[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Lens; DOI=10.1074/jbc.271.26.15623; PubMed=8663049 [NCBI, ExPASy, EBI, Israel, Japan] Graham C., Hodin J., Wistow G.; "A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin."; J. Biol. Chem. 271:15623-15628(1996).
[2]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, AND HOMOTETRAMERIZATION. DOI=10.1021/bi027367w; PubMed=12693930 [NCBI, ExPASy, EBI, Israel, Japan] Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., Wistow G.; "Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens."; Biochemistry 42:4349-4356(2003).

Comments

FUNCTION: Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.
CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.
PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
TISSUE SPECIFICITY: Eye specific, with very high expression in the lens.
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

U02483; AAB60268.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1O9J; X-ray; 2.40 A; A/B/C/D=1-501.	[ExPASy / RCSB / EBI]
1PEJ; Model; -; A=1-501.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1O9J; -.
1PEJ; -.

ModBase

Q28399.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004029;	Molecular function: aldehyde dehydrogenase (NAD) 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; FALSE_NEG.

Phylogenomic databases

HOVERGEN

Q28399; -.

Other

ProtoNet

Q28399.

UniRef

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

Keywords

3D-structure; Cytoplasm; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 501`	`501`	`Aldehyde dehydrogenase, cytosolic 1.`	`PRO_0000056427`
`NP_BIND`	`246 251`	`6`	`NAD.`
`ACT_SITE`	`269 269`		`Proton acceptor.`
`ACT_SITE`	`303 303`		`Nucleophile.`
`SITE`	`170 170`	`1`	`Transition state stabilizer.`
`STRAND`	`22 25`	`4`
`STRAND`	`28 30`	`3`
`STRAND`	`37 41`	`5`
`TURN`	`43 45`	`3`
`STRAND`	`48 53`	`6`
`HELIX`	`57 71`	`15`
`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`
`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`	`241 246`	`6`
`HELIX`	`248 260`	`13`
`STRAND`	`265 269`	`5`
`STRAND`	`274 278`	`5`
`HELIX`	`284 296`	`13`
`HELIX`	`297 300`	`4`
`STRAND`	`306 312`	`7`
`HELIX`	`313 326`	`14`
`HELIX`	`348 364`	`17`
`STRAND`	`367 370`	`4`
`STRAND`	`373 379`	`7`
`STRAND`	`385 390`	`6`
`HELIX`	`395 398`	`4`
`STRAND`	`403 411`	`9`
`HELIX`	`414 422`	`9`
`STRAND`	`423 425`	`3`
`STRAND`	`428 433`	`6`
`HELIX`	`437 446`	`10`
`STRAND`	`449 455`	`7`
`HELIX`	`470 472`	`3`
`STRAND`	`473 475`	`3`
`HELIX`	`479 483`	`5`
`HELIX`	`484 486`	`3`
`STRAND`	`487 495`	`9`

Sequence information

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

Molecular weight: 54538 Da [This is the MW of the unprocessed precursor]

CRC64: 9E3D5BBE083ACAD7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC EVEEADKEDV 

        70         80         90        100        110        120 
DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKVFASAYL 

       130        140        150        160        170        180 
MDLDYCIKAL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGLIFPWN APMILLACKI 

       190        200        210        220        230        240 
GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 

       250        260        270        280        290        300 
KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG 

       310        320        330        340        350        360 
QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR 

       430        440        450        460        470        480 
ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE 

       490        500 
YGIHEYTEVK TVTMKISEKN S

Q28399 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