RDH7_RAT
ID RDH7_RAT Reviewed; 317 AA.
AC P55006; P50169; Q4KMB6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Retinol dehydrogenase 7;
DE EC=1.1.1.105;
DE AltName: Full=Retinol dehydrogenase 3 {ECO:0000312|RGD:631370};
DE AltName: Full=Retinol dehydrogenase type III;
DE Short=RODH III;
GN Name=Rdh7 {ECO:0000312|RGD:631370}; Synonyms=Rdh3 {ECO:0000312|RGD:631370};
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7876135; DOI=10.1074/jbc.270.8.3900;
RA Chai X., Boerman M.H.E.M., Zhai Y., Napoli J.L.;
RT "Cloning of a cDNA for liver microsomal retinol dehydrogenase. A tissue-
RT specific, short-chain alcohol dehydrogenase.";
RL J. Biol. Chem. 270:3900-3904(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8647450; DOI=10.1016/0378-1119(95)00833-0;
RA Chai X., Zhai Y., Napoli J.L.;
RT "Cloning of a rat cDNA encoding retinol dehydrogenase isozyme type III.";
RL Gene 169:219-222(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Spleen;
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).
CC -!- FUNCTION: Acts on retinol bound on cellular retinol-binding protein
CC (CRBP).
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;
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U18762; AAB07997.1; -; mRNA.
DR EMBL; U33501; AAB07995.1; -; mRNA.
DR EMBL; BC088090; AAH88090.1; -; mRNA.
DR EMBL; BC098650; AAH98650.1; -; mRNA.
DR PIR; A55884; A55884.
DR RefSeq; NP_598227.3; NM_133543.3.
DR AlphaFoldDB; P55006; -.
DR SMR; P55006; -.
DR IntAct; P55006; 2.
DR STRING; 10116.ENSRNOP00000005875; -.
DR iPTMnet; P55006; -.
DR PhosphoSitePlus; P55006; -.
DR PaxDb; P55006; -.
DR PRIDE; P55006; -.
DR Ensembl; ENSRNOT00000005875; ENSRNOP00000005875; ENSRNOG00000004391.
DR GeneID; 360420; -.
DR KEGG; rno:360420; -.
DR UCSC; RGD:631370; rat.
DR CTD; 54150; -.
DR RGD; 631370; Rdh7.
DR eggNOG; KOG1610; Eukaryota.
DR GeneTree; ENSGT00940000154118; -.
DR OrthoDB; 942985at2759; -.
DR PhylomeDB; P55006; -.
DR TreeFam; TF325617; -.
DR Reactome; R-RNO-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR PRO; PR:P55006; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042572; P:retinol metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
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; Microsome; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..317
FT /note="Retinol dehydrogenase 7"
FT /id="PRO_0000054762"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 33..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 119
FT /note="M -> V (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="L -> V (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> T (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> Q (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="M -> T (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> P (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="Y -> H (in Ref. 1; AAB07997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35737 MW; 8193672B8576897A CRC64;
MWLYLLALVG LWNLLRLFRE RKVVSHLQDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC
LTEKGAEQLR SKTSDRLETV ILDVTKTESI VAATQWVKER VGNRGLWGLV NNAGISVPMG
PNEWMRKKDF ASVLDVNLLG VIEVTLNMLP LVRKARGRVV NIASTMGRMS LLGGGYCISK
YGVEAFSDSL RRELTYFGVK VAIIEPGGFK TNVTNMERLS DNLKKLWDQA TEEVKEIYGE
KFRDSYMKAM ESLVNMCSGD LSLVTDCMEH ALTSCHPRTR YSAGWDAKFF YLPMSYLPTF
LSDAVIYWGS VKPARAL
