ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P27463


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AL1A1_CHICK
Primary accession number P27463
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 62)
Name and origin of the protein
Protein name Retinal dehydrogenase 1
Synonyms RALDH 1
RalDH1
EC 1.2.1.36
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
ALHDII
ALDH-E1
Gene name
Name: ALDH1A1
From
Gallus gallus (Chicken) [TaxID: 9031] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryonic retina;
DOI=10.1016/S0014-4835(05)80219-2; PubMed=1559558 [NCBI, ExPASy, EBI, Israel, Japan]
Godbout R.;
"High levels of aldehyde dehydrogenase transcripts in the undifferentiated chick retina.";
Exp. Eye Res. 54:297-305(1992).
Comments
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
X58869; CAA41679.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S14629; S14629.
RefSeq NP_989908.1; -.
UniGene Gga.4119
3D structure databases
HSSP P51977; 1BXS. [HSSP ENTRY / PDB]
ModBase P27463.
Ontologies
GO
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.
BLOCKS P27463.
ProtoNet P27463.
Genome annotation databases
Ensembl ENSGALG00000015147; Gallus gallus. [Contig view]
GeneID 395264; -.
KEGG gga:395264; -.
Phylogenomic databases
HOVERGEN P27463; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   509  509     Retinal dehydrogenase 1. PRO_0000056421
NP_BIND   254   259  6     NAD (By similarity). 
ACT_SITE   277   277        Proton acceptor (By similarity). 
ACT_SITE   311   311        Nucleophile (By similarity). 
SITE   178   178  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 509 AA [This is the length of the unprocessed precursor] Molecular weight: 55809 Da [This is the MW of the unprocessed precursor] CRC64: 7771181FA2F05DA9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKQGSPSNP APVLPALPEP LKDLKIKYTK IFINNEWHDS VSGKKFEVFN PANEEKICEV 

        70         80         90        100        110        120 
AEGDKADIDK AVKAARKAFE LGSPWRTMDA SERGRLLNKL ADLVERDRLT LATMEAIDGG 

       130        140        150        160        170        180 
KLFSTAYLMD LGACIKTIRY CAGWADKIHG RTVPMDGNFF TFTRHEPVGV CGQIIPWNFP 

       190        200        210        220        230        240 
LVMFIWKIAP ALCCGNTVVV KPAEQTPLSA LYMGSLIKEA GFPPGVVNIV PGFGPTAGAA 

       250        260        270        280        290        300 
ISHHMDIDKV SFTGSTEVGK LIKEAAGKTN LKRVTLELGG KSPNIIFADA DLDEAAEFAH 

       310        320        330        340        350        360 
IGLFYHQGQC CIAGSRIFVE EPIYDEFVRR SIERAKKYTL GDPLLPGVQQ GPQIDKEQFQ 

       370        380        390        400        410        420 
KILDLIESGK KEGAKLECGG GPWGNKGYFI QPTVFSNVTD DMRIAKEEIF GPVQQIMKFK 

       430        440        450        460        470        480 
TIDEVIKRAN NTTYGLAAAV FTKDIDKALT FASALQAGTV WVNCYSAFSA QCPFGGFKMS 

       490        500 
GNGRELGEYG LQEYTEVKTV TIKIPQKNS 

P27463 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!