.7 nTPM

Single-cell type

hepatocytes: 172 nCPM
epicardial cells: 89 nCPM
proximal tubule cells: 82 nCPM
renal collecting duct principal cells: 47 nCPM
oligodendrocytes: 26 nCPM
brain excitatory neurons: 21 nCPM

Immune cell

basophil: 2.4 nTPM
NK-cell: 0.9 nTPM
neutrophil: 0.8 nTPM
gdT-cell: 0.4 nTPM
memory B-cell: 0.4 nTPM
naive B-cell: 0.4 nTPM

Brain region

cerebral cortex: 25 nTPM
white matter: 22 nTPM
cerebellum: 19 nTPM
hippocampal formation: 18 nTPM
pons: 18 nTPM
amygdala: 17 nTPM

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance): 1.46
gnomAD pLI: 0
gnomAD missense Z: 0.49
DepMap mean gene effect: -0.04
DepMap dependency class: selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

retinal dehydrogenase (NAD+) activity
aminomuconate-semialdehyde dehydrogenase activity

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads ALDH8A1 as an antibody target. Whether an autoantibody or antibody against ALDH8A1 could matter depends on whether native ALDH8A1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

ALDH8A1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.

Annotation status

The present source text does not explicitly label ALDH8A1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

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