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P51647

- AL1A1_RAT

UniProt

P51647 - AL1A1_RAT

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Protein
Retinal dehydrogenase 1
Gene
Aldh1a1, Aldh
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Is capable of converting 9-cis and all-trans retinal to corresponding retinoic acid with high efficiency, 9-cis retinal being 2-fold more active than all-trans retinal.

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Enzyme regulationi

Inhibited by chloral hydrate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei170 – 1701Transition state stabilizer By similarity
Active sitei269 – 2691Proton acceptor By similarity
Active sitei303 – 3031Nucleophile By similarity
Binding sitei456 – 4561NAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2516NAD By similarity

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: RGD
  2. aldehyde dehydrogenase (NAD) activity Source: RGD
  3. benzaldehyde dehydrogenase (NAD+) activity Source: RGD
  4. identical protein binding Source: RGD
  5. retinal dehydrogenase activity Source: RGD

GO - Biological processi

  1. 9-cis-retinoic acid biosynthetic process Source: Ensembl
  2. 9-cis-retinoic acid metabolic process Source: RGD
  3. estrous cycle phase Source: RGD
  4. kidney development Source: RGD
  5. liver development Source: RGD
  6. midgut development Source: RGD
  7. optic cup morphogenesis involved in camera-type eye development Source: Ensembl
  8. positive regulation of apoptotic process Source: Ensembl
  9. protein homotetramerization Source: RGD
  10. response to drug Source: RGD
  11. response to estradiol Source: RGD
  12. response to ethanol Source: RGD
  13. response to organic cyclic compound Source: RGD
  14. response to oxidative stress Source: RGD
  15. response to retinoic acid Source: RGD
  16. retinoic acid biosynthetic process Source: RGD
  17. retinol metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.36. 5301.
ReactomeiREACT_226337. Ethanol oxidation.
SABIO-RKP51647.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 1 (EC:1.2.1.36)
Short name:
RALDH 1
Short name:
RalDH1
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene namesi
Name:Aldh1a1
Synonyms:Aldh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi2087. Aldh1a1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 501500Retinal dehydrogenase 1
PRO_0000056419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine Inferred
Modified residuei91 – 911N6-acetyllysine By similarity
Modified residuei128 – 1281N6-acetyllysine By similarity
Modified residuei252 – 2521N6-acetyllysine By similarity
Modified residuei353 – 3531N6-acetyllysine By similarity
Modified residuei367 – 3671N6-acetyllysine By similarity
Modified residuei410 – 4101N6-acetyllysine By similarity
Modified residuei419 – 4191N6-acetyllysine By similarity
Modified residuei435 – 4351N6-acetyllysine By similarity
Modified residuei495 – 4951N6-acetyllysine By similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP51647.
PRIDEiP51647.

PTM databases

PhosphoSiteiP51647.

Expressioni

Tissue specificityi

Strongly expressed in kidney, lung, testis, intestine, stomach, and trachea, but weakly in the liver.

Gene expression databases

GenevestigatoriP51647.

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP51647.
SMRiP51647. Positions 9-501.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00550000074289.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
KOiK07249.
OMAiEWHDSAS.
OrthoDBiEOG7PS1F7.
PhylomeDBiP51647.
TreeFamiTF300455.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51647-1 [UniParc]FASTAAdd to Basket

