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P42330 (AK1C3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldo-keto reductase family 1 member C3

EC=1.-.-.-
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase type 5
Short name=17-beta-HSD 5
3-alpha-HSD type II, brain
3-alpha-hydroxysteroid dehydrogenase type 2
Short name=3-alpha-HSD type 2
EC=1.1.1.357
Chlordecone reductase homolog HAKRb
Dihydrodiol dehydrogenase 3
Short name=DD-3
Short name=DD3
Dihydrodiol dehydrogenase type I
HA1753
Indanol dehydrogenase
EC=1.1.1.112
Prostaglandin F synthase
Short name=PGFS
EC=1.1.1.188
Testosterone 17-beta-dehydrogenase 5
EC=1.1.1.239
EC=1.1.1.64
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EC=1.3.1.20
Gene names
Name:AKR1C3
Synonyms:DDH1, HSD17B5, KIAA0119, PGFS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2. Functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone.

Catalytic activity

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.

A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.

(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH.

Testosterone + NAD+ = androstenedione + NADH.

Testosterone + NADP+ = androst-4-ene-3,17-dione + NADPH.

Indan-1-ol + NAD(P)+ = indanone + NAD(P)H.

Enzyme regulation

Strongly inhibited by nonsteroidal anti-inflammatory drugs (NSAID) including flufenamic acid and indomethacin. Also inhibited by the flavinoid, rutin, and by selective serotonin inhibitors (SSRIs).

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in many tissues including adrenal gland, brain, kidney, liver, lung, mammary gland, placenta, small intestine, colon, spleen, prostate and testis. The dominant HSD in prostate and mammary gland. In the prostate, higher levels in epithelial cells than in stromal cells. In the brain, expressed in medulla, spinal cord, frontotemporal lobes, thalamus, subthalamic nuclei and amygdala. Weaker expression in the hippocampus, substantia nigra and caudate. Ref.2 Ref.4 Ref.5 Ref.6 Ref.8 Ref.14

Sequence similarities

Belongs to the aldo/keto reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=142.1 µM for progesterone Ref.6

KM=2.37 µM for 5-alpha-dihydrotestosterone

KM=1.0 µM for androstanediol

Vmax=20.1 nmol/min/mg enzyme with progesterone as substrate

Vmax=1.8 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone as substrate

Vmax=4.4 nmol/min/mg enzyme with androstanediol as substrate

Sequence caution

The sequence BAA04619.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 18508192. Source: UniProtKB

arachidonic acid metabolic process

Traceable author statement. Source: Reactome

cellular response to cadmium ion

Inferred from direct assay PubMed 21787718. Source: UniProtKB

cellular response to calcium ion

Inferred from direct assay PubMed 22170488. Source: UniProtKB

cellular response to corticosteroid stimulus

Inferred from direct assay PubMed 19336506. Source: UniProtKB

cellular response to jasmonic acid stimulus

Inferred from direct assay PubMed 19487289. Source: UniProtKB

cellular response to prostaglandin stimulus

Inferred from direct assay PubMed 22170488. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from direct assay PubMed 21787718. Source: UniProtKB

cellular response to starvation

Inferred from expression pattern PubMed 18641923. Source: UniProtKB

cyclooxygenase pathway

Traceable author statement. Source: Reactome

daunorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

doxorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

farnesol catabolic process

Inferred from direct assay PubMed 21187079. Source: UniProtKB

keratinocyte differentiation

Inferred from expression pattern PubMed 22170488. Source: UniProtKB

male gonad development

Inferred from expression pattern PubMed 19942269. Source: UniProtKB

multicellular organismal macromolecule metabolic process

Inferred from expression pattern PubMed 18641923. Source: UniProtKB

negative regulation of retinoic acid biosynthetic process

Inferred from direct assay PubMed 21851338. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 16983398PubMed 19442656PubMed 21232532. Source: UniProtKB

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of cell death

Inferred from direct assay PubMed 21787718. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 18508192PubMed 20036328. Source: UniProtKB

