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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Ovis aries (Sheep)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid.

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

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

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

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:ALDH1
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 501500Retinal dehydrogenase 1PRO_0000056420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei91 – 911N6-acetyllysineBy similarity
Modified residuei128 – 1281N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity
Modified residuei337 – 3371PhosphothreonineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei367 – 3671N6-acetyllysineBy similarity
Modified residuei410 – 4101N6-acetyllysineBy similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei419 – 4191N6-acetyllysineBy similarity
Modified residuei495 – 4951N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP51977.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi28 – 303Combined sources
Beta strandi37 – 415Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 536Combined sources
Helixi57 – 7014Combined sources
Helixi76 – 794Combined sources
Helixi82 – 9817Combined sources
Helixi100 – 11112Combined sources
Helixi115 – 1206Combined sources
Helixi122 – 13615Combined sources
Helixi137 – 1393Combined sources
Beta strandi142 – 1454Combined sources
Beta strandi148 – 15912Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 18514Combined sources
Beta strandi189 – 1935Combined sources
Helixi200 – 21213Combined sources
Beta strandi218 – 2214Combined sources
Turni226 – 2283Combined sources
Helixi229 – 2346Combined sources
Beta strandi241 – 2466Combined sources
Helixi248 – 26013Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi275 – 2784Combined sources
Helixi284 – 29613Combined sources
Helixi297 – 3004Combined sources
Beta strandi308 – 3125Combined sources
Helixi313 – 32715Combined sources
Helixi348 – 36417Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi385 – 3895Combined sources
Helixi395 – 3984Combined sources
Beta strandi403 – 4119Combined sources
Helixi414 – 4229Combined sources
Beta strandi428 – 4336Combined sources
Helixi437 – 44610Combined sources
Beta strandi450 – 4556Combined sources
Helixi470 – 4723Combined sources
Beta strandi473 – 4753Combined sources
Helixi479 – 4846Combined sources
Beta strandi487 – 4959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXSX-ray2.35A/B/C/D1-501[»]
5ABMX-ray1.70A/B/C/D2-501[»]
5AC0X-ray1.90A/B1-501[»]
5AC1X-ray2.08A/B/C/D1-501[»]
ProteinModelPortaliP51977.
SMRiP51977. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51977.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000118999.
HOVERGENiHBG000097.
KOiK07249.
OMAiSSRETSM.

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.

P51977-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSAMPDVP APLTNLQFKY TKIFINNEWH SSVSGKKFPV FNPATEEKLC
60 70 80 90 100
EVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLN KLADLIERDR
110 120 130 140 150
LLLATMEAMN GGKLFSNAYL MDLGGCIKTL RYCAGWADKI QGRTIPMDGN
160 170 180 190 200
FFTYTRSEPV GVCGQIIPWN FPLLMFLWKI GPALSCGNTV VVKPAEQTPL
210 220 230 240 250
TALHMGSLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD KVAFTGSTEV
260 270 280 290 300
GKLIKEAAGK SNLKRVSLEL GGKSPCIVFA DADLDNAVEF AHQGVFYHQG
310 320 330 340 350
QCCIAASRLF VEESIYDEFV RRSVERAKKY VLGNPLTPGV SQGPQIDKEQ
360 370 380 390 400
YEKILDLIES GKKEGAKLEC GGGPWGNKGY FIQPTVFSDV TDDMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GIFTNDIDKA ITVSSALQSG
460 470 480 490 500
TVWVNCYSVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTIKISQKN

S
Length:501
Mass (Da):54,825
Last modified:January 23, 2007 - v2
Checksum:i58B897197D621AB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12761 mRNA. Translation: AAA85435.1.
PIRiS78582. S14752.
RefSeqiNP_001009778.1. NM_001009778.1.
UniGeneiOar.873.

Genome annotation databases

EnsembliENSOART00000013815; ENSOARP00000013613; ENSOARG00000012705.
GeneIDi443343.
KEGGioas:443343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12761 mRNA. Translation: AAA85435.1.
PIRiS78582. S14752.
RefSeqiNP_001009778.1. NM_001009778.1.
UniGeneiOar.873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXSX-ray2.35A/B/C/D1-501[»]
5ABMX-ray1.70A/B/C/D2-501[»]
5AC0X-ray1.90A/B1-501[»]
5AC1X-ray2.08A/B/C/D1-501[»]
ProteinModelPortaliP51977.
SMRiP51977. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP51977.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOART00000013815; ENSOARP00000013613; ENSOARG00000012705.
GeneIDi443343.
KEGGioas:443343.

Organism-specific databases

CTDi216.

Phylogenomic databases

GeneTreeiENSGT00760000118999.
HOVERGENiHBG000097.
KOiK07249.
OMAiSSRETSM.

Enzyme and pathway databases

UniPathwayiUPA00912.

Miscellaneous databases

EvolutionaryTraceiP51977.

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]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterisation of the cDNA for sheep liver cytosolic aldehyde dehydrogenase."
    Stayner C.K., Tweedie J.W.
    Adv. Exp. Med. Biol. 372:61-66(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases."
    Moore S.A., Baker H.M., Blythe T.J., Kitson K.E., Kitson T.M., Baker E.N.
    Structure 6:1541-1551(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    Tissue: Liver.

Entry informationi

Entry nameiAL1A1_SHEEP
AccessioniPrimary (citable) accession number: P51977
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.