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Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (NADPH-dependent retinol dehydrogenase/reductase) (NRDR) (humNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) (SCAD-SRL) (Short chain dehydrogenase/reductase family 25C member 2) (Short-chain dehydrogenase/reductase family member 4)

 DHRS4_HUMAN             Reviewed;         278 AA.
Q9BTZ2; B2RB10; B7WNS9; D3YTB8; E2QRL8; O95162; Q20CR0; Q2LC19;
Q2LE81; Q58IU4; Q6E0Y1; Q6UWU3; Q71UQ6; Q8TD03; Q9H3N5; Q9NV08;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
25-OCT-2017, entry version 156.
RecName: Full=Dehydrogenase/reductase SDR family member 4;
EC=1.1.1.184;
AltName: Full=NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase;
Short=CR;
Short=PHCR;
AltName: Full=NADPH-dependent retinol dehydrogenase/reductase;
Short=NRDR;
Short=humNRDR;
AltName: Full=Peroxisomal short-chain alcohol dehydrogenase;
Short=PSCD;
AltName: Full=SCAD-SRL;
AltName: Full=Short chain dehydrogenase/reductase family 25C member 2;
AltName: Full=Short-chain dehydrogenase/reductase family member 4;
Name=DHRS4; Synonyms=SDR25C2; ORFNames=UNQ851/PRO1800;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND SUBCELLULAR
LOCATION.
PubMed=10333503; DOI=10.1042/bj3400561;
Fransen M., Van Veldhoven P.P., Subramani S.;
"Identification of peroxisomal proteins by using M13 phage protein VI
phage display: molecular evidence that mammalian peroxisomes contain a
2,4-dienoyl-CoA reductase.";
Biochem. J. 340:561-568(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Furukawa A., Ohnishi T., Huang D., Araki N., Ichikawa Y.;
"cDNA cloning and characterization of peroxisomal short-chain
dehydrogenase / reductase that reduces all-trans retinal to retinol.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=15473316;
Du J., Huang D.-Y., Liu G.-F., Wang G.-L., Xu X.-L., Wang B., Zhu L.;
"cDNA cloning of a short isoform of human liver NADP (H) -dependent
retinol dehydrogenase/reductase and analysis of its characteristics.";
Yi Chuan Xue Bao 31:661-667(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tu Q., Yu L., Bi A., Li N., He W., Zhao S.;
"Molecular cloning and expression analysis of a novel human cDNA
encoding a protein homologous to human Hep27 protein.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Li Y.F., Liu G.-F., Song X.-H., Yang Y.M., Zhong J.C., Du K., Zhu W.,
Huang D.-Y.;
"A minor misassignment error inside segmental duplication (MMEISD) of
DHRS4 gene in human genome sequence.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Li Y.F., Liu G.-F., Song X.-H., Du K., Huang D.-Y.;
"cDNA cloning of a short isoform of human neuroblastoma NADP(H)-
dependent retinol dehydrogenase/reductase and analysis of its
characteristics.";
Ai Bian Ji Bian Tu Bian 17:321-326(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA]
(ISOFORM 6), NUCLEOTIDE SEQUENCE [MRNA] OF 40-278 (ISOFORM 5),
SUBCELLULAR LOCATION (ISOFORM 4), AND TISSUE SPECIFICITY (ISOFORM 4).
TISSUE=Cervix carcinoma, and Neuroblastoma;
PubMed=17230527; DOI=10.1002/ijc.22306;
Song X.-H., Liang B., Liu G.-F., Li R., Xie J.-P., Du K., Huang D.-Y.;
"Expression of a novel alternatively spliced variant of NADP(H)-
dependent retinol dehydrogenase/reductase with deletion of exon 3 in
cervical squamous carcinoma.";
Int. J. Cancer 120:1618-1626(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 (ISOFORM 5), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ALTERNATIVE SPLICING (ISOFORM 8).
PubMed=23128527; DOI=10.1159/000343326;
Yan Y., Song X., Liu G., Su Z., Du Y., Sui X., Chang X., Huang D.;
"Human NRDRB1, an alternatively spliced isoform of NADP(H)-dependent
retinol dehydrogenase/reductase enhanced enzymatic activity of
Benzil.";
Cell. Physiol. Biochem. 30:1371-1382(2012).
