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Aldo-keto reductase family 1 member C1 (EC 1.1.1.-) (20-alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (EC 1.1.1.149) (Chlordecone reductase homolog HAKRC) (Dihydrodiol dehydrogenase 1/2) (DD1/DD2) (High-affinity hepatic bile acid-binding protein) (HBAB) (Indanol dehydrogenase) (EC 1.1.1.112) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)

 AK1C1_HUMAN             Reviewed;         323 AA.
Q04828; P52896; Q5SR15; Q7M4N2; Q9UCX2;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
28-FEB-2018, entry version 188.
RecName: Full=Aldo-keto reductase family 1 member C1;
EC=1.1.1.-;
AltName: Full=20-alpha-hydroxysteroid dehydrogenase;
Short=20-alpha-HSD;
EC=1.1.1.149 {ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
AltName: Full=Chlordecone reductase homolog HAKRC;
AltName: Full=Dihydrodiol dehydrogenase 1/2;
Short=DD1/DD2;
AltName: Full=High-affinity hepatic bile acid-binding protein;
Short=HBAB;
AltName: Full=Indanol dehydrogenase;
EC=1.1.1.112 {ECO:0000269|PubMed:8573067};
AltName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
EC=1.3.1.20 {ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
Name=AKR1C1; Synonyms=DDH, DDH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8486699;
Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E.;
"cDNA cloning and expression of the human hepatic bile acid-binding
protein. A member of the monomeric reductase gene family.";
J. Biol. Chem. 268:10448-10457(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=8132567;
Lou H., Hammond L., Sharma V., Sparkes R.S., Lusis A.J., Stolz A.;
"Genomic organization and chromosomal localization of a novel human
hepatic dihydrodiol dehydrogenase with high affinity bile acid
binding.";
J. Biol. Chem. 269:8416-8422(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Colon;
PubMed=7515059;
Ciaccio P.J., Jaiswal A.K., Tew K.D.;
"Regulation of human dihydrodiol dehydrogenase by Michael acceptor
xenobiotics.";
J. Biol. Chem. 269:15558-15562(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7626489; DOI=10.1016/0960-0760(95)00019-V;
Khanna M., Qin K.-N., Cheng K.-C.;
"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and
molecular cloning of multiple cDNAs encoding structurally related
proteins in humans.";
J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=10672042; DOI=10.1046/j.1365-2443.2000.00310.x;
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y.,
Watanabe K., Ito S.;
"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with
three aldo-keto reductase genes.";
Genes Cells 5:111-125(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Skin fibroblast;
PubMed=11013348; DOI=10.1677/jme.0.0250221;
Zhang Y., Dufort I., Rheault P., Luu-The V.;
"Characterization of a human 20alpha-hydroxysteroid dehydrogenase.";
J. Mol. Endocrinol. 25:221-228(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Testis;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-323.
TISSUE=Liver;
PubMed=8274401; DOI=10.1016/0960-0760(93)90308-J;
Qin K.-N., New M.I., Cheng K.-C.;
"Molecular cloning of multiple cDNAs encoding human enzymes
structurally related to 3 alpha-hydroxysteroid dehydrogenase.";
J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
[11]
PROTEIN SEQUENCE OF 10-31; 40-61; 69-126; 137-153; 162-206; 209-230;
250-267; 271-289 AND 295-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8573067; DOI=10.1042/bj3130373;
Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y.,
Ishida N.;
"Relationship of human liver dihydrodiol dehydrogenases to hepatic
bile-acid-binding protein and an oxidoreductase of human colon
cells.";
Biochem. J. 313:373-376(1996).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-323, AND PROTEIN SEQUENCE OF 18-31;
105-131; 176-193 AND 271-294.
TISSUE=Liver;
PubMed=8172617; DOI=10.1042/bj2990545;
Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y.,
Sato K., Hara A.;
"Molecular cloning of two human liver 3 alpha-
hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical
with chlordecone reductase and bile-acid binder.";
Biochem. J. 299:545-552(1994).
[13]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NADP AND
20ALPHA-HYDROXY-PROGESTERONE, AND MUTAGENESIS OF GLU-127; HIS-222;
ARG-304; TYR-305; THR-307 AND ASP-309.
PubMed=12899831; DOI=10.1016/S0022-2836(03)00762-9;
Couture J.-F., Legrand P., Cantin L., Luu-The V., Labrie F.,
Breton R.;
"Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and
site-directed mutagenesis studies lead to the identification of an
alternative binding site for C21-steroids.";
J. Mol. Biol. 331:593-604(2003).
[14]
X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH NADP AND
3-CHLORO-5-PHENYLSALICYLIC ACID.
