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Protein

Retinal dehydrogenase 2

Gene

Aldh1a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently.

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei187 – 1871Transition state stabilizer
Active sitei286 – 2861Proton acceptor
Active sitei320 – 3201Nucleophile

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2686NADBy similarity

GO - Molecular functioni

  • 3-chloroallyl aldehyde dehydrogenase activity Source: GO_Central
  • aldehyde dehydrogenase (NAD) activity Source: GO_Central
  • retinal binding Source: RGD
  • retinal dehydrogenase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.36. 5301.
ReactomeiREACT_299215. RA biosynthesis pathway.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 2 (EC:1.2.1.36)
Short name:
RALDH 2
Short name:
RalDH2
Alternative name(s):
Aldehyde dehydrogenase family 1 member A2
Retinaldehyde-specific dehydrogenase type 2
Short name:
RALDH(II)
Gene namesi
Name:Aldh1a2
Synonyms:Raldh2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi620250. Aldh1a2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Retinal dehydrogenase 2PRO_0000056424Add
BLAST

Proteomic databases

PaxDbiQ63639.
PRIDEiQ63639.

Expressioni

Tissue specificityi

Found in testis and less abundantly in lung, brain, heart, liver and kidney.

Gene expression databases

GenevestigatoriQ63639.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
518
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424Combined sources
Beta strandi45 – 473Combined sources
Beta strandi54 – 585Combined sources
Turni60 – 623Combined sources
Beta strandi65 – 706Combined sources
Helixi74 – 8815Combined sources
Beta strandi89 – 913Combined sources
Helixi93 – 964Combined sources
Helixi99 – 11517Combined sources
Helixi117 – 12812Combined sources
Helixi132 – 1376Combined sources
Helixi139 – 15113Combined sources
Turni152 – 1554Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi165 – 17612Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi186 – 1883Combined sources
Helixi189 – 20214Combined sources
Beta strandi206 – 2105Combined sources
Helixi217 – 22913Combined sources
Beta strandi235 – 2384Combined sources
Turni243 – 2453Combined sources
Helixi246 – 2527Combined sources
Beta strandi258 – 2636Combined sources
Helixi265 – 27713Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi293 – 2953Combined sources
Helixi301 – 31313Combined sources
Helixi314 – 3174Combined sources
Beta strandi326 – 3294Combined sources
Helixi330 – 34617Combined sources
Helixi365 – 37915Combined sources
Turni380 – 3823Combined sources
Beta strandi384 – 3874Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi402 – 4065Combined sources
Helixi412 – 4154Combined sources
Beta strandi420 – 4289Combined sources
Helixi431 – 4399Combined sources
Beta strandi445 – 4506Combined sources
Helixi454 – 46310Combined sources
Beta strandi467 – 4726Combined sources
Helixi499 – 5013Combined sources
Beta strandi504 – 5129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BI9X-ray2.70A/B/C/D20-518[»]
ProteinModelPortaliQ63639.
SMRiQ63639. Positions 20-518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63639.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ63639.
KOiK07249.
OMAiICEIQEA.
OrthoDBiEOG7PS1F7.
PhylomeDBiQ63639.
TreeFamiTF300455.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE
60 70 80 90 100
SGRVFPVCNP ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS
110 120 130 140 150
ERGRLLDKLA DLVERDRATL ATMESLNGGK PFLQAFYIDL QGVIKTLRYY
160 170 180 190 200
AGWADKIHGM TIPVDGDYFT FTRHEPIGVC GQIIPWNFPL LMFTWKIAPA
210 220 230 240 250
LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP GYGPTAGAAI
260 270 280 290 300
ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
310 320 330 340 350
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG
360 370 380 390 400
SPFDPTTEQG PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE
410 420 430 440 450
PTVFSNVTDD MRIAKEEIFG PVQEILRFKT MDEVIERANN SDFGLVAAVF
460 470 480 490 500
TNDINKALMV SSAMQAGTVW INCYNALNAQ SPFGGFKMSG NGREMGEFGL
510
REYSEVKTVT VKIPQKNS
Length:518
Mass (Da):56,640
Last modified:March 7, 2006 - v2
Checksum:i2BDDAABB0D2D066C
GO

Sequence cautioni

The sequence AAC52637.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098910 mRNA. Translation: AAH98910.1.
U60063 mRNA. Translation: AAC52637.1. Different initiation.
RefSeqiNP_446348.2. NM_053896.2.
UniGeneiRn.10514.

Genome annotation databases

EnsembliENSRNOT00000021757; ENSRNOP00000021757; ENSRNOG00000016042.
GeneIDi116676.
KEGGirno:116676.
UCSCiRGD:620250. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098910 mRNA. Translation: AAH98910.1.
U60063 mRNA. Translation: AAC52637.1. Different initiation.
RefSeqiNP_446348.2. NM_053896.2.
UniGeneiRn.10514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BI9X-ray2.70A/B/C/D20-518[»]
ProteinModelPortaliQ63639.
SMRiQ63639. Positions 20-518.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ63639.
PRIDEiQ63639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021757; ENSRNOP00000021757; ENSRNOG00000016042.
GeneIDi116676.
KEGGirno:116676.
UCSCiRGD:620250. rat.

Organism-specific databases

CTDi8854.
RGDi620250. Aldh1a2.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ63639.
KOiK07249.
OMAiICEIQEA.
OrthoDBiEOG7PS1F7.
PhylomeDBiQ63639.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi1.2.1.36. 5301.
ReactomeiREACT_299215. RA biosynthesis pathway.

Miscellaneous databases

EvolutionaryTraceiQ63639.
NextBioi619506.
PROiQ63639.

Gene expression databases

GenevestigatoriQ63639.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Testis.
  2. "Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate."
    Wang X., Penzes P., Napoli J.L.
    J. Biol. Chem. 271:16288-16293(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-518.
    Tissue: Testis.
  3. "The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity."
    Lamb A.L., Newcomer M.E.
    Biochemistry 38:6003-6011(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-518.

Entry informationi

Entry nameiAL1A2_RAT
AccessioniPrimary (citable) accession number: Q63639
Secondary accession number(s): Q4FZY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: April 1, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.