[15]
SUBCELLULAR LOCATION (ISOFORM 7).
PubMed=22227495; DOI=10.1016/j.gene.2011.12.033;
Su Z., Li R., Song X., Liu G., Li Y., Chang X., Li C., Huang D.;
"Identification of a novel isoform of DHRS4 protein with a nuclear
localization signal.";
Gene 494:161-167(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Reduces all-trans-retinal and 9-cis retinal. Can also
catalyze the oxidation of all-trans-retinol with NADP as co-
factor, but with much lower efficiency. Reduces alkyl phenyl
ketones and alpha-dicarbonyl compounds with aromatic rings, such
as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine,
menadione and 4-hexanoylpyridine. Has no activity towards
aliphatic aldehydes and ketones (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10333503}.
Note=Isoform 1 is peroxisomal, while isoform 4 is not.
-!- SUBCELLULAR LOCATION: Isoform 7: Nucleus
{ECO:0000269|PubMed:22227495}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=SDR-SRL3;
IsoId=Q9BTZ2-1; Sequence=Displayed;
Name=2; Synonyms=SDR-SRL1;
IsoId=Q9BTZ2-2; Sequence=VSP_008586;
Name=3; Synonyms=SDR-SRL2;
IsoId=Q9BTZ2-3; Sequence=VSP_008585;
Name=4; Synonyms=NRDRB1;
IsoId=Q9BTZ2-4; Sequence=VSP_031436;
Name=5; Synonyms=NRDRB2;
IsoId=Q9BTZ2-5; Sequence=VSP_031436, VSP_031438;
Note=Contains a phosphoserine at position 140.
{ECO:0000244|PubMed:18669648};
Name=6; Synonyms=DHRS4L2, NRDRA1;
IsoId=Q9BTZ2-6; Sequence=VSP_031435;
Name=7; Synonyms=NRDRA2;
IsoId=Q9BTZ2-7; Sequence=VSP_031437, VSP_031439;
Note=Mainly localized in the nucleus.;
Name=8; Synonyms=NRDRB1;
IsoId=Q9BTZ2-8; Sequence=VSP_044947, VSP_031436;
Note=Enhanced dicarbonyl reductase activity. high expression in
liver.;
-!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in normal
cervix (at protein level). Isoform 4 is expressed in some
neoplastic cervical tissues, but not in normal cervix (at protein
level). Isoform 5 and isoform 6 are expressed in a few neoplastic
cervical tissues.
-!- MISCELLANEOUS: Inhibited by kaempferol, quercetin, genistein and
myristic acid. {ECO:0000250}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD02292.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL61824.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB18775.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG37057.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF044127; AAD02292.1; ALT_INIT; mRNA.
EMBL; AB045131; BAB18775.1; ALT_INIT; mRNA.
EMBL; AY071856; AAL61824.2; ALT_INIT; mRNA.
EMBL; AF064256; AAQ13444.1; -; mRNA.
EMBL; AY616182; AAT70757.1; -; mRNA.
EMBL; DQ344810; ABD75823.1; -; mRNA.
EMBL; AY943857; AAX49568.1; -; mRNA.
EMBL; DQ325464; ABC61320.1; -; mRNA.
EMBL; DQ338571; ABC61321.1; -; mRNA.
EMBL; AK001870; BAA91953.1; -; mRNA.
EMBL; AK314448; BAG37057.1; ALT_INIT; mRNA.
EMBL; AY358638; AAQ89001.1; -; mRNA.
EMBL; AL136419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003019; AAH03019.1; -; mRNA.
CCDS; CCDS61408.1; -. [Q9BTZ2-7]
CCDS; CCDS61409.1; -. [Q9BTZ2-2]
CCDS; CCDS61410.1; -. [Q9BTZ2-4]
CCDS; CCDS61411.1; -. [Q9BTZ2-5]
CCDS; CCDS61412.1; -. [Q9BTZ2-3]
CCDS; CCDS9605.1; -. [Q9BTZ2-1]
RefSeq; NP_001269916.1; NM_001282987.1. [Q9BTZ2-7]
RefSeq; NP_001269917.1; NM_001282988.1. [Q9BTZ2-4]
RefSeq; NP_001269918.1; NM_001282989.1. [Q9BTZ2-2]
RefSeq; NP_001269919.1; NM_001282990.1. [Q9BTZ2-5]
RefSeq; NP_001269920.1; NM_001282991.1. [Q9BTZ2-3]
RefSeq; NP_066284.2; NM_021004.3. [Q9BTZ2-1]
UniGene; Hs.528385; -.
