RDH13_MOUSE
ID RDH13_MOUSE Reviewed; 334 AA.
AC Q8CEE7; Q8CC07;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Retinol dehydrogenase 13;
DE EC=1.1.1.300 {ECO:0000250|UniProtKB:Q8NBN7};
GN Name=Rdh13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Has no activity towards steroid.
CC {ECO:0000250|UniProtKB:Q8NBN7}.
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:0000250|UniProtKB:Q8NBN7};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:Q9ERI6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q8NBN7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NBN7}. Note=Localized on the outer side of the
CC inner mitochondrial membrane. {ECO:0000250|UniProtKB:Q8NBN7}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AK028434; BAC25950.1; -; mRNA.
DR EMBL; AK034180; BAC28618.1; -; mRNA.
DR EMBL; BC082583; AAH82583.1; -; mRNA.
DR CCDS; CCDS20735.1; -.
DR RefSeq; NP_001277338.1; NM_001290409.1.
DR RefSeq; NP_001277340.1; NM_001290411.1.
DR RefSeq; NP_780581.1; NM_175372.4.
DR AlphaFoldDB; Q8CEE7; -.
DR SMR; Q8CEE7; -.
DR BioGRID; 224445; 5.
DR IntAct; Q8CEE7; 1.
DR STRING; 10090.ENSMUSP00000008579; -.
DR iPTMnet; Q8CEE7; -.
DR PhosphoSitePlus; Q8CEE7; -.
DR SwissPalm; Q8CEE7; -.
DR EPD; Q8CEE7; -.
DR jPOST; Q8CEE7; -.
DR MaxQB; Q8CEE7; -.
DR PaxDb; Q8CEE7; -.
DR PeptideAtlas; Q8CEE7; -.
DR PRIDE; Q8CEE7; -.
DR ProteomicsDB; 253190; -.
DR Antibodypedia; 32994; 138 antibodies from 21 providers.
DR DNASU; 108841; -.
DR Ensembl; ENSMUST00000008579; ENSMUSP00000008579; ENSMUSG00000008435.
DR GeneID; 108841; -.
DR KEGG; mmu:108841; -.
DR UCSC; uc009exm.2; mouse.
DR CTD; 112724; -.
DR MGI; MGI:1918732; Rdh13.
DR VEuPathDB; HostDB:ENSMUSG00000008435; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000159641; -.
DR HOGENOM; CLU_010194_44_5_1; -.
DR InParanoid; Q8CEE7; -.
DR OMA; RHTGMHQ; -.
DR OrthoDB; 921996at2759; -.
DR PhylomeDB; Q8CEE7; -.
DR TreeFam; TF105429; -.
DR Reactome; R-MMU-5365859; RA biosynthesis pathway.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 108841; 4 hits in 76 CRISPR screens.
DR PRO; PR:Q8CEE7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CEE7; protein.
DR Bgee; ENSMUSG00000008435; Expressed in ear vesicle and 253 other tissues.
DR ExpressionAtlas; Q8CEE7; baseline and differential.
DR Genevisible; Q8CEE7; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR GO; GO:0009644; P:response to high light intensity; IMP:MGI.
DR GO; GO:0010842; P:retina layer formation; IMP:MGI.
DR GO; GO:0042574; P:retinal 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 Acetylation; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8NBN7"
FT CHAIN 2..334
FT /note="Retinol dehydrogenase 13"
FT /id="PRO_0000054769"
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:0000250|UniProtKB:Q8NBN7"
FT CONFLICT 114..148
FT /note="Missing (in Ref. 1; BAC28618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36464 MW; 4EBBCE1643C1FECE CRC64;
MSRFLLPVSV VGTVIGGTVL LKDYVAGGAC PSKATIPGKT VIVTGANTGI GKQTALELAK
RGGNVILACR DMEKCEVAAK DIRGETLNPR VRAERLDLAS LKSIREFARK VIKEEERVDI
LVNNAAVMRC PHWTTEDGFE MQFGVNYLGH FLLTNLLLDK LKASAPSRII NLSSLAHVAG
HIDFEDLNWQ MKKYDTKAAY CQSKLAVVLF TKELSHRLQG SGVTVNALHP GVARTELGRH
TGMHNSAFSG FMLGPFFWLL FKSPQLAAQP STYLAVAEEL ENVSGKYFDG LREKAPSPEA
EDEEVARRLW TESARLVGLA MAHGSPGRGH AIPR
