[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 4-518. TISSUE=Testis; DOI=10.1074/jbc.271.27.16288; PubMed=8663198 [NCBI, ExPASy, EBI, Israel, Japan] Wang X., Penzes P., Napoli J.L.; "Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate."; J. Biol. Chem. 271:16288-16293(1996).
[3]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-518. DOI=10.1021/bi9900471; PubMed=10320326 [NCBI, ExPASy, EBI, Israel, Japan] Lamb A.L., Newcomer M.E.; "The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity."; Biochemistry 38:6003-6011(1999).

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: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Found in testis and less abundantly in lung, brain, heart, liver and kidney.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC098910; AAH98910.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U60063; AAC52637.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_446348.1; -.

UniGene

Rn.10514

3D structure databases

PDB

1BI9; X-ray; 2.70 A; A/B/C/D=20-518.

[ExPASy / RCSB / EBI]

PDBsum

1BI9; -.

ModBase

Q63639.

Organism-specific databases

RGD

620250; Aldh1a2.

Gene expression databases

ArrayExpress

Q63639; -.

GermOnline

ENSRNOG00000016042; Rattus norvegicus.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

Q63639.

Genome annotation databases

Ensembl

ENSRNOG00000016042; Rattus norvegicus. [Contig view]

GeneID

116676; -.

KEGG

rno:116676; -.

NMPDR

fig|10116.3.peg.28888; -.

Phylogenomic databases

HOVERGEN

Q63639; -.

Other

ProtoNet

Q63639.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 518`	`518`	`Retinal dehydrogenase 2.`	`PRO_0000056424`
`NP_BIND`	`263 268`	`6`	`NAD (By similarity).`
`ACT_SITE`	`286 286`		`Proton acceptor.`
`ACT_SITE`	`320 320`		`Nucleophile.`
`SITE`	`187 187`	`1`	`Transition state stabilizer.`
`MOD_RES`	`119 119`		`Phosphothreonine (By similarity).`
`MOD_RES`	`122 122`		`Phosphothreonine (By similarity).`
`STRAND`	`39 42`	`4`
`STRAND`	`45 47`	`3`
`STRAND`	`54 58`	`5`
`TURN`	`60 62`	`3`
`STRAND`	`65 70`	`6`
`HELIX`	`74 88`	`15`
`STRAND`	`89 91`	`3`
`HELIX`	`93 96`	`4`
`HELIX`	`99 115`	`17`
`HELIX`	`117 128`	`12`
`HELIX`	`132 137`	`6`
`HELIX`	`139 151`	`13`
`TURN`	`152 155`	`4`
`STRAND`	`159 162`	`4`
`STRAND`	`165 176`	`12`
`STRAND`	`179 183`	`5`
`STRAND`	`186 188`	`3`
`HELIX`	`189 202`	`14`
`STRAND`	`206 210`	`5`
`HELIX`	`217 229`	`13`
`STRAND`	`235 238`	`4`
`TURN`	`243 245`	`3`
`HELIX`	`246 252`	`7`
`STRAND`	`258 263`	`6`
`HELIX`	`265 277`	`13`
`STRAND`	`282 286`	`5`
`STRAND`	`293 295`	`3`
`HELIX`	`301 313`	`13`
`HELIX`	`314 317`	`4`
`STRAND`	`326 329`	`4`
`HELIX`	`330 346`	`17`
`HELIX`	`365 379`	`15`
`TURN`	`380 382`	`3`
`STRAND`	`384 387`	`4`
`STRAND`	`393 396`	`4`
`STRAND`	`402 406`	`5`
`HELIX`	`412 415`	`4`
`STRAND`	`420 428`	`9`
`HELIX`	`431 439`	`9`
`STRAND`	`445 450`	`6`
`HELIX`	`454 463`	`10`
`STRAND`	`467 472`	`6`
`HELIX`	`499 501`	`3`
`STRAND`	`504 512`	`9`

Sequence information

Length: 518 AA [This is the length of the unprocessed precursor]

Molecular weight: 56640 Da [This is the MW of the unprocessed precursor]

CRC64: 2BDDAABB0D2D066C [This is a checksum on the sequence]

        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

Q63639 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools