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Protein

Retinol dehydrogenase 12

Gene

RDH12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei175SubstrateBy similarity1
Active sitei200Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 52NADPBy similarity7

GO - Molecular functioni

  • NADP-retinol dehydrogenase activity Source: Reactome
  • retinol dehydrogenase activity Source: UniProtKB

GO - Biological processi

  • photoreceptor cell maintenance Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • retinoid metabolic process Source: Reactome
  • retinol metabolic process Source: UniProtKB
  • visual perception Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processSensory transduction, Vision
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000139988-MONOMER.
BRENDAi1.1.1.105. 2681.
1.1.1.300. 2681.
ReactomeiR-HSA-2453864. Retinoid cycle disease events.
R-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).

Chemistry databases

SwissLipidsiSLP:000001789.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol dehydrogenase 12 (EC:1.1.1.-)
Alternative name(s):
All-trans and 9-cis retinol dehydrogenase
Short chain dehydrogenase/reductase family 7C member 2
Gene namesi
Name:RDH12
Synonyms:SDR7C2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000139988.9.
HGNCiHGNC:19977. RDH12.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Involvement in diseasei

Leber congenital amaurosis 13 (LCA13)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
See also OMIM:612712
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02085849T → M in LCA13; aberrant activity in interconverting isomers of retinol and retinal; there is differing activity profiles associated with each of the alleles of the R-161-Q polymorphism; genetic background may act as a modifier of mutation effect. 1 PublicationCorresponds to variant dbSNP:rs28940314Ensembl.1
Natural variantiVAR_02085951I → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894473Ensembl.1
Natural variantiVAR_06719379A → V Found in a patient with LCA13. 1 PublicationCorresponds to variant dbSNP:rs763414313Ensembl.1
Natural variantiVAR_02086099L → I in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs28940315Ensembl.1
Natural variantiVAR_020861151H → D in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs104894475Ensembl.1
Natural variantiVAR_020862151H → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894475Ensembl.1
Natural variantiVAR_020863175S → P in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894472Ensembl.1
Natural variantiVAR_020864226Y → C in LCA13; diminished activity in interconverting isomers of retinol and retinal. 1 PublicationCorresponds to variant dbSNP:rs28940313Ensembl.1
Natural variantiVAR_020865230P → A in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894476Ensembl.1
Retinitis pigmentosa 53 (RP53)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
See also OMIM:612712
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06416676G → R in RP53. 1 PublicationCorresponds to variant dbSNP:rs368489658Ensembl.1
Natural variantiVAR_064169126A → V in RP53. 1 PublicationCorresponds to variant dbSNP:rs202126574Ensembl.1

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

Organism-specific databases

DisGeNETi145226.
GeneReviewsiRDH12.
MalaCardsiRDH12.
MIMi612712. phenotype.
OpenTargetsiENSG00000139988.
Orphaneti65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
PharmGKBiPA134864793.

Chemistry databases

DrugBankiDB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRDH12.
DMDMi116242750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000547661 – 316Retinol dehydrogenase 12Add BLAST316

Proteomic databases

MaxQBiQ96NR8.
PaxDbiQ96NR8.
PeptideAtlasiQ96NR8.
PRIDEiQ96NR8.

PTM databases

iPTMnetiQ96NR8.
PhosphoSitePlusiQ96NR8.

Expressioni

Tissue specificityi

Widely expressed, mostly in eye, kidney, brain, skeletal muscle and stomach.

Gene expression databases

BgeeiENSG00000139988.
CleanExiHS_RDH12.
ExpressionAtlasiQ96NR8. baseline and differential.
GenevisibleiQ96NR8. HS.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi126895. 30 interactors.
IntActiQ96NR8. 5 interactors.
MINTiMINT-3056571.
STRINGi9606.ENSP00000267502.

Structurei

3D structure databases

ProteinModelPortaliQ96NR8.
SMRiQ96NR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1208. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000119068.
HOVERGENiHBG078800.
InParanoidiQ96NR8.
KOiK11153.
OMAiVHHAGKI.
OrthoDBiEOG091G0FGA.
PhylomeDBiQ96NR8.
TreeFamiTF105429.

