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Q8IZV5 (RDH10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol dehydrogenase 10

EC=1.1.1.300
Gene names
Name:RDH10
ORF Names:UNQ9375/PRO34191
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinol to all-trans-retinal. Has no detectable activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol. Ref.1

Catalytic activity

All-trans-retinol + NADP+ = all-trans-retinal + NADPH. Ref.1

Pathway

Cofactor metabolism; retinol metabolism.

Subcellular location

Microsome membrane; Single-pass membrane protein Potential. Endoplasmic reticulum membrane; Single-pass membrane protein Potential Ref.1.

Tissue specificity

Detected in retina, kidney, liver, small intestine, placenta, lung, heart and skeletal muscle. Ref.1 Ref.4

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbud elongation involved in lung branching

Inferred from electronic annotation. Source: Ensembl

ear development

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye development

Inferred from electronic annotation. Source: Ensembl

embryonic forelimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic viscerocranium morphogenesis

Inferred from electronic annotation. Source: Ensembl

gonad development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

metanephros development

Inferred from electronic annotation. Source: Ensembl

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

nose development

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

primary lung bud formation

Inferred from electronic annotation. Source: Ensembl

retinal metabolic process

Inferred from direct assay PubMed 19458327. Source: UniProtKB

retinoic acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

retinol metabolic process

Inferred from direct assay PubMed 19458327. Source: UniProtKB

visual perception

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 19458327. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from direct assay PubMed 19458327. Source: UniProtKB

   Molecular_functionNADP-retinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

retinol dehydrogenase activity

Inferred from direct assay PubMed 19458327. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Retinol dehydrogenase 10
PRO_0000307682

Regions

Transmembrane3 – 2321Helical; Signal-anchor; Potential
Nucleotide binding40 – 6425NADP By similarity

Sites

Active site2101Proton acceptor By similarity
Binding site1971Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8IZV5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D10ABE05E7D11FC6

FASTA34138,087
        10         20         30         40         50         60 
MNIVVEFFVV TFKVLWAFVL AAARWLVRPK EKSVAGQVCL ITGAGSGLGR LFALEFARRR 

        70         80         90        100        110        120 
ALLVLWDINT QSNEETAGMV RHIYRDLEAA DAAALQAGNG EEEILPHCNL QVFTYTCDVG 

       130        140        150        160        170        180 
KRENVYLTAE RVRKEVGEVS VLVNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF 

       190        200        210        220        230        240 
LPTMLEINHG HIVTVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA AEKDGIKTTL 

       250        260        270        280        290        300 
VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMKAI LTDQPMICTP RLMYIVTFMK 

       310        320        330        340 
SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNEAKNG I 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel all-trans retinol short-chain dehydrogenase/reductase from the RPE."
Wu B.X., Chen Y., Chen Y., Fan J., Rohrer B., Crouch R.K., Ma J.-X.
Invest. Ophthalmol. Vis. Sci. 43:3365-3372(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Retina.
[2]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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: Eye.
[4]"Genomic organization and transcription of the human retinol dehydrogenase 10 (RDH10) gene."
Picozzi P., Marozzi A., Fornasari D., Benfante R., Barisani D., Meneveri R., Ginelli E.
FEBS Lett. 554:59-66(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF456765 mRNA. Translation: AAN64747.1.
AY358270 mRNA. Translation: AAQ88637.1.
BC067131 mRNA. Translation: AAH67131.1.
RefSeqNP_742034.1. NM_172037.4.
UniGeneHs.244940.

3D structure databases

ProteinModelPortalQ8IZV5.
SMRQ8IZV5. Positions 30-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127600. 2 interactions.
STRING9606.ENSP00000240285.

PTM databases

PhosphoSiteQ8IZV5.

Polymorphism databases

DMDM74750799.

Proteomic databases

PaxDbQ8IZV5.
PRIDEQ8IZV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240285; ENSP00000240285; ENSG00000121039.
GeneID157506.
KEGGhsa:157506.
UCSCuc003xzi.3. human.

Organism-specific databases

CTD157506.
GeneCardsGC08P074207.
HGNCHGNC:19975. RDH10.
MIM607599. gene.
neXtProtNX_Q8IZV5.
PharmGKBPA134989620.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG051352.
InParanoidQ8IZV5.
KOK11151.
OMAMNNNEAK.
OrthoDBEOG7Z3F50.
PhylomeDBQ8IZV5.
TreeFamTF312837.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000121039-MONOMER.
BRENDA1.1.1.105. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
UniPathwayUPA00912.

Gene expression databases

ArrayExpressQ8IZV5.
BgeeQ8IZV5.
CleanExHS_RDH10.
GenevestigatorQ8IZV5.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi157506.
NextBio87473.
PROQ8IZV5.
SOURCESearch...

Entry information

Entry nameRDH10_HUMAN
AccessionPrimary (citable) accession number: Q8IZV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM