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O75452 (RDH16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 16

EC=1.1.-.-
Alternative name(s):
Microsomal NAD(+)-dependent retinol dehydrogenase 4
Short name=RoDH-4
Sterol/retinol dehydrogenase
Gene names
Name:RDH16
Synonyms:RODH4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction. Ref.1 Ref.2 Ref.4

Enzyme regulation

Inhibited by citral, perillyl alcohol, geraniol, farnesol and geranyl geraniol. Ref.1

Subcellular location

Microsome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein Potential Ref.1 Ref.2 Ref.4.

Tissue specificity

Highly expressed in adult liver (at protein level). Detected in endometrium, liver and foreskin. Detected in the spineous layers of adult skin, and at lower levels in basal and granular skin layers. Detected in fetal liver and lung. Ref.1 Ref.2 Ref.3

Induction

Transiently up-regulated by retinoic acid. Ref.1 Ref.2

Post-translational modification

Not N-glycosylated. Ref.4

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.14 µM for androsterone Ref.1

KM=0.22 µM for androstanediol

KM=0.80 µM for dihydrotestosterone

KM=0.13 µM for NAD

KM=190 µM for NADP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Retinol dehydrogenase 16
PRO_0000307693

Regions

Topological domain1 – 288288Cytoplasmic Potential
Transmembrane289 – 30921Helical; Anchor for type IV membrane protein; Potential
Topological domain310 – 3178Lumenal Potential
Nucleotide binding33 – 5725NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site1641Substrate By similarity

Experimental info

Sequence conflict130 – 1312FV → LL in AAC72923. Ref.2
Sequence conflict1471S → N in AAC72923. Ref.2
Sequence conflict1541R → K in AAC39922. Ref.1
Sequence conflict1631S → F in AAC72923. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O75452 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: F9208C22B0515CFD

FASTA31735,673
        10         20         30         40         50         60 
MWLYLAVFVG LYYLLHWYRE RQVLSHLRDK YVFITGCDSG FGKLLARQLD ARGLRVLAAC 

        70         80         90        100        110        120 
LTEKGAEQLR GQTSDRLETV TLDVTKTESV AAAAQWVKEC VRDKGLWGLV NNAGISLPTA 

       130        140        150        160        170        180 
PNELLTKQDF VTILDVNLLG VIDVTLSLLP LVRRARGRVV NVSSVMGRVS LFGGGYCISK 

       190        200        210        220        230        240 
YGVEAFSDSL RRELSYFGVK VAMIEPGYFK TAVTSKERFL KSFLEIWDRS SPEVKEAYGE 

       250        260        270        280        290        300 
KFVADYKKSA EQMEQKCTQD LSLVTNCMEH ALIACHPRTR YSAGWDAKLL YLPMSYMPTF 

       310 
LVDAIMYWVS PSPAKAL 

« Hide

References

[1]"cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids."
Gough W.H., VanOoteghem S., Sint T., Kedishvili N.Y.
J. Biol. Chem. 273:19778-19785(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes."
Jurukovski V., Markova N.G., Karaman-Jurukovska N., Randolph R.K., Su J., Napoli J.L., Simon M.
Mol. Genet. Metab. 67:62-73(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
Tissue: Keratinocyte.
[3]"Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria."
Cain J.M., Zaino R., Shearer D., Bennett R.A., Olt G., Weisz J.
Am. J. Obstet. Gynecol. 186:675-683(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4."
Lapshina E.A., Belyaeva O.V., Chumakova O.V., Kedishvili N.Y.
Biochemistry 42:776-784(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LACK OF GLYCOSYLATION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF057034 mRNA. Translation: AAC39922.1.
AF086735 mRNA. Translation: AAC72923.1.
RefSeqNP_003699.3. NM_003708.3.
UniGeneHs.134958.

3D structure databases

ProteinModelPortalO75452.
SMRO75452. Positions 28-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000381206.

PTM databases

PhosphoSiteO75452.

Proteomic databases

PaxDbO75452.
PRIDEO75452.

Protocols and materials databases

DNASU8608.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398138; ENSP00000381206; ENSG00000139547.
GeneID8608.
KEGGhsa:8608.
UCSCuc001smi.4. human.

Organism-specific databases

CTD8608.
GeneCardsGC12M057346.
H-InvDBHIX0036688.
HGNCHGNC:29674. RDH16.
HPAHPA038518.
neXtProtNX_O75452.
PharmGKBPA142671089.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG005482.
InParanoidO75452.
KOK11154.
OMAVKECVRD.
OrthoDBEOG7FXZZX.
PhylomeDBO75452.
TreeFamTF325617.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000139547-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SABIO-RKO75452.

Gene expression databases

BgeeO75452.
CleanExHS_RDH16.
GenevestigatorO75452.

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]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi8608.
NextBio32255.
PROO75452.

Entry information

Entry nameRDH16_HUMAN
AccessionPrimary (citable) accession number: O75452
Secondary accession number(s): Q9UNV2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: March 19, 2014
This is version 93 of the entry and version 2 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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM