RDH13_HUMAN
ID RDH13_HUMAN Reviewed; 331 AA.
AC Q8NBN7; Q6UX79; Q96G88;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Retinol dehydrogenase 13 {ECO:0000305};
DE EC=1.1.1.300 {ECO:0000269|PubMed:18039331};
DE AltName: Full=Short chain dehydrogenase/reductase family 7C member 3;
GN Name=RDH13; Synonyms=SDR7C3; ORFNames=PSEC0082, UNQ736/PRO1430;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [5]
RP TISSUE SPECIFICITY, AND CAUTION.
RX PubMed=12226107; DOI=10.1074/jbc.m208882200;
RA Haeseleer F., Jang G.-F., Imanishi Y., Driessen C.A.G.G., Matsumura M.,
RA Nelson P.S., Palczewski K.;
RT "Dual-substrate specificity short chain retinol dehydrogenases from the
RT vertebrate retina.";
RL J. Biol. Chem. 277:45537-45546(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18039331; DOI=10.1111/j.1742-4658.2007.06184.x;
RA Belyaeva O.V., Korkina O.V., Stetsenko A.V., Kedishvili N.Y.;
RT "Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain
RT dehydrogenase/reductase with a retinaldehyde reductase activity.";
RL FEBS J. 275:138-147(2008).
CC -!- FUNCTION: Retinol dehydrogenase with a clear preference for NADP.
CC Oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with
CC much higher efficiency (PubMed:18039331). Has no activity toward
CC steroids (PubMed:18039331). {ECO:0000269|PubMed:18039331}.
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; Evidence={ECO:0000269|PubMed:18039331};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for all-trans-retinal {ECO:0000269|PubMed:18039331};
CC KM=3 uM for all-trans-retinol {ECO:0000269|PubMed:18039331};
CC KM=1.5 uM for NADPH {ECO:0000269|PubMed:18039331};
CC KM=6000 uM for NAD {ECO:0000269|PubMed:18039331};
CC Vmax=230 nmol/min/mg enzyme with all-trans-retinal as substrate
CC {ECO:0000269|PubMed:18039331};
CC Vmax=5 nmol/min/mg enzyme with all-trans-retinol as substrate
CC {ECO:0000269|PubMed:18039331};
CC Vmax=230 nmol/min/mg enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:18039331};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:Q9ERI6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18039331}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18039331}. Note=Localized on the outer side of the
CC inner mitochondrial membrane. {ECO:0000269|PubMed:18039331}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBN7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBN7-2; Sequence=VSP_040383;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:18039331). In the retina,
CC detected in the inner segment of the photoreceptor cells. Weak signals
CC are observed in a small population of inner nuclear neurons and the
CC inner plexiform layer (PubMed:12226107). {ECO:0000269|PubMed:12226107,
CC ECO:0000269|PubMed:18039331}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to lack retinol dehydrogenase (RDH)
CC activity. However, a more recent publication demonstrates a retinol
CC dehydrogenase activity for RDH13. {ECO:0000269|PubMed:12226107,
CC ECO:0000269|PubMed:18039331}.
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DR EMBL; AY358473; AAQ88837.1; -; mRNA.
DR EMBL; AK075392; BAC11591.1; -; mRNA.
DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009881; AAH09881.1; -; mRNA.
DR CCDS; CCDS42627.1; -. [Q8NBN7-2]
DR CCDS; CCDS54320.1; -. [Q8NBN7-1]
DR RefSeq; NP_001139443.1; NM_001145971.1. [Q8NBN7-1]
DR RefSeq; NP_612421.1; NM_138412.3. [Q8NBN7-2]
DR RefSeq; XP_005258530.1; XM_005258473.1. [Q8NBN7-1]
DR RefSeq; XP_011524709.1; XM_011526407.1.
DR AlphaFoldDB; Q8NBN7; -.
DR SMR; Q8NBN7; -.
DR BioGRID; 125200; 89.
DR IntAct; Q8NBN7; 27.
DR MINT; Q8NBN7; -.
DR STRING; 9606.ENSP00000391121; -.
DR DrugBank; DB00162; Vitamin A.
DR DrugCentral; Q8NBN7; -.
DR SwissLipids; SLP:000001877; -.
DR GlyGen; Q8NBN7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NBN7; -.
DR PhosphoSitePlus; Q8NBN7; -.
DR BioMuta; RDH13; -.
DR DMDM; 62298570; -.
DR EPD; Q8NBN7; -.
DR jPOST; Q8NBN7; -.
DR MassIVE; Q8NBN7; -.
DR MaxQB; Q8NBN7; -.
DR PaxDb; Q8NBN7; -.
DR PeptideAtlas; Q8NBN7; -.
DR PRIDE; Q8NBN7; -.
