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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Equus caballus (Horse)
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 (By similarity).By similarity

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
Sitei169 – 1691Transition state stabilizerBy similarity
Active sitei268 – 2681Proton acceptorPROSITE-ProRule annotation
Active sitei302 – 3021NucleophilePROSITE-ProRule annotation
Binding sitei455 – 4551NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi245 – 2506NADBy 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
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Retinal dehydrogenase 1PRO_0000056414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylserine1 Publication
Modified residuei90 – 901N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei251 – 2511N6-acetyllysineBy similarity
Modified residuei336 – 3361PhosphothreonineBy similarity
Modified residuei352 – 3521N6-acetyllysineBy similarity
Modified residuei366 – 3661N6-acetyllysineBy similarity
Modified residuei409 – 4091N6-acetyllysineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Modified residuei418 – 4181N6-acetyllysineBy similarity
Modified residuei434 – 4341N6-acetyllysineBy similarity
Modified residuei494 – 4941N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15437.
PRIDEiP15437.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017558.

Structurei

3D structure databases

ProteinModelPortaliP15437.
SMRiP15437. Positions 7-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP15437.

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.

P15437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SSSGTPDLPV LLTDLKFQYT KIFINNEWHD SVSGKKFPVF NPATEEKLCE
60 70 80 90 100
VEEGDKEDVN KAVAAARQAF QIGSPWRTMD ASERGRLLYK LADLVERDRL
110 120 130 140 150
ILATMESMNG GKLFSNAYLM DLGGCLKTLR YCAGWADKIQ GRTIPSDGNF
160 170 180 190 200
FTYTRHEPVG VCGQILPWNF PLLMFLWKIA PALSCGNTVV VKPAEQTPLS
210 220 230 240 250
ALHVATLIKE AGFPPGVVNI VPGYGPTAGA AISSHMDIDK VAFTGSTEVG
260 270 280 290 300
KLIKEAAGKS NLKRVTLELG GKSPFIVFAD ADLETALEVT HQALFYHQGQ
310 320 330 340 350
CCVAASRLFV EESIYDEFVR RSVERAKKYV LGNPLTPGVS QGPQIDKEQY
360 370 380 390 400
DKILDLIESG KKEGAKLECG GGPWGNKGYF IQPTVFSNVS DEMRIAKEEI
410 420 430 440 450
FGPVQQIMKF KSLDDVIKRA NNTTYGLFAG SFTKDLDKAI TVSAALQAGT
460 470 480 490 500
VWVNCYGVVS AQCPFGGFKM SGNGREMGEY GFHEYTEVKT VTVKISQKNS
Length:500
Mass (Da):54,744
Last modified:April 1, 1990 - v1
Checksum:iA438E4204BEF7340
GO

Sequence databases

PIRiS02302.

Cross-referencesi

Sequence databases

PIRiS02302.

3D structure databases

ProteinModelPortaliP15437.
SMRiP15437. Positions 7-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017558.

Proteomic databases

PaxDbiP15437.
PRIDEiP15437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP15437.

Enzyme and pathway databases

UniPathwayiUPA00912.

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. "The cytoplasmic isoenzyme of horse liver aldehyde dehydrogenase. Relationship to the corresponding human isoenzyme."
    von Bahr-Lindstroem H., Hempel J., Joernvall H.
    Eur. J. Biochem. 141:37-42(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiAL1A1_HORSE
AccessioniPrimary (citable) accession number: P15437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 17, 2016
This is version 99 of the entry and version 1 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

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.