UniGene; Hs.743442; -.
PDB; 3O4R; X-ray; 1.70 A; A/B/C/D=19-278.
PDBsum; 3O4R; -.
ProteinModelPortal; Q9BTZ2; -.
SMR; Q9BTZ2; -.
BioGrid; 116107; 57.
IntAct; Q9BTZ2; 2.
STRING; 9606.ENSP00000326219; -.
DrugBank; DB00162; Vitamin A.
iPTMnet; Q9BTZ2; -.
PhosphoSitePlus; Q9BTZ2; -.
BioMuta; DHRS4; -.
DMDM; 308153604; -.
EPD; Q9BTZ2; -.
MaxQB; Q9BTZ2; -.
PaxDb; Q9BTZ2; -.
PeptideAtlas; Q9BTZ2; -.
PRIDE; Q9BTZ2; -.
Ensembl; ENST00000313250; ENSP00000326219; ENSG00000157326. [Q9BTZ2-1]
Ensembl; ENST00000397074; ENSP00000380264; ENSG00000157326. [Q9BTZ2-3]
Ensembl; ENST00000397075; ENSP00000380265; ENSG00000157326. [Q9BTZ2-2]
Ensembl; ENST00000558263; ENSP00000453367; ENSG00000157326. [Q9BTZ2-7]
Ensembl; ENST00000558581; ENSP00000452645; ENSG00000157326. [Q9BTZ2-4]
Ensembl; ENST00000559632; ENSP00000453983; ENSG00000157326. [Q9BTZ2-5]
GeneID; 10901; -.
KEGG; hsa:10901; -.
UCSC; uc001wla.5; human. [Q9BTZ2-1]
CTD; 10901; -.
DisGeNET; 10901; -.
EuPathDB; HostDB:ENSG00000157326.18; -.
GeneCards; DHRS4; -.
HGNC; HGNC:16985; DHRS4.
HPA; HPA023972; -.
MIM; 611596; gene.
neXtProt; NX_Q9BTZ2; -.
OpenTargets; ENSG00000157326; -.
PharmGKB; PA128395792; -.
eggNOG; KOG0725; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00760000118868; -.
HOVERGEN; HBG105779; -.
InParanoid; Q9BTZ2; -.
KO; K11147; -.
OMA; FELLGAY; -.
OrthoDB; EOG091G0G3R; -.
PhylomeDB; Q9BTZ2; -.
TreeFam; TF315405; -.
BRENDA; 1.1.1.300; 2681.
Reactome; R-HSA-5365859; RA biosynthesis pathway.
EvolutionaryTrace; Q9BTZ2; -.
GeneWiki; DHRS4; -.
GenomeRNAi; 10901; -.
PRO; PR:Q9BTZ2; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000157326; -.
ExpressionAtlas; Q9BTZ2; baseline and differential.
Genevisible; Q9BTZ2; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0000253; F:3-keto sterol reductase activity; IDA:UniProtKB.
GO; GO:0018455; F:alcohol dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:UniProtKB.
GO; GO:0052650; F:NADP-retinol dehydrogenase activity; TAS:Reactome.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
GO; GO:0042180; P:cellular ketone metabolic process; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
InterPro; IPR029511; DHRS4-like.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PANTHER; PTHR43943:SF8; PTHR43943:SF8; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
NADP; Nucleus; Oxidoreductase; Peroxisome; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 278 Dehydrogenase/reductase SDR family member
4.
/FTId=PRO_0000054647.
NP_BIND 36 60 NADP. {ECO:0000250}.
MOTIF 276 278 Microbody targeting signal.
ACT_SITE 182 182 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 169 169 Substrate. {ECO:0000250}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 216 216 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 216 216 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 227 227 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LB2}.
MOD_RES 234 234 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LB2}.
VAR_SEQ 1 18 Missing (in isoform 8). {ECO:0000305}.
/FTId=VSP_044947.
VAR_SEQ 19 221 Missing (in isoform 6).
{ECO:0000303|PubMed:17230527}.
