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Protein

Aldehyde dehydrogenase family 1 member A3

Gene

Aldh1a3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid (PubMed:11044606, PubMed:11013254, PubMed:14623956). Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde (By similarity). Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region (PubMed:14623956).By similarity3 Publications

Catalytic activityi

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.2 Publications

Kineticsi

  1. KM=0.33 µM for all-trans retinal1 Publication
  1. Vmax=58 nmol/min/mg enzyme for all-trans retinal1 Publication

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei181Transition state stabilizerBy similarity1
Binding sitei204NADBy similarity1
Binding sitei207NADBy similarity1
Active sitei280Proton acceptorPROSITE-ProRule annotation1
Active sitei314NucleophilePROSITE-ProRule annotation1
Binding sitei361NADBy similarity1
Binding sitei411NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi257 – 262NADBy similarity6

GO - Molecular functioni

  • 3-chloroallyl aldehyde dehydrogenase activity Source: MGI
  • aldehyde dehydrogenase (NAD) activity Source: MGI
  • aldehyde dehydrogenase [NAD(P)+] activity Source: MGI
  • NAD+ binding Source: MGI
  • protein homodimerization activity Source: MGI
  • thyroid hormone binding Source: MGI

GO - Biological processi

  • embryonic camera-type eye development Source: MGI
  • embryonic eye morphogenesis Source: MGI
  • face development Source: MGI
  • inner ear morphogenesis Source: MGI
  • locomotory behavior Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • nucleus accumbens development Source: MGI
  • olfactory pit development Source: MGI
  • optic cup morphogenesis involved in camera-type eye development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of retinoic acid receptor signaling pathway Source: MGI
  • retinal metabolic process Source: MGI
  • retinoic acid biosynthetic process Source: MGI
  • retinoic acid metabolic process Source: MGI
  • retinol metabolic process Source: UniProtKB-UniPathway
  • righting reflex Source: MGI

Keywordsi

Molecular functionOxidoreductase
LigandNAD

Enzyme and pathway databases

BRENDAi1.2.1.36. 3474.
1.2.1.5. 3474.
ReactomeiR-MMU-5365859. RA biosynthesis pathway.
SABIO-RKQ9JHW9.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 1 member A3 (EC:1.2.1.52 Publications)
Alternative name(s):
Aldehyde dehydrogenase 61 Publication
Retinaldehyde dehydrogenase 3
Short name:
RALDH-31 Publication
Short name:
RalDH31 Publication
Gene namesi
Name:Aldh1a3
Synonyms:Aldh6, Raldh3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1861722. Aldh1a3.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate, but all die within 10 hours after birth (PubMed:14623956, PubMed:23536097). Lethality is due to respiratory distress, caused by choanal atresia, i.e. the lack of communication between the nasal and oral cavities. Mutant embryos at 11.5 dpc lack detectable retinoic acid in the ventral retina, nasal epithelium and in the nasolacrimal groove. At 14.5 dpc mutant embryos display shortening of the ventral retina associated with lens rotation and persistence of the retrolenticular membrane, indicative of retinoic acid deficiency. Still, at 18.5 dpc the ventral retina appears normal. Embryos at 18.5 dpc lack Harderian glands, and display multiple malformations in the nasal region, including choanal atresia, lack of maxillary sinuses and nasolacrimal ducts (PubMed:14623956). Oral gavage of pregnant females with retinoic acid prevents choanal atresia and other malformations of the nasal region (PubMed:14623956, PubMed:23536097). Females that were fed retinoic acid give birth to pups with malformations of the inner ear vestibular organ, causing repetitive circling behavior with head tilting (PubMed:23536097). Likewise, mice display impaired ability in crossing a beam without slipping and an impaired ability to swim (PubMed:23536097).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000564792 – 512Aldehyde dehydrogenase family 1 member A3Add BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JHW9.
PaxDbiQ9JHW9.
PRIDEiQ9JHW9.

PTM databases

iPTMnetiQ9JHW9.
PhosphoSitePlusiQ9JHW9.

Expressioni

Tissue specificityi

Detected in embryonic head (at protein level) (PubMed:14623956). Ventral retina.5 Publications

Developmental stagei

In mouse embryos, RALDH3 expression is first noticed in the ventral optic eminence at E8.75, then in the optic vesicle/cup, otic vesicle and olfactory placode/pit from E9.5 to E11.5.1 Publication

Gene expression databases

BgeeiENSMUSG00000015134.
CleanExiMM_ALDH1A3.
ExpressionAtlasiQ9JHW9. baseline and differential.
GenevisibleiQ9JHW9. MM.

Interactioni

Subunit structurei

Homotetramer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi208193. 1 interactor.
STRINGi10090.ENSMUSP00000015278.