PubMed=21414777; DOI=10.1016/j.bmcl.2011.01.076;
El-Kabbani O., Dhagat U., Soda M., Endo S., Matsunaga T., Hara A.;
"Probing the inhibitor selectivity pocket of human 20alpha-
hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and
site-directed mutagenesis.";
Bioorg. Med. Chem. Lett. 21:2564-2567(2011).
-!- FUNCTION: Converts progesterone to its inactive form, 20-alpha-
dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine,
may have a role in the transport of bile. May have a role in
monitoring the intrahepatic bile acid concentration. Has a low
bile-binding ability. May play a role in myelin formation.
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067}.
-!- CATALYTIC ACTIVITY: 17-alpha,20-alpha-dihydroxypregn-4-en-3-one +
NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H.
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067}.
-!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) =
catechol + NADPH. {ECO:0000269|PubMed:11013348,
ECO:0000269|PubMed:8573067}.
-!- CATALYTIC ACTIVITY: Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H.
{ECO:0000269|PubMed:8573067}.
-!- ENZYME REGULATION: Inhibited by hexestrol with an IC(50) of 9.5
uM, 1,10-phenanthroline with an IC(50) of 55 uM, 1,7-
phenanthroline with an IC(50) of 72 uM, flufenamic acid with an
IC(50) of 6.0 uM, indomethacin with an IC(50) of 140 uM, ibuprofen
with an IC(50) of 950 uM, lithocholic acid with an IC(50) of 25
uM, ursodeoxycholic acid with an IC(50) of 340 uM and
chenodeoxycholic acid with an IC(50) of 570 uM.
{ECO:0000269|PubMed:8573067}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5 uM for (s)-tetralol {ECO:0000269|PubMed:11013348,
ECO:0000269|PubMed:8573067};
KM=38 uM for (s)-indan-1-ol {ECO:0000269|PubMed:11013348,
ECO:0000269|PubMed:8573067};
KM=580 uM for benzene dihydrodiol {ECO:0000269|PubMed:11013348,
ECO:0000269|PubMed:8573067};
KM=3 uM for 5-beta-pregnane-3-alpha,20-alpha-diol
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=3 uM for 5-beta-pregnan-20-alpha-ol-3-one
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=12 uM for 4-pregnen-20-alpha-ol-3-one
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=133 uM for 9-alpha,11-beta-prostaglandin F(2)
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=2 uM for 5-beta-pregnan-3-alpha-ol-20-one
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=1 uM for 5-beta-androstane-3,17-dione
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
KM=12 uM for prostaglandin D(2) {ECO:0000269|PubMed:11013348,
ECO:0000269|PubMed:8573067};
KM=0.6 uM for 20-alpha-hydroxyprogesterone (with NADH)
{ECO:0000269|PubMed:11013348, ECO:0000269|PubMed:8573067};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
-!- INTERACTION:
P26045:PTPN3; NbExp=5; IntAct=EBI-2116455, EBI-1047946;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in all tissues tested including
liver, prostate, testis, adrenal gland, brain, uterus, mammary
gland and keratinocytes. Highest levels found in liver, mammary
gland and brain. {ECO:0000269|PubMed:11013348}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
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EMBL; M86609; AAB02880.1; -; mRNA.
EMBL; U05861; AAA18115.1; -; Genomic_DNA.
EMBL; U05853; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05854; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05855; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05857; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05858; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05859; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05860; AAA18115.1; JOINED; Genomic_DNA.
EMBL; U05684; AAA16227.1; -; mRNA.
EMBL; AB031083; BAA92883.1; -; mRNA.
EMBL; AB032150; BAA92886.1; -; Genomic_DNA.
EMBL; BT007197; AAP35861.1; -; mRNA.
EMBL; AL713867; CAI16409.1; -; Genomic_DNA.
EMBL; AC091817; CAI16409.1; JOINED; Genomic_DNA.
EMBL; BC015490; AAH15490.1; -; mRNA.
EMBL; BC020216; AAH20216.1; -; mRNA.
EMBL; BC040210; AAH40210.1; -; mRNA.
EMBL; S68290; AAD14012.1; -; mRNA.
EMBL; D26124; BAA05121.1; -; mRNA.
CCDS; CCDS7061.1; -.
PIR; A53436; A53436.
PIR; I73675; I73675.
PIR; S59619; S59619.
PIR; S61515; S61515.
RefSeq; NP_001344.2; NM_001353.5.
UniGene; Hs.460260; -.
PDB; 1MRQ; X-ray; 1.59 A; A=2-323.
PDB; 3C3U; X-ray; 1.80 A; A=1-323.
PDB; 3GUG; X-ray; 1.90 A; A=1-323.
PDB; 3NTY; X-ray; 1.87 A; A=1-323.