/FTId=VSP_031435.
VAR_SEQ 103 222 Missing (in isoform 3).
{ECO:0000303|PubMed:10333503}.
/FTId=VSP_008585.
VAR_SEQ 103 136 Missing (in isoform 4, isoform 5 and
isoform 8).
{ECO:0000303|PubMed:17230527}.
/FTId=VSP_031436.
VAR_SEQ 137 222 Missing (in isoform 2).
{ECO:0000303|PubMed:10333503,
ECO:0000303|PubMed:15473316}.
/FTId=VSP_008586.
VAR_SEQ 137 188 TLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSP
GFSPYNVSKTA -> RRLSGDRVFHSSLQSISSLDGQGKRG
KHERNPADKKVRRARGLCWHRVFPVL (in isoform
7). {ECO:0000303|Ref.5}.
/FTId=VSP_031437.
VAR_SEQ 178 222 Missing (in isoform 5).
{ECO:0000303|PubMed:17230527}.
/FTId=VSP_031438.
VAR_SEQ 189 278 Missing (in isoform 7).
{ECO:0000303|Ref.5}.
/FTId=VSP_031439.
VARIANT 31 31 A -> T (in dbSNP:rs1043442).
/FTId=VAR_057272.
VARIANT 202 202 P -> S (in dbSNP:rs1043650).
/FTId=VAR_061846.
CONFLICT 37 37 V -> A (in Ref. 8; BAA91953).
{ECO:0000305}.
CONFLICT 50 50 R -> W (in Ref. 7; ABC61321).
{ECO:0000305}.
CONFLICT 89 89 H -> M (in Ref. 4; AAQ13444).
{ECO:0000305}.
CONFLICT 102 102 T -> M (in Ref. 1; AAD02292).
{ECO:0000305}.
CONFLICT 126 126 I -> L (in Ref. 1; AAD02292).
{ECO:0000305}.
TURN 29 32 {ECO:0000244|PDB:3O4R}.
STRAND 34 39 {ECO:0000244|PDB:3O4R}.
HELIX 43 54 {ECO:0000244|PDB:3O4R}.
STRAND 58 64 {ECO:0000244|PDB:3O4R}.
HELIX 66 78 {ECO:0000244|PDB:3O4R}.
STRAND 83 87 {ECO:0000244|PDB:3O4R}.
HELIX 93 107 {ECO:0000244|PDB:3O4R}.
STRAND 112 115 {ECO:0000244|PDB:3O4R}.
TURN 126 128 {ECO:0000244|PDB:3O4R}.
HELIX 131 141 {ECO:0000244|PDB:3O4R}.
HELIX 143 158 {ECO:0000244|PDB:3O4R}.
STRAND 162 167 {ECO:0000244|PDB:3O4R}.
HELIX 170 172 {ECO:0000244|PDB:3O4R}.
HELIX 180 200 {ECO:0000244|PDB:3O4R}.
HELIX 201 203 {ECO:0000244|PDB:3O4R}.
STRAND 205 212 {ECO:0000244|PDB:3O4R}.
HELIX 221 223 {ECO:0000244|PDB:3O4R}.
HELIX 227 237 {ECO:0000244|PDB:3O4R}.
HELIX 245 248 {ECO:0000244|PDB:3O4R}.
HELIX 249 255 {ECO:0000244|PDB:3O4R}.
HELIX 258 260 {ECO:0000244|PDB:3O4R}.
STRAND 267 271 {ECO:0000244|PDB:3O4R}.
SEQUENCE 278 AA; 29537 MW; 3B06A229E1BBE47B CRC64;
MHKAGLLGLC ARAWNSVRMA SSGMTRRDPL ANKVALVTAS TDGIGFAIAR RLAQDGAHVV
VSSRKQQNVD QAVATLQGEG LSVTGTVCHV GKAEDRERLV ATAVKLHGGI DILVSNAAVN
PFFGSIMDVT EEVWDKTLDI NVKAPALMTK AVVPEMEKRG GGSVVIVSSI AAFSPSPGFS
PYNVSKTALL GLTKTLAIEL APRNIRVNCL APGLIKTSFS RMLWMDKEKE ESMKETLRIR
RLGEPEDCAG IVSFLCSEDA SYITGETVVV GGGTPSRL


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