Retinal dehydrogenase 1 - Rattus norvegicus (Rat)

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P51647 (AL1A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Aldh

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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	Is capable of converting 9-cis and all-trans retinal to corresponding retinoic acid with high efficiency, 9-cis retinal being 2-fold more active than all-trans retinal.
Catalytic activity	Retinal + NAD⁺ + H₂O = retinoate + NADH.
Enzyme regulation	Inhibited by chloral hydrate.
Pathway	Cofactor metabolism; retinol metabolism.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	9-cis-retinoic acid biosynthetic process Inferred from electronic annotation. Source: Compara 9-cis-retinoic acid metabolic process Inferred from direct assay PubMed 17167544. Source: RGD estrous cycle phase Inferred from expression pattern PubMed 18202528. Source: RGD kidney development Inferred from expression pattern PubMed 15567713. Source: RGD liver development Inferred from expression pattern PubMed 14729401. Source: RGD midgut development Inferred from expression pattern PubMed 15964596. Source: RGD optic cup morphogenesis involved in camera-type eye development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from direct assay PubMed 10998257. Source: RGD response to drug Inferred from expression pattern PubMed 10323328. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 18202528. Source: RGD response to ethanol Inferred from direct assay PubMed 17673211. Source: RGD response to oxidative stress Inferred from mutant phenotype PubMed 15623782. Source: RGD response to retinoic acid Inferred from expression pattern PubMed 11169459. Source: RGD retinoic acid biosynthetic process Inferred from mutant phenotype PubMed 21138835. Source: RGD retinol metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from direct assay PubMed 21138835. Source: RGD nucleus Inferred from direct assay PubMed 21138835. Source: RGD
Molecular_function	3-chloroallyl aldehyde dehydrogenase activity Traceable author statement Ref.1. Source: RGD benzaldehyde dehydrogenase (NAD+) activity Inferred from direct assay PubMed 10998257. Source: RGD identical protein binding Inferred from direct assay PubMed 10998257. Source: RGD retinal dehydrogenase activity Inferred from direct assay PubMed 17167544. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 501

500

Retinal dehydrogenase 1

PRO_0000056419

Regions

Nucleotide binding

246 – 251

NAD By similarity

Sites

Active site

269

Proton acceptor By similarity

Active site

303

Nucleophile By similarity

Binding site

456

NAD By similarity

Site

170

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

N-acetylserine Probable

Modified residue

N6-acetyllysine By similarity

Modified residue

128

N6-acetyllysine By similarity

Modified residue

252

N6-acetyllysine By similarity

Modified residue

353

N6-acetyllysine By similarity

Modified residue

367

N6-acetyllysine By similarity

Modified residue

410

N6-acetyllysine By similarity

Modified residue

419

N6-acetyllysine By similarity

Modified residue

435

N6-acetyllysine By similarity

Modified residue

495

N6-acetyllysine By similarity

Experimental info

Sequence conflict

100

R → C in AAA96657. Ref.1

Sequence conflict

106

I → M AA sequence Ref.6

Sequence conflict

170

N → E in AAA96657. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P51647 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A3614C21BCE7E144
Show »

FASTA

501

54,459

        10         20         30         40         50         60 
MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC HVEEGDKADV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR LLLATIEAIN GGKVFANAYL 

       130        140        150        160        170        180 
SDLGGSIKAL KYCAGWADKI HGQTIPSDGD IFTFTRREPI GVCGQIIPWN FPLLMFIWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 

       250        260        270        280        290        300 
KVAFTGSTQV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG 

       310        320        330        340        350        360 
QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ HDKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDDVIKR 

       430        440        450        460        470        480 
ANNTTYGLAA GVFTKDLDRA ITVSSALQAG VVWVNCYMIL SAQCPFGGFK MSGNGRELGE 

       490        500 
HGLYEYTELK TVAMKISQKN S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation." Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A. Gene 166:303-306(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Kidney.
[2]	"A preliminary report on the cloning of a constitutively expressed rat liver cytosolic ALDH cDNA by PCR." Kathmann E.C., Lipsky J.J. Adv. Exp. Med. Biol. 414:69-72(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	"Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic aldehyde dehydrogenase." Kathmann E.C., Lipsky J.J. Biochem. Biophys. Res. Commun. 236:527-531(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[4]	"Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli." Napoli J.L., Penzes P., Wang X., Sperkova Z. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[5]	"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: Pituitary.
[6]	"A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid." Labrecque J., Dumas F., Lacroix A., Bhat P.V. Biochem. J. 305:681-684(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438. Strain: Sprague-Dawley. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42009 mRNA. Translation: AAA96657.1. AF001896 mRNA. Translation: AAC53304.1. AF001898 mRNA. Translation: AAC53306.1. AF001897 mRNA. Translation: AAC53305.1. U79118 mRNA. Translation: AAB63423.1. BC061526 mRNA. Translation: AAH61526.1.
IPI	IPI00332042.
PIR	JC4524. JC5553.
RefSeq	NP_071852.2. NM_022407.3.
UniGene	Rn.6132.
3D structure databases
ProteinModelPortal	P51647.
SMR	P51647. Positions 9-501.
ModBase	Search...
PTM databases
PhosphoSite	P51647.
Proteomic databases
PaxDb	P51647.
PRIDE	P51647.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024000; ENSRNOP00000024000; ENSRNOG00000017619.
GeneID	24188.
KEGG	rno:24188.
UCSC	RGD:2087. rat.
Organism-specific databases
CTD	216.
RGD	2087. Aldh1a1.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	ENSGT00550000074289.
HOGENOM	HOG000271505.
HOVERGEN	HBG000097.
KO	K07249.
OrthoDB	EOG4Z8XW6.
Enzyme and pathway databases
BRENDA	1.2.1.36. 5301.
SABIO-RK	P51647.
UniPathway	UPA00912.
Gene expression databases
Genevestigator	P51647.
GermOnline	ENSRNOG00000017619. Rattus norvegicus.
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	P51647.
ChEMBL	CHEMBL2931.
NextBio	602555.

Entry information

Entry name

AL1A1_RAT

Accession

Primary (citable) accession number: P51647
Secondary accession number(s): O09184

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents