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Q96NR8 (RDH12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinol dehydrogenase 12

EC=1.1.1.-
Alternative name(s):
All-trans and 9-cis retinol dehydrogenase
Gene names
Name:RDH12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Tissue specificity

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

Involvement in disease

Leber congenital amaurosis 13 (LCA13) [MIM:612712]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7

Retinitis pigmentosa 53 (RP53) [MIM:612712]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBCP0CG482EBI-3916363,EBI-3390054

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Retinol dehydrogenase 12
PRO_0000054766

Regions

Nucleotide binding46 – 527NADP By similarity

Sites

Active site2001Proton acceptor By similarity
Binding site1751Substrate By similarity

Natural variations

Natural variant471A → T in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064163
Natural variant491T → 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. Ref.7
Corresponds to variant rs28940314 [ dbSNP | Ensembl ].
VAR_020858
Natural variant511I → N in LCA13. Ref.6
VAR_020859
Natural variant551T → M in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064164
Natural variant651R → Q. Ref.8
VAR_064165
Natural variant761G → R in RP53. Ref.10
VAR_064166
Natural variant791A → V Found in a patient with LCA13. Ref.11
VAR_067193
Natural variant991L → I in LCA13; exhibits a profound loss of catalytic activity. Ref.6 Ref.8
Corresponds to variant rs28940315 [ dbSNP | Ensembl ].
VAR_020860
Natural variant1011D → N. Ref.8
VAR_064167
Natural variant1251N → K in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064168
Natural variant1261A → V in RP53. Ref.9
VAR_064169
Natural variant1451G → E in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064170
Natural variant1511H → D in LCA13; exhibits a profound loss of catalytic activity. Ref.6 Ref.8
VAR_020861
Natural variant1511H → N in LCA13. Ref.6
VAR_020862
Natural variant1551T → I in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064171
Natural variant1611R → Q. Ref.1 Ref.8 Ref.11
Corresponds to variant rs17852293 [ dbSNP | Ensembl ].
VAR_028281
Natural variant1751S → P in LCA13. Ref.6
VAR_020863
Natural variant1931R → C in retinal dystrophy; unknown pathological significance. Ref.8
VAR_064172
Natural variant2061A → D in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064173
Natural variant2061A → V in retinal dystrophy; unknown pathological significance. Ref.8
VAR_064174
Natural variant2261Y → C in LCA13; diminished activity in interconverting isomers of retinol and retinal. Ref.7
Corresponds to variant rs28940313 [ dbSNP | Ensembl ].
VAR_020864
Natural variant2301P → A in LCA13. Ref.6
VAR_020865
Natural variant2301P → L in retinal dystrophy; unknown pathological significance. Ref.8
VAR_064175
Natural variant2341R → H in retinal dystrophy; unknown pathological significance; exhibits a loss of catalytic activity. Ref.8
VAR_064176
Natural variant2391R → W in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064177
Natural variant2741L → P in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064178
Natural variant2851C → Y in retinal dystrophy; exhibits a profound loss of catalytic activity. Ref.8
VAR_064179

Sequences

Sequence LengthMass (Da)Tools
Q96NR8 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: EA0915E1E484879B

FASTA31635,094
        10         20         30         40         50         60 
MLVTLGLLTS FFSFLYMVAP SIRKFFAGGV CRTNVQLPGK VVVITGANTG IGKETARELA 

        70         80         90        100        110        120 
SRGARVYIAC RDVLKGESAA SEIRVDTKNS QVLVRKLDLS DTKSIRAFAE GFLAEEKQLH 

       130        140        150        160        170        180 
ILINNAGVMM CPYSKTADGF ETHLGVNHLG HFLLTYLLLE RLKVSAPARV VNVSSVAHHI 

       190        200        210        220        230        240 
GKIPFHDLQS EKRYSRGFAY CHSKLANVLF TRELAKRLQG TGVTTYAVHP GVVRSELVRH 

       250        260        270        280        290        300 
SSLLCLLWRL FSPFVKTARE GAQTSLHCAL AEGLEPLSGK YFSDCKRTWV SPRARNNKTA 