DR ProteomicsDB; 72802; -. [Q8NBN7-1]
DR ProteomicsDB; 72803; -. [Q8NBN7-2]
DR Antibodypedia; 32994; 138 antibodies from 21 providers.
DR DNASU; 112724; -.
DR Ensembl; ENST00000396247.7; ENSP00000379547.2; ENSG00000160439.16. [Q8NBN7-2]
DR Ensembl; ENST00000415061.8; ENSP00000391121.2; ENSG00000160439.16. [Q8NBN7-1]
DR Ensembl; ENST00000610356.4; ENSP00000477732.1; ENSG00000160439.16. [Q8NBN7-2]
DR Ensembl; ENST00000613257.1; ENSP00000479552.1; ENSG00000276341.1. [Q8NBN7-2]
DR Ensembl; ENST00000613935.1; ENSP00000482809.1; ENSG00000274504.1. [Q8NBN7-2]
DR Ensembl; ENST00000615256.4; ENSP00000477512.1; ENSG00000276684.4. [Q8NBN7-1]
DR Ensembl; ENST00000615688.1; ENSP00000482782.1; ENSG00000275474.1. [Q8NBN7-2]
DR Ensembl; ENST00000616348.1; ENSP00000477884.1; ENSG00000276826.1. [Q8NBN7-2]
DR Ensembl; ENST00000620423.1; ENSP00000482051.1; ENSG00000278149.1. [Q8NBN7-2]
DR Ensembl; ENST00000621614.4; ENSP00000484637.1; ENSG00000276684.4. [Q8NBN7-2]
DR Ensembl; ENST00000621849.1; ENSP00000480095.1; ENSG00000273944.1. [Q8NBN7-2]
DR Ensembl; ENST00000622200.1; ENSP00000484111.1; ENSG00000274418.1. [Q8NBN7-2]
DR Ensembl; ENST00000622572.1; ENSP00000484246.1; ENSG00000278284.1. [Q8NBN7-2]
DR GeneID; 112724; -.
DR KEGG; hsa:112724; -.
DR MANE-Select; ENST00000415061.8; ENSP00000391121.2; NM_001145971.2; NP_001139443.1.
DR UCSC; uc002qio.4; human. [Q8NBN7-1]
DR CTD; 112724; -.
DR DisGeNET; 112724; -.
DR GeneCards; RDH13; -.
DR HGNC; HGNC:19978; RDH13.
DR HPA; ENSG00000160439; Low tissue specificity.
DR neXtProt; NX_Q8NBN7; -.
DR OpenTargets; ENSG00000160439; -.
DR PharmGKB; PA134897935; -.
DR VEuPathDB; HostDB:ENSG00000160439; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000159641; -.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; Q8NBN7; -.
DR OMA; RHTGMHQ; -.
DR OrthoDB; 921996at2759; -.
DR PhylomeDB; Q8NBN7; -.
DR TreeFam; TF105429; -.
DR BRENDA; 1.1.1.300; 2681.
DR PathwayCommons; Q8NBN7; -.
DR Reactome; R-HSA-5365859; RA biosynthesis pathway.
DR SignaLink; Q8NBN7; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 112724; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; RDH13; human.
DR GenomeRNAi; 112724; -.
DR Pharos; Q8NBN7; Tbio.
DR PRO; PR:Q8NBN7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8NBN7; protein.
DR Bgee; ENSG00000160439; Expressed in lower esophagus mucosa and 95 other tissues.
DR ExpressionAtlas; Q8NBN7; baseline and differential.
DR Genevisible; Q8NBN7; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0009644; P:response to high light intensity; IEA:Ensembl.
DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl.
DR GO; GO:0042574; P:retinal metabolic process; IDA: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 Acetylation; Alternative splicing; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..331
FT /note="Retinol dehydrogenase 13"
FT /id="PRO_0000054768"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8WNV7,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 45..51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040383"
FT CONFLICT 106
FT /note="E -> V (in Ref. 2; BAC11591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 35932 MW; DC5C1A6E54F1E6CC CRC64;
MSRYLLPLSA LGTVAGAAVL LKDYVTGGAC PSKATIPGKT VIVTGANTGI GKQTALELAR
RGGNIILACR DMEKCEAAAK DIRGETLNHH VNARHLDLAS LKSIREFAAK IIEEEERVDI
LINNAGVMRC PHWTTEDGFE MQFGVNHLGH FLLTNLLLDK LKASAPSRII NLSSLAHVAG
HIDFDDLNWQ TRKYNTKAAY CQSKLAIVLF TKELSRRLQG SGVTVNALHP GVARTELGRH
TGIHGSTFSS TTLGPIFWLL VKSPELAAQP STYLAVAEEL ADVSGKYFDG LKQKAPAPEA
EDEEVARRLW AESARLVGLE APSVREQPLP R
