[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=7484410 [NCBI, ExPASy, EBI, Israel, Japan] Stayner C.K., Tweedie J.W.; "Cloning and characterisation of the cDNA for sheep liver cytosolic aldehyde dehydrogenase."; Adv. Exp. Med. Biol. 372:61-66(1995).
[2]	X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). TISSUE=Liver; DOI=10.1016/S0969-2126(98)00152-X; PubMed=9862807 [NCBI, ExPASy, EBI, Israel, Japan] Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., Baker E.N.; "Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases."; Structure 6:1541-1551(1998).

Comments

FUNCTION: Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid.
CATALYTIC ACTIVITY: Retinal + NAD⁺ + H₂O = retinoate + NADH.
PATHWAY: Cofactor metabolism; retinol metabolism .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
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

U12761; AAA85435.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S78582; S14752.

NP_001009778.1; -.

3D structure databases

PDB

1BXS; X-ray; 2.35 A; A/B/C/D=1-501.

[ExPASy / RCSB / EBI]

PDBsum

1BXS; -.

ModBase

P51977.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0001758;	Molecular function: retinal dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

Genome annotation databases

GeneID

443343; -.

Phylogenomic databases

HOVERGEN

P51977; -.

Other

ProtoNet

P51977.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 501`	`500`	`Retinal dehydrogenase 1.`	`PRO_0000056420`
`NP_BIND`	`246 251`	`6`	`NAD (By similarity).`
`ACT_SITE`	`269 269`		`Proton acceptor.`
`ACT_SITE`	`303 303`		`Nucleophile.`
`SITE`	`170 170`	`1`	`Transition state stabilizer.`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`STRAND`	`22 25`	`4`
`STRAND`	`28 30`	`3`
`STRAND`	`37 41`	`5`
`TURN`	`43 45`	`3`
`STRAND`	`48 53`	`6`
`HELIX`	`57 70`	`14`
`HELIX`	`76 79`	`4`
`HELIX`	`82 98`	`17`
`HELIX`	`100 111`	`12`
`HELIX`	`115 120`	`6`
`HELIX`	`122 136`	`15`
`HELIX`	`137 139`	`3`
`STRAND`	`142 145`	`4`
`STRAND`	`148 159`	`12`
`STRAND`	`162 166`	`5`
`STRAND`	`169 171`	`3`
`HELIX`	`172 185`	`14`
`STRAND`	`189 193`	`5`
`HELIX`	`200 212`	`13`
`STRAND`	`218 221`	`4`
`TURN`	`226 228`	`3`
`HELIX`	`229 234`	`6`
`STRAND`	`240 246`	`7`
`HELIX`	`248 260`	`13`
`STRAND`	`265 269`	`5`
`STRAND`	`275 278`	`4`
`HELIX`	`284 296`	`13`
`TURN`	`297 300`	`4`
`STRAND`	`308 312`	`5`
`HELIX`	`313 327`	`15`
`HELIX`	`348 363`	`16`
`STRAND`	`373 375`	`3`
`STRAND`	`377 379`	`3`
`STRAND`	`385 389`	`5`
`HELIX`	`395 398`	`4`
`STRAND`	`403 411`	`9`
`HELIX`	`414 422`	`9`
`STRAND`	`428 433`	`6`
`HELIX`	`437 446`	`10`
`STRAND`	`450 455`	`6`
`HELIX`	`470 472`	`3`
`STRAND`	`473 475`	`3`
`HELIX`	`479 484`	`6`
`STRAND`	`487 495`	`9`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 54825 Da [This is the MW of the unprocessed precursor]

CRC64: 58B897197D621AB1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSAMPDVP APLTNLQFKY TKIFINNEWH SSVSGKKFPV FNPATEEKLC EVEEGDKEDV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLIERDR LLLATMEAMN GGKLFSNAYL 

       130        140        150        160        170        180 
MDLGGCIKTL RYCAGWADKI QGRTIPMDGN FFTYTRSEPV GVCGQIIPWN FPLLMFLWKI 

       190        200        210        220        230        240 
GPALSCGNTV VVKPAEQTPL TALHMGSLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 

       250        260        270        280        290        300 
KVAFTGSTEV GKLIKEAAGK SNLKRVSLEL GGKSPCIVFA DADLDNAVEF AHQGVFYHQG 

       310        320        330        340        350        360 
QCCIAASRLF VEESIYDEFV RRSVERAKKY VLGNPLTPGV SQGPQIDKEQ YEKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGPWGNKGY FIQPTVFSDV TDDMRIAKEE IFGPVQQIMK FKSLDDVIKR 

       430        440        450        460        470        480 
ANNTFYGLSA GIFTNDIDKA ITVSSALQSG TVWVNCYSVV SAQCPFGGFK MSGNGRELGE 

       490        500 
YGFHEYTEVK TVTIKISQKN S

P51977 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