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 19442656. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 18508192. Source: UniProtKB

positive regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 19442656. Source: UniProtKB

progesterone metabolic process

Inferred from direct assay PubMed 21232532. Source: UniProtKB

prostaglandin metabolic process

Inferred from expression pattern PubMed 20036328. Source: UniProtKB

protein import into nucleus, translocation

Inferred from direct assay PubMed 21787718. Source: UniProtKB

regulation of retinoic acid receptor signaling pathway

Inferred from direct assay PubMed 21851338. Source: UniProtKB

regulation of testosterone biosynthetic process

Inferred from mutant phenotype PubMed 19336506. Source: UniProtKB

renal absorption

Non-traceable author statement PubMed 16157291. Source: UniProtKB

response to nutrient

Inferred from expression pattern PubMed 19007764. Source: UniProtKB

response to prostaglandin

Inferred from direct assay PubMed 18508192. Source: UniProtKB

retinal metabolic process

Inferred from direct assay PubMed 21851338. Source: UniProtKB

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Inferred from expression pattern PubMed 20036328. Source: UniProtKB

testosterone biosynthetic process

Inferred from mutant phenotype PubMed 16983398. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18574251PubMed 19336506PubMed 19942269PubMed 22170488. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from direct assay PubMed 18574251. Source: UniProtKB

   Molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity

Inferred from direct assay PubMed 22170488. Source: UniProtKB

alditol:NADP+ 1-oxidoreductase activity

Inferred from direct assay PubMed 21232532. Source: UniProtKB

aldo-keto reductase (NADP) activity

Traceable author statement PubMed 9792917. Source: UniProtKB

androsterone dehydrogenase activity

Inferred from direct assay PubMed 16983398. Source: UniProtKB

delta4-3-oxosteroid 5beta-reductase activity

Inferred from direct assay PubMed 16983398. Source: UniProtKB

dihydrotestosterone 17-beta-dehydrogenase activity

Inferred from direct assay PubMed 16983398. Source: UniProtKB

geranylgeranyl reductase activity

Inferred from direct assay PubMed 21187079. Source: UniProtKB

indanol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ketoreductase activity

Inferred from direct assay PubMed 19487289. Source: UniProtKB

ketosteroid monooxygenase activity

Inferred from direct assay PubMed 21232532. Source: UniProtKB

oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor

Inferred from direct assay PubMed 19442656PubMed 20837989. Source: UniProtKB

phenanthrene 9,10-monooxygenase activity

Inferred from direct assay PubMed 21851338. Source: UniProtKB

prostaglandin D2 11-ketoreductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

prostaglandin F receptor activity

Inferred from direct assay PubMed 18508192. Source: UniProtKB

prostaglandin-F synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

retinal dehydrogenase activity

Inferred from direct assay PubMed 21851338. Source: UniProtKB

retinol dehydrogenase activity

Inferred from direct assay PubMed 21851338. Source: UniProtKB

testosterone 17-beta-dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

testosterone dehydrogenase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Aldo-keto reductase family 1 member C3
PRO_0000124638

Regions

Nucleotide binding13 – 2210NADP Potential
Nucleotide binding217 – 28064NADP By similarity

Sites

Active site551Proton donor By similarity
Binding site1171Substrate By similarity
Site541Important for substrate specificity By similarity
Site841Lowers pKa of active site Tyr By similarity
Site2271Involved in ligand recognition and product release
Site3061Involved in ligand recognition and product release

Natural variations

Natural variant51H → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9
Corresponds to variant rs12529 [ dbSNP | Ensembl ].
VAR_013288
Natural variant661R → Q.
Corresponds to variant rs35961894 [ dbSNP | Ensembl ].
VAR_032767
Natural variant771E → G.
Corresponds to variant rs41306308 [ dbSNP | Ensembl ].
VAR_061001
Natural variant1701R → C.
Corresponds to variant rs35575889 [ dbSNP | Ensembl ].
VAR_032768
Natural variant1751M → I No effect on 17beta-HSD activity. Ref.1 Ref.2 Ref.14
Corresponds to variant rs1131132 [ dbSNP | Ensembl ].
VAR_013289
Natural variant1801P → S.
Corresponds to variant rs34186955 [ dbSNP | Ensembl ].
VAR_032769