Family and domain databases

InterProiView protein in InterPro
IPR036291. NAD(P)-bd_dom_sf.
IPR002347. SDR_fam.
PfamiView protein in Pfam
PF00106. adh_short. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96NR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVTLGLLTS FFSFLYMVAP SIRKFFAGGV CRTNVQLPGK VVVITGANTG
60 70 80 90 100
IGKETARELA SRGARVYIAC RDVLKGESAA SEIRVDTKNS QVLVRKLDLS
110 120 130 140 150
DTKSIRAFAE GFLAEEKQLH ILINNAGVMM CPYSKTADGF ETHLGVNHLG
160 170 180 190 200
HFLLTYLLLE RLKVSAPARV VNVSSVAHHI GKIPFHDLQS EKRYSRGFAY
210 220 230 240 250
CHSKLANVLF TRELAKRLQG TGVTTYAVHP GVVRSELVRH SSLLCLLWRL
260 270 280 290 300
FSPFVKTARE GAQTSLHCAL AEGLEPLSGK YFSDCKRTWV SPRARNNKTA
310
ERLWNVSCEL LGIRWE
Length:316
Mass (Da):35,094
Last modified:October 17, 2006 - v3
Checksum:iEA0915E1E484879B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06416347A → T in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs761231974Ensembl.1
Natural variantiVAR_02085849T → M in LCA13; aberrant activity in interconverting isomers of retinol and retinal; there is differing activity profiles associated with each of the alleles of the R-161-Q polymorphism; genetic background may act as a modifier of mutation effect. 1 PublicationCorresponds to variant dbSNP:rs28940314Ensembl.1
Natural variantiVAR_02085951I → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894473Ensembl.1
Natural variantiVAR_06416455T → M in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs766631462Ensembl.1
Natural variantiVAR_06416565R → Q1 PublicationCorresponds to variant dbSNP:rs745471670Ensembl.1
Natural variantiVAR_06416676G → R in RP53. 1 PublicationCorresponds to variant dbSNP:rs368489658Ensembl.1
Natural variantiVAR_06719379A → V Found in a patient with LCA13. 1 PublicationCorresponds to variant dbSNP:rs763414313Ensembl.1
Natural variantiVAR_02086099L → I in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs28940315Ensembl.1
Natural variantiVAR_064167101D → N1 PublicationCorresponds to variant dbSNP:rs148334092Ensembl.1
Natural variantiVAR_064168125N → K in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
Natural variantiVAR_064169126A → V in RP53. 1 PublicationCorresponds to variant dbSNP:rs202126574Ensembl.1
Natural variantiVAR_064170145G → E in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
Natural variantiVAR_020861151H → D in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs104894475Ensembl.1
Natural variantiVAR_020862151H → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894475Ensembl.1
Natural variantiVAR_064171155T → I in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs121434337Ensembl.1
Natural variantiVAR_028281161R → Q3 PublicationsCorresponds to variant dbSNP:rs17852293Ensembl.1
Natural variantiVAR_020863175S → P in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894472Ensembl.1
Natural variantiVAR_064172193R → C in retinal dystrophy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs148629905Ensembl.1
Natural variantiVAR_064173206A → D in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
Natural variantiVAR_064174206A → V in retinal dystrophy; unknown pathological significance. 1 Publication1
Natural variantiVAR_020864226Y → C in LCA13; diminished activity in interconverting isomers of retinol and retinal. 1 PublicationCorresponds to variant dbSNP:rs28940313Ensembl.1
Natural variantiVAR_020865230P → A in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894476Ensembl.1
Natural variantiVAR_064175230P → L in retinal dystrophy; unknown pathological significance. 1 Publication1
Natural variantiVAR_064176234R → H in retinal dystrophy; unknown pathological significance; exhibits a loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs750636662Ensembl.1
Natural variantiVAR_064177239R → W in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs751589863Ensembl.1
Natural variantiVAR_064178274L → P in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
Natural variantiVAR_064179285C → Y in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK054835 mRNA. Translation: BAB70811.1.
AK315462 mRNA. Translation: BAG37849.1.
AL049779 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80951.1.
BC025724 mRNA. Translation: AAH25724.1.
CCDSiCCDS9787.1.
RefSeqiNP_689656.2. NM_152443.2.
UniGeneiHs.415322.
Hs.739915.

Genome annotation databases

EnsembliENST00000267502; ENSP00000267502; ENSG00000139988.
ENST00000551171; ENSP00000449079; ENSG00000139988.
GeneIDi145226.
KEGGihsa:145226.
UCSCiuc001xjz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRDH12_HUMAN
AccessioniPrimary (citable) accession number: Q96NR8
Secondary accession number(s): B2RDA2, Q8TAW6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 17, 2006
Last modified: November 22, 2017
This is version 148 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families