Q92781 (RDH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
11-cis retinol dehydrogenase
Short name=11-cis RDH
EC=1.1.1.315

Gene names

Name:	RDH5
Synonyms:	RDH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Active in the presence of NAD as cofactor but not in the presence of NADP.
Catalytic activity	11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH.
Pathway	Cofactor metabolism; retinol metabolism.
Subcellular location	Membrane; Peripheral membrane protein.
Tissue specificity	Abundant in the retinal pigment epithelium.
Involvement in disease	Defects in RDH5 are a cause of retinitis punctata albescens (RPA) [MIM:136880]; also known as fundus albipunctatus (FA). RPA is a rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW visual perception Traceable author statement. Source: ProtInc
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro retinol dehydrogenase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	11-cis retinol dehydrogenase		PRO_0000054758
Regions
	Nucleotide binding	32 – 56	25	NADP By similarity
Sites
	Active site	175	1	Proton acceptor By similarity
	Binding site	163	1	Substrate By similarity
Natural variations
	Natural variant	21	1	R → Q. Corresponds to variant rs3138143 [ dbSNP | Ensembl ].		VAR_052321
	Natural variant	33	1	I → V. Ref.5		VAR_009272
	Natural variant	35	1	G → S in RPA. Ref.7		VAR_016814
	Natural variant	70	1	R → G. Corresponds to variant rs1058635 [ dbSNP | Ensembl ].		VAR_052322
	Natural variant	73	1	S → F in RPA. Ref.5		VAR_009273
	Natural variant	107	1	G → R in RPA; associated with macular dystrophy. Ref.7 Ref.9		VAR_016815
	Natural variant	132	1	V → M in RPA. Ref.7		VAR_016816
	Natural variant	164	1	V → F in RPA. Ref.10		VAR_016817
	Natural variant	177	1	V → G in RPA. Ref.6		VAR_016818
	Natural variant	238	1	G → W in RPA. Ref.4 Ref.5		VAR_009274
	Natural variant	267	1	C → W in RPA. Ref.8		VAR_016819
	Natural variant	280	1	R → H in RPA. Ref.4 Ref.6 Ref.7		VAR_016820
	Natural variant	281	1	Y → H in RPA. Ref.7		VAR_016821
	Natural variant	294	1	A → P in RPA. Ref.4		VAR_016822
	Natural variant	310	1	L → EV in RPA.		VAR_016823
Experimental info
	Sequence conflict	30	1	F → L in AAH28298. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q92781 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 2CE24343F2EEA4B7	FASTA	318	34,979
	10 20 30 40 50 60 MWLPLLLGAL LWAVLWLLRD RQSLPASNAF VFITGCDSGF GRLLALQLDQ RGFRVLASCL 70 80 90 100 110 120 TPSGAEDLQR VASSRLHTTL LDITDPQSVQ QAAKWVEMHV KEAGLFGLVN NAGVAGIIGP 130 140 150 160 170 180 TPWLTRDDFQ RVLNVNTMGP IGVTLALLPL LQQARGRVIN ITSVLGRLAA NGGGYCVSKF 190 200 210 220 230 240 GLEAFSDSLR RDVAHFGIRV SIVEPGFFRT PVTNLESLEK TLQACWARLP PATQAHYGGA 250 260 270 280 290 300 FLTKYLKMQQ RIMNLICDPD LTKVSRCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAS 310 LVDAVLTWVL PKPAQAVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human 11-cis retinol dehydrogenase and organization and chromosomal localization of the corresponding gene." Simon A., Lagercrantz J., Bajalica-Lagercrantz S., Eriksson U. Genomics 36:424-430(1996) [PubMed: 8884265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Retinol dehydrogenase: complete genomic sequence and its relationship to retinitis pigmentosa." Gu S., Jablonka S., Gal A. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"11-cis retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus." Gonzalez-Fernandez F., Kurz D., Bao Y., Newman S., Conway B.P., Young J.E., Han D.P., Khani S.C. Mol. Vis. 5:41-41(1999) [PubMed: 10617778] [Abstract] Cited for: VARIANTS RPA TRP-238; HIS-280 AND PRO-294.
[5]	"Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus." Yamamoto H., Simon A., Eriksson U., Harris E., Berson E.L., Dryja T.P. Nat. Genet. 22:188-191(1999) [PubMed: 10369264] [Abstract] Cited for: VARIANTS RPA PHE-73 AND TRP-238, VARIANT VAL-33.
[6]	"A novel compound heterozygous mutation in the RDH5 gene in a patient with fundus albipunctatus." Kuroiwa S., Kikuchi T., Yoshimura N. Am. J. Ophthalmol. 130:672-675(2000) [PubMed: 11078852] [Abstract] Cited for: VARIANTS RPA GLY-177 AND HIS-280.
[7]	"A high association with cone dystrophy in Fundus albipunctatus caused by mutations of the RDH5 gene." Nakamura M., Hotta Y., Tanikawa A., Terasaki H., Miyake Y. Invest. Ophthalmol. Vis. Sci. 41:3925-3932(2000) [PubMed: 11053295] [Abstract] Cited for: VARIANTS RPA SER-35; ARG-107; MET-132; HIS-280; HIS-281 AND 309-GLU-VAL-310 DELINS.
[8]	"Null mutation in the human 11-cis retinol dehydrogenase gene associated with fundus albipunctatus." Driessen C.A., Janssen B.P., Winkens H.J., Kuhlmann L.D., Van Vugt A.H., Pinckers A.J., Deutman A.F., Janssen J.J. Ophthalmology 108:1479-1484(2001) [PubMed: 11470705] [Abstract] Cited for: VARIANT RPA TRP-267.
[9]	"Macular dystrophy in a Japanese family with fundus albipunctatus." Hotta K., Nakamura M., Kondo M., Ito S., Terasaki H., Miyake Y., Hida T. Am. J. Ophthalmol. 135:917-919(2003) [PubMed: 12788147] [Abstract] Cited for: VARIANT RPA ARG-107.
[10]	"A novel RDH5 gene mutation in a patient with fundus albipunctatus presenting with macular atrophy and fading white dots." Yamamoto H., Yakushijin K., Kusuhara S., Escano M.F., Nagai A., Negi A. Am. J. Ophthalmol. 136:572-574(2003) [PubMed: 12967826] [Abstract] Cited for: VARIANT RPA PHE-164.
+	Additional computationally mapped references.

