Retinal dehydrogenase 1 - Mus musculus (Mouse)

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P24549 (AL1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 130. History...

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

Documents (3) |

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:	Ahd-2, Ahd2, Aldh1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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	In addition to the activity on acetaldehyde and related substrates, is also involved in the oxidation of aldehydes derived from biogenic amines such as epinephrine and norepinephrine, as well as the aldehydes generated via lipid peroxidation. 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	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in the liver, lung, and testis. Apparently not expressed at detectable levels in kidney, stomach, ovary, heart, and brain.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Sequence caution	The sequence AAH44729.1 differs from that shown. Reason: Erroneous initiation.

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 direct assay PubMed 11876656. Source: MGI estrous cycle phase Inferred from electronic annotation. Source: Compara kidney development Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara midgut development Inferred from electronic annotation. Source: Compara optic cup morphogenesis involved in camera-type eye development Inferred from genetic interaction PubMed 16611695. Source: MGI positive regulation of apoptotic process Inferred from genetic interaction PubMed 16207763 PubMed 16611695. Source: MGI protein homotetramerization Inferred from electronic annotation. Source: Compara response to drug Inferred from direct assay PubMed 18971422. Source: MGI response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara retinol metabolic process Inferred from mutant phenotype PubMed 12851412. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	3-chloroallyl aldehyde dehydrogenase activity Inferred from direct assay PubMed 12610736. Source: MGI benzaldehyde dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: Compara 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

Removed By similarity

Chain

2 – 501

500

Retinal dehydrogenase 1

PRO_0000056417

Regions

Nucleotide binding

246 – 251

NAD By similarity

Region

300 – 305

Antabuse binding

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 By similarity

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

A → R in AAA37202. Ref.1

Sequence conflict

A → R in AAA37203. Ref.1

Sequence conflict

T → S in AAB32754. Ref.2

Sequence conflict

H → Q in AAB32754. Ref.2

Sequence conflict

R → C in AAA37202. Ref.1

Sequence conflict

140

I → Y AA sequence Ref.4

Sequence conflict

458

M → I in AAA37202. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P24549 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 0E428151B799BD1D
Show »

FASTA

501

54,468

        10         20         30         40         50         60 
MSSPAQPAVP APLADLKIQH TKIFINNEWH NSVSGKKFPV LNPATEEVIC HVEEGDKADV 

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

       130        140        150        160        170        180 
SDLGGCIKAL KYCAGWADKI HGQTIPSDGD IFTYTRREPI GVCGQIIPWN FPMLMFIWKI 

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

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

       310        320        330        340        350        360 
QCCVAASRIF VEESVYDEFV KRSVERAKKY VLGNPLTPGI NQGPQIDKEQ HDKILDLIES 

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

       430        440        450        460        470        480 
ANNTTYGLAA GLFTKDLDKA ITVSSALQAG VVWVNCYMML SAQCPFGGFK MSGNGRELGE 

       490        500 
HGLYEYTELK TVAMKISQKN S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a cytosolic aldehyde dehydrogenase-encoding cDNA from mouse liver." Rongnoparut P., Weaver S. Gene 101:261-265(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: BALB/c and C57BL/6. Tissue: Liver.
[2]	"DNA sequence analysis of the cytosolic acetaldehyde dehydrogenase gene (Ahd-2) in mouse strains with variable ethanol preferences." Bond S.L., Singh S.M. Biochem. Med. Metab. Biol. 52:155-159(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: 129/ReJ, BALB/c and C57BL/6J. Tissue: Liver.
[3]	"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]. Strain: FVB/N. Tissue: Colon and Liver.
[4]	"Aldehyde dehydrogenase is a positional marker in the retina." McCaffery P., Tempst P., Lara G., Drager U.C. Development 112:693-702(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-52; 140-156; 211-230; 309-320; 330-349; 400-410; 421-435 AND 477-490. Tissue: Embryonic retina.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M74570 mRNA. Translation: AAA37202.1. M74571 Genomic DNA. Translation: AAA37203.1. S75713 mRNA. Translation: AAB32754.2. S77047 Genomic DNA. No translation available. BC044729 mRNA. Translation: AAH44729.1. Different initiation. BC054386 mRNA. Translation: AAH54386.1.
IPI	IPI00626662.
PIR	JQ1004.
RefSeq	NP_038495.2. NM_013467.3.
UniGene	Mm.250866.
3D structure databases
ProteinModelPortal	P24549.
SMR	P24549. Positions 9-501.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24549. 1 interaction.
PTM databases
PhosphoSite	P24549.
2D gel databases
REPRODUCTION-2DPAGE	IPI00626662. P24549.
SWISS-2DPAGE	P24549.
Proteomic databases
PaxDb	P24549.
PRIDE	P24549.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000087638; ENSMUSP00000084918; ENSMUSG00000053279.
GeneID	11668.
KEGG	mmu:11668.
UCSC	uc008gyn.1. mouse.
Organism-specific databases
CTD	216.
MGI	MGI:1353450. Aldh1a1.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	ENSGT00550000074289.
HOGENOM	HOG000271505.
HOVERGEN	HBG000097.
InParanoid	P24549.
KO	K07249.
OMA	CCIAGSR.
OrthoDB	EOG4Z8XW6.
Enzyme and pathway databases
BRENDA	1.2.1.36. 3474.
SABIO-RK	P24549.
UniPathway	UPA00912.
Gene expression databases
Bgee	P24549.
CleanEx	MM_ALDH1A1.
Genevestigator	P24549.
GermOnline	ENSMUSG00000053279. Mus musculus.
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
NextBio	279287.
SOURCE	Search...

Entry information

Entry name

AL1A1_MOUSE

Accession

Primary (citable) accession number: P24549
Secondary accession number(s): Q7TQJ0, Q811J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 130 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Protein-protein interaction databases

PTM databases

2D gel 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