PDB; 4YVP; X-ray; 2.60 A; A/B=1-323.
PDBsum; 1MRQ; -.
PDBsum; 3C3U; -.
PDBsum; 3GUG; -.
PDBsum; 3NTY; -.
PDBsum; 4YVP; -.
ProteinModelPortal; Q04828; -.
SMR; Q04828; -.
BioGrid; 108012; 8.
IntAct; Q04828; 4.
MINT; Q04828; -.
STRING; 9606.ENSP00000370254; -.
BindingDB; Q04828; -.
ChEMBL; CHEMBL5905; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB07931; Hexestrol.
DrugBank; DB00157; NADH.
DrugBank; DB00936; Salicylic acid.
SwissLipids; SLP:000000802; -.
iPTMnet; Q04828; -.
PhosphoSitePlus; Q04828; -.
SwissPalm; Q04828; -.
BioMuta; AKR1C1; -.
DMDM; 416877; -.
EPD; Q04828; -.
MaxQB; Q04828; -.
PaxDb; Q04828; -.
PeptideAtlas; Q04828; -.
PRIDE; Q04828; -.
DNASU; 1645; -.
Ensembl; ENST00000380872; ENSP00000370254; ENSG00000187134.
GeneID; 1645; -.
KEGG; hsa:1645; -.
UCSC; uc001ihq.4; human.
CTD; 1645; -.
DisGeNET; 1645; -.
EuPathDB; HostDB:ENSG00000187134.12; -.
GeneCards; AKR1C1; -.
HGNC; HGNC:384; AKR1C1.
HPA; CAB047303; -.
HPA; HPA068265; -.
MalaCards; AKR1C1; -.
MIM; 600449; gene.
neXtProt; NX_Q04828; -.
OpenTargets; ENSG00000187134; -.
PharmGKB; PA24677; -.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00760000119041; -.
HOGENOM; HOG000250272; -.
HOVERGEN; HBG000020; -.
InParanoid; Q04828; -.
KO; K00212; -.
OMA; MAPSTHF; -.
PhylomeDB; Q04828; -.
TreeFam; TF106492; -.
BioCyc; MetaCyc:HS10741-MONOMER; -.
BRENDA; 1.1.1.149; 2681.
BRENDA; 1.1.1.270; 2681.
BRENDA; 1.1.1.50; 2681.
BRENDA; 1.3.1.20; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SABIO-RK; Q04828; -.
SIGNOR; Q04828; -.
ChiTaRS; AKR1C1; human.
EvolutionaryTrace; Q04828; -.
GeneWiki; AKR1C1; -.
GenomeRNAi; 1645; -.
PRO; PR:Q04828; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000187134; -.
CleanEx; HS_AKR1C1; -.
ExpressionAtlas; Q04828; baseline and differential.
Genevisible; Q04828; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0047006; F:17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; TAS:UniProtKB.
GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; IDA:UniProtKB.
GO; GO:0032052; F:bile acid binding; IDA:UniProtKB.
GO; GO:0031406; F:carboxylic acid binding; IDA:UniProtKB.
GO; GO:0047718; F:indanol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0047086; F:ketosteroid monooxygenase activity; IDA:UniProtKB.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; IDA:UniProtKB.
GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IDA:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:UniProtKB.
GO; GO:0008206; P:bile acid metabolic process; IDA:UniProtKB.
GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; TAS:UniProtKB.
GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
GO; GO:0007586; P:digestion; IDA:UniProtKB.
GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; TAS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0046683; P:response to organophosphorus; IEP:UniProtKB.
GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0006805; P:xenobiotic metabolic process; NAS:UniProtKB.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR018170; Aldo/ket_reductase_CS.
InterPro; IPR020471; Aldo/keto_reductase.
InterPro; IPR023210; NADP_OxRdtase_dom.
InterPro; IPR036812; NADP_OxRdtase_dom_sf.
PANTHER; PTHR11732; PTHR11732; 1.
Pfam; PF00248; Aldo_ket_red; 1.
PIRSF; PIRSF000097; AKR; 1.
PRINTS; PR00069; ALDKETRDTASE.
SUPFAM; SSF51430; SSF51430; 1.
PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
NADP; Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 323 Aldo-keto reductase family 1 member C1.
/FTId=PRO_0000124633.
NP_BIND 20 24 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
NP_BIND 166 167 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
NP_BIND 216 222 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
NP_BIND 270 280 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
ACT_SITE 55 55 Proton donor. {ECO:0000250}.
BINDING 24 24 Substrate.
BINDING 50 50 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
BINDING 117 117 Substrate. {ECO:0000250}.
BINDING 190 190 NADP. {ECO:0000269|PubMed:12899831,
ECO:0000269|PubMed:21414777}.