Experimental info

Mutagenesis751K → E: No effect on 17beta-HSD activity. Ref.14
Sequence conflict31S → P no nucleotide entry Ref.3
Sequence conflict61Q → K no nucleotide entry Ref.3
Sequence conflict381T → S in AAF07272. Ref.6
Sequence conflict751K → E in AAD14011. Ref.1
Sequence conflict751K → E no nucleotide entry Ref.3
Sequence conflict751K → M in AAB41916. Ref.2
Sequence conflict891F → S in AAF07272. Ref.6
Sequence conflict2701K → R in AAF07272. Ref.6

Secondary structure

........................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42330 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 86A7690D9498C6FD

FASTA32336,853
        10         20         30         40         50         60 
MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ 

        70         80         90        100        110        120 
VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM 

       130        140        150        160        170        180 
SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV 

       250        260        270        280        290        300 
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD 

       310        320 
RNLHYFNSDS FASHPNYPYS DEY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase."
Qin K.-N., New M.I., Cheng K.-C.
J. Steroid Biochem. Mol. Biol. 46:673-679(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-5 AND ILE-175.
Tissue: Liver.
[2]"Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases."
Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.
J. Biol. Chem. 270:20162-20168(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, TISSUE SPECIFICITY, VARIANTS GLN-5 AND ILE-175.
[3]"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans."
Khanna M., Qin K.-N., Cheng K.-C.
J. Steroid Biochem. Mol. Biol. 53:41-46(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-5.
Tissue: Liver.
[4]"Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution."
Lin H.-K., Jez J.M., Schlegel B.P., Peehl D.M., Pachter J.A., Penning T.M.
Mol. Endocrinol. 11:1971-1984(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT GLN-5.
Tissue: Prostate.
[5]"cDNA cloning, expression and characterization of human prostaglandin F synthase."
Suzuki-Yamamoto T., Nishizawa M., Fukui M., Okuda-Ashitaka E., Nakajima T., Ito S., Watanabe K.
FEBS Lett. 462:335-340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-190, CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT GLN-5.
Tissue: Lung.
[6]"Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes."
Griffin L.D., Mellon S.H.
Proc. Natl. Acad. Sci. U.S.A. 96:13512-13517(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT GLN-5.
Tissue: Brain.
[7]"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes."
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.
Genes Cells 5:111-125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[8]"Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3)."
Penning T.M., Burczynski M.E., Jez J.M., Lin H.-K., Ma H., Moore M., Ratnam K., Palackal N.
Mol. Cell. Endocrinol. 171:137-149(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
Tissue: Prostate.
[9]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-5.
Tissue: Bone marrow.
[10]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[12]"The DNA sequence and comparative analysis of human chromosome 10."
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. expand/collapse author list , 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.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Urinary bladder.
[14]"Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase."
Dufort I., Rheault P., Huang X.-F., Soucy P., Luu-The V.
Endocrinology 140:568-574(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT ILE-175, MUTAGENESIS OF LYS-75.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Crystal structure of human prostaglandin F synthase (AKR1C3)."
Komoto J., Yamada T., Watanabe K., Takusagawa F.
Biochemistry 43:2188-2198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PROSTAGLANDIN H(2); NADPH AND RUTIN.
[17]"Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal anti-inflammatory drugs flufenamic acid and indomethacin."
Lovering A.L., Ride J.P., Bunce C.M., Desmond J.C., Cummings S.M., White S.A.
Cancer Res. 64:1802-1810(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FLUFENAMIC ACID AND INDOMETHACIN.
[18]"Crystal structures of the multispecific 17beta-hydroxysteroid dehydrogenase type 5: critical androgen regulation in human peripheral tissues."
Qiu W., Zhou M., Labrie F., Lin S.-X.
Mol. Endocrinol. 18:1798-1807(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADP AND DELTA4 -3 ANDROSTENE-3,17-DIONE, IMPORTANCE OF TRP-227 AND PHE-306 IN LIGAND RECOGNITION AND PRODUCT RELEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S68288 mRNA. Translation: AAD14011.1.
L43839 expand/collapse EMBL AC list , L43831, L43832, L43833, L43834, L43835, L43836, L43837, L43838 Genomic DNA. Translation: AAB41916.1.
AB018580 mRNA. Translation: BAA88488.1.
AB028065 Genomic DNA. Translation: BAA88489.1.
AF149416 mRNA. Translation: AAF07272.2.
AB032157 Genomic DNA. Translation: BAA92892.1.
D17793 mRNA. Translation: BAA04619.2. Different initiation.
BT007286 mRNA. Translation: AAP35950.1.
AK290365 mRNA. Translation: BAF83054.1.
AL391427 Genomic DNA. No translation available.
BC001479 mRNA. Translation: AAH01479.1.
BC019230 mRNA. Translation: AAH19230.1.
CCDSCCDS7063.1.
PIRB57407.
I73674.
RefSeqNP_001240837.1. NM_001253908.1.
NP_003730.4. NM_003739.5.
UniGeneHs.78183.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY0X-ray1.69A/B1-323[»]
1RY8X-ray1.69A/B1-323[»]
1S1PX-ray1.20A1-323[»]
1S1RX-ray2.00A1-323[»]
1S2AX-ray1.70A1-323[»]
1S2CX-ray1.80A1-323[»]
1XF0X-ray2.00A1-323[»]
1ZQ5X-ray1.30A1-323[»]
2F38X-ray2.00A1-323[»]
2FGBX-ray1.35A1-323[»]
3R43X-ray2.00A1-323[»]
3R58X-ray2.30A1-323[»]
3R6IX-ray1.95A1-323[»]
3R7MX-ray2.10A1-323[»]
3R8GX-ray1.80A1-323[»]
3R8HX-ray1.90A1-323[»]
3R94X-ray2.01A1-323[»]
3UFYX-ray1.90A1-323[»]
3UG8X-ray1.73A1-323[»]
3UGRX-ray1.65A1-323[»]
3UWEX-ray1.68A1-323[»]
4DBSX-ray1.85A/B1-323[»]
4DBUX-ray2.53A/B1-323[»]
4DBWX-ray1.80A/B1-323[»]
4DZ5X-ray1.70A1-323[»]
4FA3X-ray2.20A1-323[»]
4FALX-ray2.00A1-323[»]
4FAMX-ray2.00A/B1-323[»]
4H7CX-ray1.97A1-323[»]
4HMNX-ray2.40A1-323[»]
ProteinModelPortalP42330.
SMRP42330. Positions 6-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114196. 5 interactions.
IntActP42330. 5 interactions.
MINTMINT-1379107.

