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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: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.
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
Sitei187Transition state stabilizer1
Active sitei286Proton acceptor1
Active sitei320Nucleophile1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi263 – 268NADBy similarity6

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.
ReactomeiR-RNO-5365859. 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
Proteomesi
  • UP000002494 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000564241 – 518Retinal dehydrogenase 2Add BLAST518

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei168PhosphotyrosineBy similarity1
Modified residuei351PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63639.
PRIDEiQ63639.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000016042.
GenevisibleiQ63639. RN.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021757.

Structurei

Secondary structure

1518
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 42Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi54 – 58Combined sources5
Turni60 – 62Combined sources3
Beta strandi65 – 70Combined sources6
Helixi74 – 88Combined sources15
Beta strandi89 – 91Combined sources3
Helixi93 – 96Combined sources4
Helixi99 – 115Combined sources17
Helixi117 – 128Combined sources12
Helixi132 – 137Combined sources6
Helixi139 – 151Combined sources13
Turni152 – 155Combined sources4
Beta strandi159 – 162Combined sources4
Beta strandi165 – 176Combined sources12
Beta strandi179 – 183Combined sources5
Beta strandi186 – 188Combined sources3
Helixi189 – 202Combined sources14
Beta strandi206 – 210Combined sources5
Helixi217 – 229Combined sources13
Beta strandi235 – 238Combined sources4
Turni243 – 245Combined sources3
Helixi246 – 252Combined sources7
Beta strandi258 – 263Combined sources6
Helixi265 – 277Combined sources13
Beta strandi282 – 286Combined sources5
Beta strandi293 – 295Combined sources3
Helixi301 – 313Combined sources13
Helixi314 – 317Combined sources4
Beta strandi326 – 329Combined sources4
Helixi330 – 346Combined sources17
Helixi365 – 379Combined sources15
Turni380 – 382Combined sources3
Beta strandi384 – 387Combined sources4
Beta strandi393 – 396Combined sources4
Beta strandi402 – 406Combined sources5
Helixi412 – 415Combined sources4
Beta strandi420 – 428Combined sources9
Helixi431 – 439Combined sources9
Beta strandi445 – 450Combined sources6
Helixi454 – 463Combined sources10
Beta strandi467 – 472Combined sources6
Helixi499 – 501Combined sources3
Beta strandi504 – 512Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ63639.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ63639.
KOiK07249.
OMAiKPIANAY.
OrthoDBiEOG091G05E8.
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 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

EnsembliENSRNOT00000079115; ENSRNOP00000073203; ENSRNOG00000055049.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BI9X-ray2.70A/B/C/D20-518[»]
ProteinModelPortaliQ63639.
SMRiQ63639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021757.

Proteomic databases

PaxDbiQ63639.
PRIDEiQ63639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000079115; ENSRNOP00000073203; ENSRNOG00000055049.
GeneIDi116676.
KEGGirno:116676.
UCSCiRGD:620250. rat.

Organism-specific databases

CTDi8854.
RGDi620250. Aldh1a2.

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ63639.
KOiK07249.
OMAiKPIANAY.
OrthoDBiEOG091G05E8.
PhylomeDBiQ63639.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi1.2.1.36. 5301.
ReactomeiR-RNO-5365859. RA biosynthesis pathway.

Miscellaneous databases

EvolutionaryTraceiQ63639.
PROiQ63639.

Gene expression databases

BgeeiENSRNOG00000016042.
GenevisibleiQ63639. RN.

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...

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: November 2, 2016
This is version 131 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

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.