BINDING 222 222 Substrate.
BINDING 227 227 Substrate.
SITE 54 54 Important for substrate specificity.
{ECO:0000250}.
SITE 84 84 Lowers pKa of active site Tyr.
{ECO:0000250}.
SITE 222 222 May be involved in the mediating step
between the transformation of
progesterone and the release of the
cofactor.
VARIANT 170 170 R -> H (in dbSNP:rs139588200).
/FTId=VAR_048214.
VARIANT 172 172 Q -> L (in dbSNP:rs11474).
/FTId=VAR_048215.
MUTAGEN 127 127 E->D: 30-fold decrease in k(cat)/K(m)
value for progesterone reduction; no
effect on the K(m) value.
{ECO:0000269|PubMed:12899831}.
MUTAGEN 222 222 H->I: Marked decrease in k(cat)/K(m)
value for progesterone; 24-fold decrease
for progesterone reduction; 18-fold
decrease for 20alpha-OHProg oxidation.
95-fold decrease in K(m) value for NADPH.
{ECO:0000269|PubMed:12899831}.
MUTAGEN 222 222 H->S: Marked decrease in k(cat)/K(m)
value for progesterone; 10-fold decrease
for progesterone reduction; 3-fold
decrease for 20alpha-OHProg oxidation.
10-fold decrease in K(m) value for NADPH.
{ECO:0000269|PubMed:12899831}.
MUTAGEN 304 304 R->L: 70-fold decrease in progesterone
reduction. No effect on DHT reduction.
{ECO:0000269|PubMed:12899831}.
MUTAGEN 305 305 Y->F: No effect on progesterone
reduction. {ECO:0000269|PubMed:12899831}.
MUTAGEN 307 307 T->V: No effect on progesterone
reduction. {ECO:0000269|PubMed:12899831}.
MUTAGEN 309 309 D->V: No effect on progesterone
reduction. {ECO:0000269|PubMed:12899831}.
CONFLICT 3 3 S -> A (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 95 95 V -> D (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
CONFLICT 158 158 G -> E (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
CONFLICT 171 172 RQ -> ST (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
CONFLICT 183 184 KY -> QV (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
CONFLICT 222 222 H -> L (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
CONFLICT 319 319 F -> I (in Ref. 4; no nucleotide entry
and 10; AAD14012). {ECO:0000305}.
STRAND 7 9 {ECO:0000244|PDB:1MRQ}.
STRAND 15 22 {ECO:0000244|PDB:1MRQ}.
HELIX 33 44 {ECO:0000244|PDB:1MRQ}.
STRAND 48 50 {ECO:0000244|PDB:1MRQ}.
HELIX 53 55 {ECO:0000244|PDB:1MRQ}.
HELIX 58 70 {ECO:0000244|PDB:1MRQ}.
HELIX 76 78 {ECO:0000244|PDB:1MRQ}.
STRAND 80 85 {ECO:0000244|PDB:1MRQ}.
HELIX 87 89 {ECO:0000244|PDB:1MRQ}.
HELIX 92 106 {ECO:0000244|PDB:1MRQ}.
STRAND 111 116 {ECO:0000244|PDB:1MRQ}.
STRAND 124 126 {ECO:0000244|PDB:3C3U}.
STRAND 133 135 {ECO:0000244|PDB:4YVP}.
HELIX 144 156 {ECO:0000244|PDB:1MRQ}.
STRAND 159 167 {ECO:0000244|PDB:1MRQ}.
HELIX 170 177 {ECO:0000244|PDB:1MRQ}.
STRAND 187 192 {ECO:0000244|PDB:1MRQ}.
STRAND 194 197 {ECO:0000244|PDB:3GUG}.
HELIX 200 208 {ECO:0000244|PDB:1MRQ}.
STRAND 212 217 {ECO:0000244|PDB:1MRQ}.
TURN 225 227 {ECO:0000244|PDB:1MRQ}.
HELIX 235 237 {ECO:0000244|PDB:1MRQ}.
HELIX 239 248 {ECO:0000244|PDB:1MRQ}.
HELIX 252 262 {ECO:0000244|PDB:1MRQ}.
STRAND 266 270 {ECO:0000244|PDB:1MRQ}.
HELIX 274 280 {ECO:0000244|PDB:1MRQ}.
HELIX 281 285 {ECO:0000244|PDB:1MRQ}.
HELIX 290 297 {ECO:0000244|PDB:1MRQ}.
HELIX 309 311 {ECO:0000244|PDB:1MRQ}.
SEQUENCE 323 AA; 36788 MW; 9CB215478FBD29D5 CRC64;
MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ
VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV
SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP
GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
RNVRYLTLDI FAGPPNYPFS DEY


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