DHR13_MOUSE
ID DHR13_MOUSE Reviewed; 376 AA.
AC Q5SS80; Q14BH2; Q8BMX8;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dehydrogenase/reductase SDR family member 13;
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Short chain dehydrogenase/reductase family 7C member 5 {ECO:0000250|UniProtKB:Q6UX07};
DE Short=Protein SDR7C5 {ECO:0000250|UniProtKB:Q6UX07};
DE Flags: Precursor;
GN Name=Dhrs13 {ECO:0000312|MGI:MGI:1917701};
GN Synonyms=Sdr7c5 {ECO:0000250|UniProtKB:Q6UX07};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, 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: Putative oxidoreductase. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SS80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SS80-2; Sequence=VSP_029641;
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25347.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK011939; BAC25347.1; ALT_FRAME; mRNA.
DR EMBL; AL669840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115881; AAI15882.1; -; mRNA.
DR CCDS; CCDS36236.1; -. [Q5SS80-1]
DR RefSeq; NP_899109.2; NM_183286.2. [Q5SS80-1]
DR RefSeq; XP_011247557.1; XM_011249255.2.
DR AlphaFoldDB; Q5SS80; -.
DR SMR; Q5SS80; -.
DR BioGRID; 214059; 2.
DR STRING; 10090.ENSMUSP00000021187; -.
DR iPTMnet; Q5SS80; -.
DR PhosphoSitePlus; Q5SS80; -.
DR SwissPalm; Q5SS80; -.
DR EPD; Q5SS80; -.
DR MaxQB; Q5SS80; -.
DR PaxDb; Q5SS80; -.
DR PeptideAtlas; Q5SS80; -.
DR PRIDE; Q5SS80; -.
DR ProteomicsDB; 279864; -. [Q5SS80-1]
DR ProteomicsDB; 279865; -. [Q5SS80-2]
DR Antibodypedia; 14931; 83 antibodies from 15 providers.
DR Ensembl; ENSMUST00000021187; ENSMUSP00000021187; ENSMUSG00000020834. [Q5SS80-1]
DR GeneID; 70451; -.
DR KEGG; mmu:70451; -.
DR UCSC; uc007khu.1; mouse. [Q5SS80-1]
DR CTD; 147015; -.
DR MGI; MGI:1917701; Dhrs13.
DR VEuPathDB; HostDB:ENSMUSG00000020834; -.
DR eggNOG; KOG1208; Eukaryota.
DR GeneTree; ENSGT00940000155599; -.
DR InParanoid; Q5SS80; -.
DR OMA; NRPVVGW; -.
DR OrthoDB; 1076292at2759; -.
DR PhylomeDB; Q5SS80; -.
DR TreeFam; TF105429; -.
DR BioGRID-ORCS; 70451; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q5SS80; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SS80; protein.
DR Bgee; ENSMUSG00000020834; Expressed in manus and 204 other tissues.
DR ExpressionAtlas; Q5SS80; baseline and differential.
DR Genevisible; Q5SS80; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0052650; F:NADP-retinol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0042574; P:retinal metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; NAD; NADP; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..376
FT /note="Dehydrogenase/reductase SDR family member 13"
FT /id="PRO_0000311921"
FT REGION 311..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029641"
FT CONFLICT 240
FT /note="P -> R (in Ref. 1; BAC25347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 40745 MW; B4C77A8058948865 CRC64;
MEMLLLGAGL LLGAYVLVYY NLVKAPSCGG IGSLRGRTVV VTGANSGIGK MTALELARRG
ARVVLACRSR ERGEAAAFDL RQESGNNEVI FMALDLASLA SVQAFATAFL SSEPRLDVLI
HNAGISSCGR TRETFNLLLR VNHVGPFLLT HLLLPRLRSC APSRVVIVSS AAHRRGRLDF
TRLDCPVVGW QQELRAYADS KLANVLFARE LATQLEGTGV TCYAAHPGPV NSELFLRHLP
GWLRPILRPL AWLVLRAPQG GAQTPLYCAL QEGIEPLSGR YFANCHVEEV SPAARDDQAA
QRLWKATKKL AGLAPGDDDD DPDEEPEPED PRAPSSQSAP SPEKTTVSGP SHSYQGSQDL
SKLTQRRIQV KDEPTP
