Retinal dehydrogenase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P00352 (AL1A1_HUMAN)

Last modified July 22, 2008. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Retinal dehydrogenase 1
      Short name(s)=RALDH 1, RalDH1
    EC=1.2.1.36
Alternative name(s):
    Aldehyde dehydrogenase family 1 member A1
    Aldehyde dehydrogenase, cytosolic
    ALHDII
    ALDH-E1

Gene names

Name:	ALDH1A1
Synonyms:	ALDC, ALDH1, PUMB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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(+) + H(2)O = retinoate + NADH.
Pathway	Cofactor metabolism; retinol metabolism.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

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Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aldehyde metabolic process Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	Ras GTPase activator activity Traceable author statement. Source: UniProtKB aldehyde dehydrogenase (NAD) activity Traceable author statement. Source: ProtInc androgen binding Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

Removed

Chain

2 – 501

500

Retinal dehydrogenase 1

Regions

Nucleotide binding

246 – 251

NAD By similarity

Sites

Active site

269

Proton acceptor

Active site

303

Nucleophile

Binding site

456

NAD

Site

170

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

N-acetylserine

Natural variations

Natural variant

177

I → F: dbSNP rs8187929.

Experimental info

Sequence conflict

121

N → S in AAC51652. Ref.2

Sequence conflict

162

V → I Ref.9 Ref.10

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Sequences

Sequence

Length

Mass (Da)

Tools

P00352-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B26464DC7168348E
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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

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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: 2591967] [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: 8214422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-177.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[7]	"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: 8493914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
[8]	"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: 6723659] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-501, ACETYLATION AT SER-2. Tissue: Liver.
[9]	"Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases." Yoshida A., Ikawa M., Hsu L.C., Tani K. Alcohol 2:103-106(1985) [PubMed: 4015823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
[10]	"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: 2987944] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501. Tissue: Liver.
[11]	"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: 3676276] [Abstract] Cited for: PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, NAD-BINDING SITE CYS-456.
[12]	"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: 2776714] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Erythrocyte.

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Cross-references

Sequence databases
	M31994 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. BC001505 mRNA. Translation: AAH01505.1. S61235 Genomic DNA. Translation: AAD13925.1. M26761 mRNA. Translation: AAA35518.1. K03000 mRNA. Translation: AAA51695.1.
PIR	DEHUE1. A33371.
RefSeq	NP_000680.2.
UniGene	Hs.76392
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
SMR	P00352. Positions 22-501.
ModBase	Search...
PTM databases
PhosphoSite	P00352.
Polymorphism databases
NIEHS-SNPs	Search...
2-D gel databases
SWISS-2DPAGE	P00352.
Cornea-2DPAGE	P00352.
DOSAC-COBS-2DPAGE	P00352.
REPRODUCTION-2DPAGE	IPI00218914. P00352.
Proteomic databases
PeptideAtlas	P00352.
Genome annotation databases
Ensembl	ENSG00000165092. Homo sapiens. [Contig view]
GeneID	216.
KEGG	hsa:216.
Organism-specific databases
H-InvDB	HIX0008099.
HGNC	HGNC:402. ALDH1A1.
HPA	HPA002123.
MIM	100640. gene.
PharmGKB	PA24692.
GenAtlas	Search...
GeneCards	Search...
GeneLynx	Search...
Phylogenomic databases
HOGENOM	P00352.
HOVERGEN	P00352.
Enzyme and pathway databases
Reactome	REACT_2063. Metabolism of xenobiotics.
Gene expression databases
ArrayExpress	P00352.
CleanEx	HS_ALDH1A1.
GermOnline	ENSG00000165092. Homo sapiens.
Family and domain databases
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProDom	P00352. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
DrugBank	DB00157. NADH. DB00755. Tretinoin. DB00162. Vitamin A.
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

AL1A1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Polymorphism databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents