RDH10_XENTR
ID RDH10_XENTR Reviewed; 341 AA.
AC Q5XGF7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Retinol dehydrogenase 10;
DE EC=1.1.1.300;
GN Name=rdh10;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Converts all-trans-retinol to all-trans-retinal. Has no detectable
CC activity towards 11-cis-retinol, 9-cis-retinol and 13-cis-retinol (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) +
CC NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.300;
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; BC084483; AAH84483.1; -; mRNA.
DR RefSeq; NP_001011091.1; NM_001011091.1.
DR AlphaFoldDB; Q5XGF7; -.
DR SMR; Q5XGF7; -.
DR STRING; 8364.ENSXETP00000025854; -.
DR PaxDb; Q5XGF7; -.
DR DNASU; 496504; -.
DR Ensembl; ENSXETT00000025854; ENSXETP00000025854; ENSXETG00000011825.
DR GeneID; 496504; -.
DR KEGG; xtr:496504; -.
DR CTD; 157506; -.
DR Xenbase; XB-GENE-944961; rdh10.
DR eggNOG; KOG1201; Eukaryota.
DR HOGENOM; CLU_010194_2_5_1; -.
DR InParanoid; Q5XGF7; -.
DR OMA; HICAPRV; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; Q5XGF7; -.
DR TreeFam; TF312837; -.
DR Reactome; R-XTR-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-XTR-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000011825; Expressed in gastrula and 12 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0002138; P:retinoic acid biosynthetic process; IEA:InterPro.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032970; RDH10.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24322:SF731; PTHR24322:SF731; 1.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Microsome; NADP;
KW Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..341
FT /note="Retinol dehydrogenase 10"
FT /id="PRO_0000307689"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 40..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38424 MW; 5E97AF00EE1BCD09 CRC64;
MHIVLEFFLV TFKVLWAFVL AAAKWLVRPK DKSVAGQVCL ITGAGSGLGR LFALEFARRR
AQLVLWDINS QSNEETAEMV RSIYRELEAE DSARRAGNAT EEEVQPCCNF QVYTYTCDVG
KRESVYSTAE RVRREVGDVY LLLNNAGVVS GHHLLECPDE LIERTMMVNC HAHFWTTKAF
LPKMMEMNHG HIVSVASSLG LFSTAGVEDY CASKFGVVGF HESLSHELKA ADKDGIKTTL
VCPYLVDTGM FRGCRIRKEI EPFLPPLKPD YCVKQAMRAI LTDQPMICTP RLMYIVTCMK
SILPFEAVVC MYRFLGADKC MYPFIAQRKQ ATNNNEAKNG I