P00352 (AL1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinal dehydrogenase 1
Short name=RALDH 1
Short name=RalDH1
EC=1.2.1.36

Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic

Gene names

Name:	ALDH1A1
Synonyms:	ALDC, ALDH1, PUMB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid By similarity.
Catalytic activity	Retinal + NAD+ + H2O = retinoate + NADH.
Pathway	Cofactor metabolism; retinol metabolism.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular aldehyde metabolic process Traceable author statement PubMed 1709013. Source: ProtInc ethanol oxidation Traceable author statement. Source: Reactome retinol metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	Ras GTPase activator activity Traceable author statement PubMed 1709013. Source: UniProtKB aldehyde dehydrogenase (NAD) activity Inferred from experiment. Source: Reactome androgen binding Traceable author statement PubMed 1709013. Source: ProtInc retinal dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.10
	Chain	2 – 501	500	Retinal dehydrogenase 1		PRO_0000056415
Regions
	Nucleotide binding	246 – 251	6	NAD By similarity
Sites
	Active site	269	1	Proton acceptor Ref.13
	Active site	303	1	Nucleophile Ref.13
	Binding site	456	1	NAD
	Site	170	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.10
	Modified residue	91	1	N6-acetyllysine Ref.15
	Modified residue	128	1	N6-acetyllysine Ref.15
	Modified residue	252	1	N6-acetyllysine Ref.15
	Modified residue	353	1	N6-acetyllysine Ref.15
	Modified residue	367	1	N6-acetyllysine Ref.15
	Modified residue	410	1	N6-acetyllysine Ref.15
	Modified residue	419	1	N6-acetyllysine Ref.15
	Modified residue	435	1	N6-acetyllysine Ref.15
	Modified residue	495	1	N6-acetyllysine Ref.15
Natural variations
	Natural variant	121	1	N → S. Ref.2 Corresponds to variant rs1049981 [ dbSNP | Ensembl ].		VAR_048901
	Natural variant	125	1	G → R. Corresponds to variant rs11554423 [ dbSNP | Ensembl ].		VAR_048902
	Natural variant	177	1	I → F. Ref.5 Corresponds to variant rs8187929 [ dbSNP | Ensembl ].		VAR_017778
Experimental info
	Sequence conflict	162	1	V → I in AAA35518. Ref.11
	Sequence conflict	162	1	V → I in AAA51695. Ref.12

Sequences

	Sequence		Length	Mass (Da)
	P00352 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B26464DC7168348E	FASTA	501	54,862
	10 20 30 40 50 60 MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV 70 80 90 100 110 120 DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR LLLATMESMN GGKLYSNAYL 130 140 150 160 170 180 NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI 190 200 210 220 230 240 GPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID 250 260 270 280 290 300 KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG 310 320 330 340 350 360 QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES 370 380 390 400 410 420 GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR 430 440 450 460 470 480 ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE 490 500 YGFHEYTEVK TVTVKISQKN S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic structure of the human cytosolic aldehyde dehydrogenase gene." Hsu L.C., Chang W.-C., Yoshida A. Genomics 5:857-865(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and expression of the full-length cDNAs encoding human liver class 1 and class 2 aldehyde dehydrogenase." Zheng C.F., Wang T.T., Weiner H. Alcohol. Clin. Exp. Res. 17:828-831(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-121. Tissue: Liver.
[3]	"Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from human lens cDNA library." Ramana K.V., Xiao T., Ansari N.H. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	NIEHS SNPs program Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-177.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: Colon.
[9]	"Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization." Yoshida A., Hsu L.C., Yanagawa Y. Adv. Exp. Med. Biol. 328:37-44(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[10]	"Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme." Hempel J., von Bahr-Lindstroem H., Joernvall H. Eur. J. Biochem. 141:21-35(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-501, ACETYLATION AT SER-2. Tissue: Liver.
[11]	"Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases." Yoshida A., Ikawa M., Hsu L.C., Tani K. Alcohol 2:103-106(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
[12]	"Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2." Hsu L.C., Tani K., Fujiyoshi T., Kurachi K., Yoshida A. Proc. Natl. Acad. Sci. U.S.A. 82:3771-3775(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501. Tissue: Liver.
[13]	"Active site of human liver aldehyde dehydrogenase." Abriola D.P., Fields R., Stein S., Mackerell A.D. Jr., Pietruszko R. Biochemistry 26:5679-5684(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, NAD-BINDING SITE CYS-456.
[14]	"Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme." Agarwal D.P., Cohn P., Goedde H.W., Hempel J. Enzyme 42:47-52(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Erythrocyte.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252; LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, MASS SPECTROMETRY.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31994 , M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA. Translation: AAA51692.1. AF003341 mRNA. Translation: AAC51652.1. AY390731 mRNA. Translation: AAR92229.1. BT006921 mRNA. Translation: AAP35567.1. AY338497 Genomic DNA. Translation: AAP88039.1. AL591031 Genomic DNA. Translation: CAI12257.1. CH471089 Genomic DNA. Translation: EAW62543.1. BC001505 mRNA. Translation: AAH01505.1. S61235 Genomic DNA. Translation: AAD13925.1. M26761 mRNA. Translation: AAA35518.1. K03000 mRNA. Translation: AAA51695.1.
IPI	IPI00218914.
PIR	DEHUE1. A33371.
RefSeq	NP_000680.2. NM_000689.4.
UniGene	Hs.76392.
3D structure databases
ProteinModelPortal	P00352.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00352. 6 interactions.
STRING	9606.ENSP00000297785.
PTM databases
PhosphoSite	P00352.
Polymorphism databases
DMDM	118495.
2D gel databases
DOSAC-COBS-2DPAGE	P00352.
REPRODUCTION-2DPAGE	IPI00218914. P00352.
SWISS-2DPAGE	P00352.
UCD-2DPAGE	P00352.
Proteomic databases
PaxDb	P00352.
PeptideAtlas	P00352.
PRIDE	P00352.
Protocols and materials databases
DNASU	216.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297785; ENSP00000297785; ENSG00000165092.
GeneID	216.
KEGG	hsa:216.
UCSC	uc004ajd.3. human.
Organism-specific databases
CTD	216.
GeneCards	GC09M075515.
HGNC	HGNC:402. ALDH1A1.
HPA	CAB020690. HPA002123.
MIM	100640. gene.
neXtProt	NX_P00352.
PharmGKB	PA24692.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HOG000271505.
HOVERGEN	HBG000097.
InParanoid	P00352.
KO	K07249.
OMA	HVASLIQ.
OrthoDB	EOG4Z8XW6.
PhylomeDB	P00352.
Enzyme and pathway databases
BioCyc	MetaCyc:HS09183-MONOMER.
Reactome	REACT_111217. Metabolism.
SABIO-RK	P00352.
UniPathway	UPA00912.
Gene expression databases
ArrayExpress	P00352.
Bgee	P00352.
CleanEx	HS_ALDH1A1.
Genevestigator	P00352.
GermOnline	ENSG00000165092. Homo sapiens.
Family and domain databases
Gene3D	3.40.309.10. 1 hit. 3.40.605.10. 1 hit.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view]
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00352.
ChEMBL	CHEMBL3577.
ChiTaRS	ALDH1A1. human.
DrugBank	DB00157. NADH. DB00755. Tretinoin. DB00162. Vitamin A.
GenomeRNAi	216.
NextBio	874.
SOURCE	Search...

Entry information

Entry name

AL1A1_HUMAN

Accession

Primary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.