Chemistry

BindingDBP42330.
ChEMBLCHEMBL4681.
DrugBankDB01093. Dimethyl sulfoxide.
DB00157. NADH.

PTM databases

PhosphoSiteP42330.

Polymorphism databases

DMDM308153646.

2D gel databases

DOSAC-COBS-2DPAGEP42330.

Proteomic databases

MaxQBP42330.
PaxDbP42330.
PRIDEP42330.

Protocols and materials databases

DNASU8644.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380554; ENSP00000369927; ENSG00000196139.
ENST00000583876; ENSP00000464178; ENSG00000265685.
GeneID8644.
KEGGhsa:8644.
UCSCuc001ihr.3. human.

Organism-specific databases

CTD8644.
GeneCardsGC10P005077.
HGNCHGNC:386. AKR1C3.
HPACAB010874.
MIM603966. gene.
neXtProtNX_P42330.
PharmGKBPA24679.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0656.
HOVERGENHBG000020.
InParanoidP42330.
KOK04119.
OMAFDIVDLC.
PhylomeDBP42330.
TreeFamTF106492.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP42330.

Gene expression databases

ArrayExpressP42330.
BgeeP42330.
CleanExHS_AKR1C3.
GenevestigatorP42330.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP42330.
GeneWikiAKR1C3.
GenomeRNAi8644.
NextBio32407.
PROP42330.
SOURCESearch...

Entry information

Entry nameAK1C3_HUMAN
AccessionPrimary (citable) accession number: P42330
Secondary accession number(s): A8K2V0 expand/collapse secondary AC list , Q5T2L1, Q96DJ1, Q96KI8, Q99530, Q9UCX1, Q9UII3, Q9UKL9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM