ID RDH8_HUMAN Reviewed; 311 AA.
AC Q9NYR8; Q9H838;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 01-MAY-2013, entry version 87.
DE RecName: Full=Retinol dehydrogenase 8;
DE EC=1.1.1.300;
DE AltName: Full=Photoreceptor outer segment all-trans retinol dehydrogenase;
GN Name=RDH8; Synonyms=PRRDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10753906; DOI=10.1074/jbc.275.15.11034;
RA Rattner A., Smallwood P.M., Nathans J.;
RT "Identification and characterization of all-trans-retinol
RT dehydrogenase from photoreceptor outer segments, the visual cycle
RT enzyme that reduces all-trans-retinal to all-trans-retinol.";
RL J. Biol. Chem. 275:11034-11043(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Converts all-trans-retinal to all-trans-retinol. May play a role
CC in the regeneration of visual pigment at high light intensity (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: All-trans-retinol + NADP(+) = all-trans-
CC retinal + NADPH.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- TISSUE SPECIFICITY: Detected in photoreceptor outer segments in
CC the retina (at protein level).
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14782.1; Type=Frameshift; Positions=26;
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DR EMBL; AF229845; AAF63160.1; -; mRNA.
DR EMBL; AK024022; BAB14782.1; ALT_FRAME; mRNA.
DR IPI; IPI00024598; -.
DR RefSeq; NP_056540.2; NM_015725.2.
DR UniGene; Hs.675522; -.
DR HSSP; P14061; 1FDU.
DR ProteinModelPortal; Q9NYR8; -.
DR STRING; 9606.ENSP00000171214; -.
DR PhosphoSite; Q9NYR8; -.
DR DMDM; 74753074; -.
DR PaxDb; Q9NYR8; -.
DR PRIDE; Q9NYR8; -.
DR DNASU; 50700; -.
DR Ensembl; ENST00000171214; ENSP00000171214; ENSG00000080511.
DR GeneID; 50700; -.
DR KEGG; hsa:50700; -.
DR UCSC; uc002mmr.3; human.
DR CTD; 50700; -.
DR GeneCards; GC19P010123; -.
DR HGNC; HGNC:14423; RDH8.
DR MIM; 608575; gene.
DR neXtProt; NX_Q9NYR8; -.
DR PharmGKB; PA34309; -.
DR eggNOG; COG1028; -.
DR HOVERGEN; HBG014077; -.
DR InParanoid; Q9NYR8; -.
DR KO; K11150; -.
DR OMA; YFRDLYL; -.
DR OrthoDB; EOG4ZCT53; -.
DR PhylomeDB; Q9NYR8; -.
DR BioCyc; MetaCyc:HS01358-MONOMER; -.
DR BRENDA; 1.1.1.105; 2681.
DR DrugBank; DB00162; Vitamin A.
DR GenomeRNAi; 50700; -.
DR NextBio; 53218; -.
DR Bgee; Q9NYR8; -.
DR CleanEx; HS_RDH8; -.
DR Genevestigator; Q9NYR8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:InterPro.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004745; F:retinol dehydrogenase activity; TAS:ProtInc.
DR GO; GO:0006703; P:estrogen biosynthetic process; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0042572; P:retinol metabolic process; IEA:Compara.
DR GO; GO:0006694; P:steroid biosynthetic process; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR011348; 17beta_DH.
DR InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR InterPro; IPR002347; Glc/ribitol_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR Pfam; PF00106; adh_short; 1.
DR PIRSF; PIRSF000095; 17beta-HSD; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Membrane; NADP; Oxidoreductase; Polymorphism;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Vision.
FT CHAIN 1 311 Retinol dehydrogenase 8.
FT /FTId=PRO_0000305972.
FT TRANSMEM 86 106 Helical; (Potential).
FT TRANSMEM 137 157 Helical; (Potential).
FT TRANSMEM 169 189 Helical; (Potential).
FT NP_BIND 9 18 NADP (By similarity).
FT ACT_SITE 155 155 Proton acceptor (By similarity).
FT BINDING 142 142 Substrate (Potential).
FT VARIANT 136 136 H -> Q (in dbSNP:rs1122206).
FT /FTId=VAR_035232.
FT VARIANT 202 202 M -> T (in dbSNP:rs1644731).
FT /FTId=VAR_035233.
SQ SEQUENCE 311 AA; 33755 MW; D62416D1F0377ECE CRC64;
MAAAPRTVLI SGCSSGIGLE LAVQLAHDPK KRYQVVATMR DLGKKETLEA AAGEALGQTL
TVAQLDVCSD ESVAQCLSCI QGEVDVLVNN AGMGLVGPLE GLSLAAMQNV FDTNFFGAVR
LVKAVLPGMK RRRQGHIVVI SSVMGLQGVI FNDVYAASKF ALEGFFESLA IQLLQFNIFI
SLVEPGPVVT EFEGKLLAQV SMAEFPGTDP ETLHYFRDLY LPASRKLFCS VGQNPQDVVQ
AIVNVISSTR PPLRRQTNIR YSPLTTLKTV DSSGSLYVRT THRLLFRCPR LLNLGLQCLS
CGCLPTRVRP R
//