Web resources

Mutations of the RDH5 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases
EMBL GenBank DDBJ	U43559 mRNA. Translation: AAC50725.1. AF037062 Genomic DNA. Translation: AAC09250.1. BC028298 mRNA. Translation: AAH28298.1.
IPI	IPI00023319.
RefSeq	NP_001186700.1. NM_001199771.1. NP_002896.2. NM_002905.3.
UniGene	Hs.94672.
3D structure databases
ProteinModelPortal	Q92781.
SMR	Q92781. Positions 25-286.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92781.
Polymorphism databases
DMDM	2492753.
Proteomic databases
PRIDE	Q92781.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000257895; ENSP00000257895; ENSG00000135437.
GeneID	5959.
KEGG	hsa:5959.
UCSC	uc001shk.1. human.
Organism-specific databases
CTD	5959.
GeneCards	GC12P056115.
H-InvDB	HIX0010703.
HGNC	HGNC:9940. RDH5.
MIM	136880. phenotype. 601617. gene.
neXtProt	NX_Q92781.
Orphanet	227796. Fundus albipunctatus. 52427. Retinitis punctata albescens.
PharmGKB	PA34308.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00560000076737.
HOGENOM	HBG750976.
HOVERGEN	HBG005482.
InParanoid	Q92781.
OMA	TDPQSVQ.
OrthoDB	EOG4BCDNF.
PhylomeDB	Q92781.
Enzyme and pathway databases
BRENDA	1.1.1.105. 2681.
Gene expression databases
ArrayExpress	Q92781.
Bgee	Q92781.
CleanEx	HS_RDH5.
Genevestigator	Q92781.
GermOnline	ENSG00000135437. Homo sapiens.
Family and domain databases
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00061.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. False negative. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00157. NADH. DB00162. Vitamin A.
NextBio	23204.
SOURCE	Search...

Entry information

Entry name

RDH1_HUMAN

Accession

Primary (citable) accession number: Q92781
Secondary accession number(s): Q8TAI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 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.