       310 
ERLWNVSCEL LGIRWE 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-161.
Tissue: Cerebellum and Kidney.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain.
[5]"Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina."
Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G., Matsumura M., Nelson P.S., Palczewski K.
J. Biol. Chem. 277:45537-45546(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Retinal dehydrogenase 12 (RDH12) mutations in Leber congenital amaurosis."
Perrault I., Hanein S., Gerber S., Barbet F., Ducroq D., Dollfus H., Hamel C., Dufier J.-L., Munnich A., Kaplan J., Rozet J.-M.
Am. J. Hum. Genet. 75:639-646(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA13 ASN-51; ILE-99; ASN-151; ASP-151; PRO-175 AND ALA-230.
[7]"Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy."
Janecke A.R., Thompson D.A., Utermann G., Becker C., Huebner C.A., Schmid E., McHenry C.L., Nair A.R., Rueschendorf F., Heckenlively J., Wissinger B., Nuernberg P., Gal A.
Nat. Genet. 36:850-854(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LCA13 MET-49 AND CYS-226.
[8]"Retinal degeneration associated with RDH12 mutations results from decreased 11-cis retinal synthesis due to disruption of the visual cycle."
Thompson D.A., Janecke A.R., Lange J., Feathers K.L., Hubner C.A., McHenry C.L., Stockton D.W., Rammesmayer G., Lupski J.R., Antinolo G., Ayuso C., Baiget M., Gouras P., Heckenlively J.R., den Hollander A., Jacobson S.G., Lewis R.A., Sieving P.A. expand/collapse author list , Wissinger B., Yzer S., Zrenner E., Utermann G., Gal A.
Hum. Mol. Genet. 14:3865-3875(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RETINAL DYSTROPHY THR-47; MET-55; ILE-99; LYS-125; GLU-145; ASP-151; ILE-155; CYS-193; ASP-206; VAL-206; LEU-230; HIS-234; TRP-239; PRO-274 AND TYR-285, VARIANTS GLN-65; ASN-101; GLN-161 AND CYS-193, CHARACTERIZATION OF VARIANTS RETINAL DYSTROPHY THR-47; MET-55; ILE-99; LYS-125; GLU-145; ASP-151; ILE-155; CYS-193; ASP-206; VAL-206; LEU-230; HIS-234; TRP-239; PRO-274 AND TYR-285, CHARACTERIZATION OF VARIANT GLN-161.
[9]"Genetic heterogeneity in two consanguineous families segregating early onset retinal degeneration: the pitfalls of homozygosity mapping."
Benayoun L., Spiegel R., Auslender N., Abbasi A.H., Rizel L., Hujeirat Y., Salama I., Garzozi H.J., Allon-Shalev S., Ben-Yosef T.
Am. J. Med. Genet. A 149:650-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP53 VAL-126.
[10]"Molecular characterization of retinitis pigmentosa in Saudi Arabia."
Aldahmesh M.A., Safieh L.A., Alkuraya H., Al-Rajhi A., Shamseldin H., Hashem M., Alzahrani F., Khan A.O., Alqahtani F., Rahbeeni Z., Alowain M., Khalak H., Al-Hazzaa S., Meyer B.F., Alkuraya F.S.
Mol. Vis. 15:2464-2469(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP53 ARG-76.
[11]"Detection of variants in 15 genes in 87 unrelated Chinese patients with Leber congenital amaurosis."
Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q., Hejtmancik J.F.
PLoS ONE 6:E19458-E19458(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-79 AND GLN-161.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9787.1.
RefSeqNP_689656.2. NM_152443.2.
UniGeneHs.415322.

3D structure databases

ProteinModelPortalQ96NR8.
SMRQ96NR8. Positions 33-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126895. 4 interactions.
IntActQ96NR8. 4 interactions.
MINTMINT-3056571.
STRING9606.ENSP00000267502.

Chemistry

DrugBankDB00162. Vitamin A.

PTM databases

PhosphoSiteQ96NR8.

Polymorphism databases

DMDM116242750.

Proteomic databases

MaxQBQ96NR8.
PaxDbQ96NR8.
PRIDEQ96NR8.

Protocols and materials databases

DNASU145226.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267502; ENSP00000267502; ENSG00000139988.
ENST00000539142; ENSP00000438715; ENSG00000139988.
ENST00000551171; ENSP00000449079; ENSG00000139988.
GeneID145226.
KEGGhsa:145226.
UCSCuc001xjz.4. human.

Organism-specific databases

CTD145226.
GeneCardsGC14P068168.
GeneReviewsRDH12.
HGNCHGNC:19977. RDH12.
MIM608830. gene.
612712. phenotype.
neXtProtNX_Q96NR8.
Orphanet65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
PharmGKBPA134864793.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG078800.
InParanoidQ96NR8.
KOK11153.
OMAIAPSIRK.
OrthoDBEOG73Z2TK.
PhylomeDBQ96NR8.
TreeFamTF105429.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000139988-MONOMER.
BRENDA1.1.1.105. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

BgeeQ96NR8.
CleanExHS_RDH12.
GenevestigatorQ96NR8.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
ProtoNetSearch...

Other

GeneWikiRDH12.
GenomeRNAi145226.
NextBio85049.
PROQ96NR8.
SOURCESearch...

Entry information

Entry nameRDH12_HUMAN
AccessionPrimary (citable) accession number: Q96NR8
Secondary accession number(s): B2RDA2, Q8TAW6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 118 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM