O75452 (RDH16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid metabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular membrane-bounded organelle Traceable author statement Ref.1. Source: ProtInc
Molecular_function	electron carrier activity Traceable author statement Ref.1. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro retinol dehydrogenase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 317	317	Retinol dehydrogenase 16		PRO_0000307693
Regions
	Topological domain	1 – 288	288	Cytoplasmic Potential
	Transmembrane	289 – 309	21	Helical; Anchor for type IV membrane protein; Potential
	Topological domain	310 – 317	8	Lumenal Potential
	Nucleotide binding	33 – 57	25	NAD By similarity
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	164	1	Substrate By similarity
Experimental info
	Sequence conflict	130 – 131	2	FV → LL in AAC72923. Ref.2
	Sequence conflict	147	1	S → N in AAC72923. Ref.2
	Sequence conflict	154	1	R → K in AAC39922. Ref.1
	Sequence conflict	163	1	S → F in AAC72923. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O75452 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: F9208C22B0515CFD	FASTA	317	35,673
	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

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.
IPI	IPI00289551.
RefSeq	NP_003699.3. NM_003708.3.
UniGene	Hs.134958.
3D structure databases
HSSP	HSSP built from PDB template 1FDU based on UniProtKB P14061.
ProteinModelPortal	O75452.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000381206.
PTM databases
PhosphoSite	O75452.
Proteomic databases
PaxDb	O75452.
PRIDE	O75452.
Protocols and materials databases
DNASU	8608.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000398138; ENSP00000381206; ENSG00000139547.
GeneID	8608.
KEGG	hsa:8608.
UCSC	uc001smi.4. human.
Organism-specific databases
CTD	8608.
GeneCards	GC12M057346.
H-InvDB	HIX0036688.
HGNC	HGNC:29674. RDH16.
HPA	HPA038518.
neXtProt	NX_O75452.
PharmGKB	PA142671089.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG005482.
InParanoid	O75452.
KO	K11154.
OMA	RMCHAFV.
OrthoDB	EOG4STS56.
PhylomeDB	O75452.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000139547-MONOMER.
SABIO-RK	O75452.
Gene expression databases
Bgee	O75452.
CleanEx	HS_RDH16.
Genevestigator	O75452.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8608.
NextBio	32255.

Entry information

Entry name

RDH16_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.