« Hide

MSSPAQPAVP APLANLKIQH TKIFINNEWH DSVSGKKFPV LNPATEEVIC    50
HVEEGDKADV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLMERDR 100
LLLATIEAIN GGKVFANAYL SDLGGSIKAL KYCAGWADKI HGQTIPSDGD 150
IFTFTRREPI GVCGQIIPWN FPLLMFIWKI GPALSCGNTV VVKPAEQTPL 200
TALHMASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTQV 250
GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDIAVEF AHHGVFYHQG 300
QCCVAASRIF VEESVYDEFV RKSVERAKKY VLGNPLTQGI NQGPQIDKEQ 350
HDKILDLIES GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE 400
IFGPVQQIMK FKSIDDVIKR ANNTTYGLAA GVFTKDLDRA ITVSSALQAG 450
VVWVNCYMIL SAQCPFGGFK MSGNGRELGE HGLYEYTELK TVAMKISQKN 500
S 501
Length:501
Mass (Da):54,459
Last modified:January 23, 2007 - v3
Checksum:iA3614C21BCE7E144
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001R → C in AAA96657. 1 Publication
Sequence conflicti106 – 1061I → M AA sequence 1 Publication
Sequence conflicti170 – 1701N → E in AAA96657. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42009 mRNA. Translation: AAA96657.1.
AF001896 mRNA. Translation: AAC53304.1.
AF001898 mRNA. Translation: AAC53306.1.
AF001897 mRNA. Translation: AAC53305.1.
U79118 mRNA. Translation: AAB63423.1.
BC061526 mRNA. Translation: AAH61526.1.
PIRiJC4524.
JC5553.
RefSeqiNP_071852.2. NM_022407.3.
XP_006231218.1. XM_006231156.1.
XP_006231219.1. XM_006231157.1.
XP_006231220.1. XM_006231158.1.
UniGeneiRn.6132.

Genome annotation databases

EnsembliENSRNOT00000024000; ENSRNOP00000024000; ENSRNOG00000017619.
GeneIDi24188.
KEGGirno:24188.
UCSCiRGD:2087. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42009 mRNA. Translation: AAA96657.1 .
AF001896 mRNA. Translation: AAC53304.1 .
AF001898 mRNA. Translation: AAC53306.1 .
AF001897 mRNA. Translation: AAC53305.1 .
U79118 mRNA. Translation: AAB63423.1 .
BC061526 mRNA. Translation: AAH61526.1 .
PIRi JC4524.
JC5553.
RefSeqi NP_071852.2. NM_022407.3.
XP_006231218.1. XM_006231156.1.
XP_006231219.1. XM_006231157.1.
XP_006231220.1. XM_006231158.1.
UniGenei Rn.6132.

3D structure databases

ProteinModelPortali P51647.
SMRi P51647. Positions 9-501.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P51647.
ChEMBLi CHEMBL2931.

PTM databases

PhosphoSitei P51647.

Proteomic databases

PaxDbi P51647.
PRIDEi P51647.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000024000 ; ENSRNOP00000024000 ; ENSRNOG00000017619 .
GeneIDi 24188.
KEGGi rno:24188.
UCSCi RGD:2087. rat.

Organism-specific databases

CTDi 216.
RGDi 2087. Aldh1a1.

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00550000074289.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
KOi K07249.
OMAi EWHDSAS.
OrthoDBi EOG7PS1F7.
PhylomeDBi P51647.
TreeFami TF300455.

Enzyme and pathway databases

UniPathwayi UPA00912 .
BRENDAi 1.2.1.36. 5301.
Reactomei REACT_226337. Ethanol oxidation.
SABIO-RK P51647.

Miscellaneous databases

NextBioi 602555.

Gene expression databases

Genevestigatori P51647.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation."
    Bhat P.V., Labrecque J., Boutin J.-M., Lacroix A., Yoshida A.
    Gene 166:303-306(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  2. "A preliminary report on the cloning of a constitutively expressed rat liver cytosolic ALDH cDNA by PCR."
    Kathmann E.C., Lipsky J.J.
    Adv. Exp. Med. Biol. 414:69-72(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic aldehyde dehydrogenase."
    Kathmann E.C., Lipsky J.J.
    Biochem. Biophys. Res. Commun. 236:527-531(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  4. "Cloning of a rat cDNA encoding retinal dehydrogenase isozyme type I and its expression in E. coli."
    Napoli J.L., Penzes P., Wang X., Sperkova Z.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  6. "A novel isoenzyme of aldehyde dehydrogenase specifically involved in the biosynthesis of 9-cis and all-trans retinoic acid."
    Labrecque J., Dumas F., Lacroix A., Bhat P.V.
    Biochem. J. 305:681-684(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19; 80-91; 96-121; 205-225; 237-258 AND 394-438.
    Strain: Sprague-Dawley.
    Tissue: Kidney.

Entry informationi

Entry nameiAL1A1_RAT
AccessioniPrimary (citable) accession number: P51647
Secondary accession number(s): O09184
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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