[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retina; PubMed=7786847 [NCBI, ExPASy, EBI, Israel, Japan] Saari J.C., Champer R.J., Asson-Batres M.A., Garwin G.G., Huang J., Crabb J.W., Milam A.H.; "Characterization and localization of an aldehyde dehydrogenase to amacrine cells of bovine retina."; Vis. Neurosci. 12:263-272(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Fetal liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity).
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

L36128; AAA74234.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT030667; ABS44983.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105193; AAI05194.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776664.1; -.

UniGene

Bt.4732

3D structure databases

HSSP

P51977; 1BXS. [HSSP ENTRY / PDB]

ModBase

P48644.

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

P48644.

Genome annotation databases

Ensembl

ENSBTAG00000008103; Bos taurus. [Contig view]

GeneID

281615; -.

KEGG

bta:281615; -.

Phylogenomic databases

HOVERGEN

P48644; -.

Other

ProtoNet

P48644.

UniRef

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

Keywords

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_0000056413`
`NP_BIND`	`246 251`	`6`	`NAD (By similarity).`
`ACT_SITE`	`269 269`		`Proton acceptor (By similarity).`
`ACT_SITE`	`303 303`		`Nucleophile (By similarity).`
`SITE`	`170 170`	`1`	`Transition state stabilizer (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`CONFLICT`	`67 67`		`A -> V (in Ref. 1; AAA74234).`

Sequence information

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

Molecular weight: 54806 Da [This is the MW of the unprocessed precursor]

CRC64: C9025D7034BC7F95 [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 KLADLIERDH 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

P48644 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