RDH16_RAT
ID RDH16_RAT Reviewed; 317 AA.
AC P50170;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Retinol dehydrogenase 16;
DE EC=1.1.1.105 {ECO:0000269|PubMed:7499345};
DE EC=1.1.1.209 {ECO:0000250|UniProtKB:O75452};
DE EC=1.1.1.315 {ECO:0000250|UniProtKB:O54909};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:O75452};
DE AltName: Full=29 kDa protein;
DE AltName: Full=Retinol dehydrogenase 2;
DE AltName: Full=Retinol dehydrogenase type 1 {ECO:0000303|PubMed:11601977};
DE AltName: Full=Retinol dehydrogenase type II {ECO:0000303|PubMed:7499345};
DE Short=RODH II {ECO:0000303|PubMed:7499345};
GN Name=Rdh16 {ECO:0000312|RGD:735050};
GN Synonyms=Rdh2, Rodh1 {ECO:0000303|PubMed:11601977}, Rodhii;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=7499345; DOI=10.1074/jbc.270.47.28408;
RA Chai X., Zhai Y., Popescu G., Napoli J.L.;
RT "Cloning of a cDNA for a second retinol dehydrogenase type II. Expression
RT of its mRNA relative to type I.";
RL J. Biol. Chem. 270:28408-28412(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 1-10.
RC TISSUE=Liver;
RX PubMed=8251521; DOI=10.1016/0304-4165(93)90019-5;
RA Ohishi N., Imaoka S., Suzuki T., Funae Y.;
RT "Characterization of two P-450 isozymes placed in the rat CYP2D
RT subfamily.";
RL Biochim. Biophys. Acta 1158:227-236(1993).
RN [4]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND CAUTION.
RX PubMed=11601977; DOI=10.1021/bi011396+;
RA Wang J., Bongianni J.K., Napoli J.L.;
RT "The N-terminus of retinol dehydrogenase type 1 signals cytosolic
RT orientation in the microsomal membrane.";
RL Biochemistry 40:12533-12540(2001).
CC -!- FUNCTION: Oxidoreductase with a preference for NAD. Oxidizes all-trans-
CC retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the
CC corresponding aldehydes (PubMed:7499345). Has higher activity towards
CC CRBP-bound retinol than with free retinol (By similarity). Oxidizes 3-
CC alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to
CC dihydrotestosterone and androstanedione. Can also catalyze the reverse
CC reaction (By similarity). {ECO:0000250|UniProtKB:O75452,
CC ECO:0000269|PubMed:7499345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-
CC trans-retinal--[retinol-binding protein] + H(+) + NADH;
CC Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC EC=1.1.1.105; Evidence={ECO:0000269|PubMed:7499345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:O75452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + NAD(+) = 13-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42056, ChEBI:CHEBI:15378, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:O75452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol + NAD(+) = 11-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42060, ChEBI:CHEBI:15378, ChEBI:CHEBI:16066,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.315; Evidence={ECO:0000250|UniProtKB:O54909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinol + NAD(+) = 9-cis-retinal + H(+) + NADH;
CC Xref=Rhea:RHEA:42052, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78272, ChEBI:CHEBI:78273;
CC Evidence={ECO:0000250|UniProtKB:O54909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC Evidence={ECO:0000250|UniProtKB:O75452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-
CC androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209;
CC Evidence={ECO:0000250|UniProtKB:O75452};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000269|PubMed:7499345}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O54909}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11601977}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:11601977}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver > kidney > brain > lung > testis.
CC {ECO:0000269|PubMed:7499345}.
CC -!- DOMAIN: The C-terminal region plays a crucial role in controlling the
CC activity of RDH16 and its required for endoplasmic reticulum (ER)
CC retention. {ECO:0000250|UniProtKB:O54909}.
CC -!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:11601977}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: Membrane topology is controversial (PubMed:11601977). Membrane
CC topology structure with endoplasmic reticulum lumen orientation of the
CC catalytic domains while the C-terminus is in the cytosol have been
CC suggested by one study (By similarity). Others investigators have
CC argued for a reverse orientation, with a membrane-embedded N-terminal
CC domain but no C-terminal transmembrane segment, and a cytosolic
CC orientation of the catalytic domain (PubMed:11601977). These
CC contracductoty results are probably because of differences in the assay
CC systems. {ECO:0000250|UniProtKB:O54909, ECO:0000269|PubMed:11601977,
CC ECO:0000305}.
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DR EMBL; U33500; AAC52316.1; -; mRNA.
DR EMBL; BC079153; AAH79153.1; -; mRNA.
DR PIR; I55462; I55462.
DR RefSeq; NP_954678.1; NM_199208.1.
DR AlphaFoldDB; P50170; -.
DR SMR; P50170; -.
DR STRING; 10116.ENSRNOP00000039311; -.
DR PaxDb; P50170; -.
DR Ensembl; ENSRNOT00000097465; ENSRNOP00000088842; ENSRNOG00000029651.
DR GeneID; 299511; -.
DR KEGG; rno:299511; -.
DR UCSC; RGD:735050; rat.
DR CTD; 8608; -.
DR RGD; 735050; Rdh16.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000154118; -.
DR InParanoid; P50170; -.
DR OrthoDB; 942985at2759; -.
DR PhylomeDB; P50170; -.
DR BRENDA; 1.1.1.53; 5301.
DR UniPathway; UPA00912; -.
DR PRO; PR:P50170; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031301; C:integral component of organelle membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; ISO:RGD.
DR GO; GO:1900054; P:positive regulation of retinoic acid biosynthetic process; IMP:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; IDA:RGD.
DR GO; GO:0001523; P:retinoid metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; IDA:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Lipid metabolism;
KW Membrane; Microsome; NAD; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Retinol dehydrogenase 16"
FT /id="PRO_0000054759"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 33..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 317 AA; 35597 MW; 13BF030FFC17BCB8 CRC64;
MWLYLLALVG LWNLLRLFRE RKVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC
LTEKGAEQLR SKTSDRLETV ILDVTKTESI VAATQWVKER VGNTGLWGLV NNAGISGHLG
PNEWMNKQNI ASVLDVNLLG MIEVTLSTVP LVRKARGRVV NVASIAGRLS FCGGGYCISK
YGVEAFSDSL RRELSYFGVK VAIVEPGFFR TDVTNGVTLS SNFQMLWDQT SSEVREVYGE
NYLASYLKML NGLDQRCNKD LSLVTDCMEH ALTSCHPRTR YSAGWDAKFF YLPMSYLPTF
LVDALFYWTS PKPEKAL
