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Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Can convert/oxidize retinaldehyde to retinoic acid. Binds free retinal and cellular retinol-binding protein-bound retinal (By similarity). May have a broader specificity and oxidize other aldehydes in vivo (By similarity).By similarity

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.By similarity

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.By similarity
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)DescriptionActionsGraphical viewLength
Sitei170Transition state stabilizerBy similarity1
Active sitei269Proton acceptorPROSITE-ProRule annotation1
Active sitei303NucleophilePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi167 – 170NADBy similarity4
Nucleotide bindingi193 – 196NADBy similarity4
Nucleotide bindingi226 – 227NADBy similarity2
Nucleotide bindingi246 – 247NADBy similarity2
Nucleotide bindingi269 – 271NADBy similarity3
Nucleotide bindingi349 – 353NADBy similarity5
Nucleotide bindingi400 – 402NADBy similarity3

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 1Curated (EC:1.2.1.-By similarity, EC:1.2.1.36By similarity)
Short name:
RALDH 1Curated
Short name:
RalDH1Curated
Alternative name(s):
Aldehyde dehydrogenase, cytosolic1 Publication
Gene namesi
Name:ALDH1A1By similarity
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000564142 – 501Retinal dehydrogenase 1Add BLAST500

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei91N6-acetyllysineBy similarity1
Modified residuei128N6-acetyllysineBy similarity1
Modified residuei252N6-acetyllysineBy similarity1
Modified residuei337PhosphothreonineBy similarity1
Modified residuei353N6-acetyllysineBy similarity1
Modified residuei367N6-acetyllysineBy similarity1
Modified residuei410N6-acetyllysineBy similarity1
Modified residuei413PhosphoserineBy similarity1
Modified residuei419N6-acetyllysineBy similarity1
Modified residuei435N6-acetyllysineBy similarity1
Modified residuei495N6-acetyllysineBy similarity1

Post-translational modificationi

The N-terminus is blocked most probably by acetylation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15437.
PeptideAtlasiP15437.
PRIDEiP15437.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017558.

Structurei

3D structure databases

ProteinModelPortaliP15437.
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.

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

P15437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSGTPDLP VLLTDLKFQY TKIFINNEWH DSVSGKKFPV FNPATEEKLC
60 70 80 90 100
EVEEGDKEDV NKAVAAARQA FQIGSPWRTM DASERGRLLY KLADLVERDR
110 120 130 140 150
LILATMESMN GGKLFSNAYL MDLGGCLKTL RYCAGWADKI QGRTIPSDGN
160 170 180 190 200
FFTYTRHEPV GVCGQILPWN FPLLMFLWKI APALSCGNTV VVKPAEQTPL
210 220 230 240 250
SALHVATLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV
260 270 280 290 300
GKLIKEAAGK SNLKRVTLEL GGKSPFIVFA DADLETALEV THQALFYHQG
310 320 330 340 350
QCCVAASRLF VEESIYDEFV RRSVERAKKY VLGNPLTPGV SQGPQIDKEQ
360 370 380 390 400
YDKILDLIES GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV SDEMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDDVIKR ANNTTYGLFA GSFTKDLDKA ITVSAALQAG
460 470 480 490 500
TVWVNCYGVV SAQCPFGGFK MSGNGREMGE YGFHEYTEVK TVTVKISQKN

S
Length:501
Mass (Da):54,875
Last modified:November 30, 2016 - v2
Checksum:i9438E4205E43D109
GO

Sequence databases

PIRiS02302.

Cross-referencesi

Sequence databases

PIRiS02302.

3D structure databases

ProteinModelPortaliP15437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000017558.

Proteomic databases

PaxDbiP15437.
PeptideAtlasiP15437.
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...

Entry informationi

Entry nameiAL1A1_HORSE
AccessioniPrimary (citable) accession number: P15437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 30, 2016
Last modified: November 30, 2016
This is version 102 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

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.