Structurei

3D structure databases

ProteinModelPortaliQ9JHW9.
SMRiQ9JHW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ9JHW9.
KOiK00129.
OMAiRIYADAR.
OrthoDBiEOG090B04CB.
PhylomeDBiQ9JHW9.
TreeFamiTF300455.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiView protein in InterPro
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
PfamiView protein in Pfam
PF00171. Aldedh. 1 hit.
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiView protein in PROSITE
PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JHW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTNGAVEN GQPDGKPPAL PRPIRNLEVK FTKIFINNDW HESKSGRKFA
60 70 80 90 100
TYNPSTLEKI CEVEEGDKPD VDKAVEAAQA AFQRGSPWRR LDALSRGQLL
110 120 130 140 150
HQLADLVERD RAILATLETM DTGKPFLHAF FVDLEGCIKT FRYFAGWADK
160 170 180 190 200
IQGRTIPTDD NVVCFTRHEP IGVCGAITPW NFPLLMLAWK LAPALCCGNT
210 220 230 240 250
VVLKPAEQTP LTALYLASLI KEVGFPPGVV NIVPGFGPTV GAAISSHPQI
260 270 280 290 300
NKIAFTGSTE VGKLVREAAS RSNLKRVTLE LGGKNPCIVC ADADLDLAVE
310 320 330 340 350
CAHQGVFFNQ GQCCTAASRV FVEEQVYGEF VRRSVEFAKK RPVGDPFDAK
360 370 380 390 400
TEQGPQIDQK QFDKILELIE SGKKEGAKLE CGGSAMEDRG LFIKPTVFSD
410 420 430 440 450
VTDNMRIAKE EIFGPVQPIL KFKNLEEVIK RANSTDYGLT AAVFTKNLDK
460 470 480 490 500
ALKLAAALES GTVWINCYNA FYAQAPFGGF KMSGNGRELG EYALAEYTEV
510
KTVTIKLEEK NP
Length:512
Mass (Da):56,157
Last modified:October 1, 2000 - v1
Checksum:i5BBC6DEE41E58CFE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91L → V in AAF67736 (PubMed:10906479).Curated1
Sequence conflicti208Q → R in AAG33935 (PubMed:11013254).Curated1
Sequence conflicti223V → E in AAF67736 (PubMed:10906479).Curated1
Sequence conflicti341R → S in AAG33935 (PubMed:11013254).Curated1
Sequence conflicti407I → R in AAF67736 (PubMed:10906479).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF253409 mRNA. Translation: AAF67736.1.
AF280404 mRNA. Translation: AAF86980.1.
AF246711 mRNA. Translation: AAG38488.1.
AF152359 mRNA. Translation: AAG33935.1.
BC058277 mRNA. Translation: AAH58277.1.
CCDSiCCDS21345.1.
RefSeqiNP_444310.3. NM_053080.3.
UniGeneiMm.140988.

Genome annotation databases

EnsembliENSMUST00000015278; ENSMUSP00000015278; ENSMUSG00000015134.
GeneIDi56847.
KEGGimmu:56847.
UCSCiuc009hhi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF253409 mRNA. Translation: AAF67736.1.
AF280404 mRNA. Translation: AAF86980.1.
AF246711 mRNA. Translation: AAG38488.1.
AF152359 mRNA. Translation: AAG33935.1.
BC058277 mRNA. Translation: AAH58277.1.
CCDSiCCDS21345.1.
RefSeqiNP_444310.3. NM_053080.3.
UniGeneiMm.140988.

3D structure databases

ProteinModelPortaliQ9JHW9.
SMRiQ9JHW9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208193. 1 interactor.
STRINGi10090.ENSMUSP00000015278.

PTM databases

iPTMnetiQ9JHW9.
PhosphoSitePlusiQ9JHW9.

Proteomic databases

MaxQBiQ9JHW9.
PaxDbiQ9JHW9.
PRIDEiQ9JHW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015278; ENSMUSP00000015278; ENSMUSG00000015134.
GeneIDi56847.
KEGGimmu:56847.
UCSCiuc009hhi.2. mouse.

Organism-specific databases

CTDi220.
MGIiMGI:1861722. Aldh1a3.

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ9JHW9.
KOiK00129.
OMAiRIYADAR.
OrthoDBiEOG090B04CB.
PhylomeDBiQ9JHW9.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi1.2.1.36. 3474.
1.2.1.5. 3474.
ReactomeiR-MMU-5365859. RA biosynthesis pathway.
SABIO-RKQ9JHW9.

Miscellaneous databases

PROiQ9JHW9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000015134.
CleanExiMM_ALDH1A3.
ExpressionAtlasiQ9JHW9. baseline and differential.
GenevisibleiQ9JHW9. MM.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiView protein in InterPro
IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
PfamiView protein in Pfam
PF00171. Aldedh. 1 hit.
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiView protein in PROSITE
PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAL1A3_MOUSE
AccessioniPrimary (citable) accession number: Q9JHW9
Secondary accession number(s): Q9EQP7, Q9JI72
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2000
Last modified: February 15, 2017
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.