Retinal dehydrogenase 2 - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

Q63639 (AL1A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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 2
Short name=RALDH 2
Short name=RalDH2
EC=1.2.1.36

Alternative name(s):
Aldehyde dehydrogenase family 1 member A2
Retinaldehyde-specific dehydrogenase type 2
Short name=RALDH(II)

Gene names

Name:	Aldh1a2
Synonyms:	Raldh2

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	518 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Retinal + NAD⁺ + H₂O = retinoate + NADH.
Pathway	Cofactor metabolism; retinol metabolism.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Tissue specificity	Found in testis and less abundantly in lung, brain, heart, liver and kidney.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.
Sequence caution	The sequence AAC52637.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	9-cis-retinoic acid biosynthetic process Inferred from electronic annotation. Source: Compara anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara blood vessel development Inferred from electronic annotation. Source: Compara cardiac muscle tissue development Inferred from electronic annotation. Source: Compara cellular response to retinoic acid Inferred from electronic annotation. Source: Compara determination of bilateral symmetry Inferred from electronic annotation. Source: Compara embryonic camera-type eye development Inferred from electronic annotation. Source: Compara embryonic digestive tract development Inferred from electronic annotation. Source: Compara embryonic forelimb morphogenesis Inferred from electronic annotation. Source: Compara face development Inferred from electronic annotation. Source: Compara heart morphogenesis Inferred from electronic annotation. Source: Compara hindbrain development Inferred from electronic annotation. Source: Compara kidney development Inferred from expression pattern PubMed 15567713. Source: RGD liver development Inferred from expression pattern PubMed 14729401. Source: RGD lung development Inferred from electronic annotation. Source: Compara midgut development Inferred from expression pattern PubMed 15964596. Source: RGD morphogenesis of embryonic epithelium Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara neural crest cell development Inferred from electronic annotation. Source: Compara neural tube development Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara pancreas development Inferred from electronic annotation. Source: Compara pituitary gland development Inferred from expression pattern PubMed 17180597. Source: RGD positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara proximal/distal pattern formation Inferred from electronic annotation. Source: Compara regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from expression pattern PubMed 15205379. Source: RGD response to vitamin A Inferred from expression pattern PubMed 11169459. Source: RGD retinal metabolic process Inferred from electronic annotation. Source: Compara retinoic acid biosynthetic process Inferred from mutant phenotype PubMed 21138835. Source: RGD retinoic acid receptor signaling pathway Inferred from electronic annotation. Source: Compara retinol metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway ureter maturation Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from direct assay PubMed 12547725. Source: RGD nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from direct assay PubMed 21138835. Source: RGD
Molecular_function	3-chloroallyl aldehyde dehydrogenase activity Inferred from electronic annotation. Source: Compara retinal binding Inferred from direct assay Ref.2. Source: RGD retinal dehydrogenase activity Inferred from direct assay PubMed 12547725. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 518

518

Retinal dehydrogenase 2

PRO_0000056424

Regions

Nucleotide binding

263 – 268

NAD By similarity

Sites

Active site

286

Proton acceptor

Active site

320

Nucleophile

Site

187

Transition state stabilizer

Amino acid modifications

Modified residue

119

Phosphothreonine By similarity

Modified residue

122

Phosphothreonine By similarity

Secondary structure

518

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q63639 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 2BDDAABB0D2D066C
Show »

FASTA

518

56,640

        10         20         30         40         50         60 
MTSSEIAMPG EVKADPAALM ASLQLLPSPT PNLEIKYTKI FINNEWQNSE SGRVFPVCNP 

        70         80         90        100        110        120 
ATGEQVCEVQ EADKVDIDKA VQAARLAFSL GSVWRRMDAS ERGRLLDKLA DLVERDRATL 

       130        140        150        160        170        180 
ATMESLNGGK PFLQAFYIDL QGVIKTLRYY AGWADKIHGM TIPVDGDYFT FTRHEPIGVC 

       190        200        210        220        230        240 
GQIIPWNFPL LMFTWKIAPA LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVVNILP 

       250        260        270        280        290        300 
GYGPTAGAAI ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD 

       310        320        330        340        350        360 
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVKRS VERAKRRIVG SPFDPTTEQG 

       370        380        390        400        410        420 
PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE PTVFSNVTDD MRIAKEEIFG 

       430        440        450        460        470        480 
PVQEILRFKT MDEVIERANN SDFGLVAAVF TNDINKALMV SSAMQAGTVW INCYNALNAQ 

       490        500        510 
SPFGGFKMSG NGREMGEFGL REYSEVKTVT VKIPQKNS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC098910 mRNA. Translation: AAH98910.1.
U60063 mRNA. Translation: AAC52637.1. Different initiation.

IPI

IPI00211419.

RefSeq

NP_446348.2. NM_053896.2.

UniGene

Rn.10514.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BI9	X-ray	2.70	A/B/C/D	20-518	[»]

ProteinModelPortal

Q63639.

SMR

Q63639. Positions 20-518.

ModBase

Search...

Proteomic databases

PaxDb

Q63639.

PRIDE

Q63639.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000021757; ENSRNOP00000021757; ENSRNOG00000016042.

GeneID

116676.

KEGG

rno:116676.

UCSC

RGD:620250. rat.

Organism-specific databases

CTD

8854.

RGD

620250. Aldh1a2.

Phylogenomic databases

eggNOG

COG1012.

GeneTree

ENSGT00550000074289.

HOGENOM

HOG000271505.

HOVERGEN

HBG000097.

InParanoid

Q63639.

K07249.

OMA

ICEIQEA.

OrthoDB

EOG4Z8XW6.

Enzyme and pathway databases

BRENDA

1.2.1.36. 5301.

UniPathway

UPA00912.

Gene expression databases

Genevestigator

Q63639.

GermOnline

ENSRNOG00000016042. 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

EvolutionaryTrace

Q63639.

NextBio

619506.

Entry information

Entry name

AL1A2_RAT

Accession

Primary (citable) accession number: Q63639
Secondary accession number(s): Q4FZY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 7, 2006
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure 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