P42330 (AK1C3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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=1.1.1.213
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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	323 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 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 cascade 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 retinal metabolic process Inferred from direct assay PubMed 21851338. Source: UniProtKB testosterone biosynthetic process Inferred from mutant phenotype PubMed 16983398. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 18574251PubMed 19336506PubMed 19942269PubMed 22170488. Source: UniProtKB nucleus Inferred from direct assay PubMed 18574251. Source: UniProtKB
Molecular_function	15-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 androsterone dehydrogenase (A-specific) activity Inferred from electronic annotation. Source: EC 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: 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: EC prostaglandin F receptor activity Inferred from direct assay PubMed 18508192. Source: UniProtKB prostaglandin-F synthase activity Inferred from electronic annotation. Source: 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: EC testosterone dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 323

323

Aldo-keto reductase family 1 member C3

PRO_0000124638

Regions

Nucleotide binding

13 – 22

10

NADP Potential

Nucleotide binding

217 – 280

64

NADP By similarity

Sites

Active site

55

1

Proton donor By similarity

Binding site

117

1

Substrate By similarity

Site

54

1

Important for substrate specificity By similarity

Site

84

1

Lowers pKa of active site Tyr By similarity

Site

227

1

Involved in ligand recognition and product release

Site

306

1

Involved in ligand recognition and product release

Natural variations

Natural variant

5

1

H → Q. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9
Corresponds to variant rs12529 [ dbSNP | Ensembl ].

VAR_013288

Natural variant

66

1

R → Q.
Corresponds to variant rs35961894 [ dbSNP | Ensembl ].

VAR_032767

Natural variant

77

1

E → G.
Corresponds to variant rs41306308 [ dbSNP | Ensembl ].

VAR_061001

Natural variant

170

1

R → C.
Corresponds to variant rs35575889 [ dbSNP | Ensembl ].

VAR_032768

Natural variant

175

1

M → I No effect on 17beta-HSD activity. Ref.1 Ref.2 Ref.14
Corresponds to variant rs1131132 [ dbSNP | Ensembl ].

VAR_013289

Natural variant

180

1

P → S.
Corresponds to variant rs34186955 [ dbSNP | Ensembl ].

VAR_032769

Experimental info

Mutagenesis

75

1

K → E: No effect on 17beta-HSD activity. Ref.14

Sequence conflict

3

1

S → P no nucleotide entry Ref.3

Sequence conflict

6

1

Q → K no nucleotide entry Ref.3

Sequence conflict

38

1

T → S in AAF07272. Ref.6

Sequence conflict

75

1

K → E in AAD14011. Ref.1

Sequence conflict

75

1

K → E no nucleotide entry Ref.3

Sequence conflict

75

1

K → M in AAB41916. Ref.2

Sequence conflict

89

1

F → S in AAF07272. Ref.6

Sequence conflict

270

1

K → R in AAF07272. Ref.6

Secondary structure

1

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323

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

15 – 22

8

Helix

33 – 44

12

Beta strand

48 – 50

3

Helix

53 – 55

3

Helix

58 – 70

13

Helix

76 – 78

3

Beta strand

80 – 85

6

Helix

87 – 89

3

Helix

92 – 94

3

Helix

95 – 106

12

Beta strand

111 – 116

6

Beta strand

124 – 126

3

Beta strand

133 – 135

3

Helix

144 – 156

13

Beta strand

159 – 167

9

Helix

170 – 177

8

Beta strand

187 – 192

6

Helix

200 – 208

9

Beta strand

212 – 217

6

Turn

225 – 227

3

Helix

235 – 237

3

Helix

239 – 248

10

Helix

252 – 262

11

Beta strand

266 – 270

5

Helix

274 – 280

7

Helix

281 – 285

5

Helix

290 – 297

8

Helix

309 – 312

4

Helix

318 – 320

3

Sequences

	Sequence		Length	Mass (Da)
	P42330 [UniParc]. Last modified October 5, 2010. Version 4. Checksum: 86A7690D9498C6FD	FASTA	323	36,853
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S68288 mRNA. Translation: AAD14011.1.
L43839 , 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.

IPI

IPI00291483.

PIR

B57407.
I73674.

RefSeq

NP_001240837.1. NM_001253908.1.
NP_003730.4. NM_003739.5.

UniGene

Hs.78183.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RY0	X-ray	1.69	A/B	1-323	[»]
1RY8	X-ray	1.69	A/B	1-323	[»]
1S1P	X-ray	1.20	A	1-323	[»]
1S1R	X-ray	2.00	A	1-323	[»]
1S2A	X-ray	1.70	A	1-323	[»]
1S2C	X-ray	1.80	A	1-323	[»]
1XF0	X-ray	2.00	A	1-323	[»]
1ZQ5	X-ray	1.30	A	1-323	[»]
2F38	X-ray	2.00	A	1-323	[»]
2FGB	X-ray	1.35	A	1-323	[»]
3R43	X-ray	2.00	A	1-323	[»]
3R58	X-ray	2.30	A	1-323	[»]
3R6I	X-ray	1.95	A	1-323	[»]
3R7M	X-ray	2.10	A	1-323	[»]
3R8G	X-ray	1.80	A	1-323	[»]
3R8H	X-ray	1.90	A	1-323	[»]
3R94	X-ray	2.01	A	1-323	[»]
3UFY	X-ray	1.90	A	1-323	[»]
3UG8	X-ray	1.73	A	1-323	[»]
3UGR	X-ray	1.65	A	1-323	[»]
3UWE	X-ray	1.68	A	1-323	[»]
4DBS	X-ray	1.85	A/B	1-323	[»]
4DBU	X-ray	2.53	A/B	1-323	[»]
4DBW	X-ray	1.80	A/B	1-323	[»]
4DZ5	X-ray	1.70	A	1-323	[»]
4FA3	X-ray	2.20	A	1-323	[»]
4FAL	X-ray	2.00	A	1-323	[»]
4FAM	X-ray	2.00	A/B	1-323	[»]

ProteinModelPortal

P42330.

SMR

P42330. Positions 6-320.

ModBase

Search...

Protein-protein interaction databases

IntAct

P42330. 5 interactions.

MINT

MINT-1379107.

PTM databases

PhosphoSite

P42330.

Polymorphism databases

DMDM

308153646.

2D gel databases

DOSAC-COBS-2DPAGE

P42330.

Proteomic databases

PaxDb

P42330.

PRIDE

P42330.

Protocols and materials databases

DNASU

8644.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380554; ENSP00000369927; ENSG00000196139.
ENST00000583876; ENSP00000464178; ENSG00000265685.

GeneID

8644.

KEGG

hsa:8644.

UCSC

uc001ihr.3. human.

Organism-specific databases

CTD

8644.

GeneCards

GC10P005077.

HGNC

HGNC:386. AKR1C3.

HPA

CAB010874.

MIM

603966. gene.

neXtProt

NX_P42330.

PharmGKB

PA24679.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0656.

HOVERGEN

HBG000020.

InParanoid

P42330.

KO

K00089.
K00212.
K04119.

OMA

PEVPRSK.

OrthoDB

EOG4Q2DG2.

PhylomeDB

P42330.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P42330.

Gene expression databases

ArrayExpress

P42330.

Bgee

P42330.

CleanEx

HS_AKR1C3.

Genevestigator

P42330.

GermOnline

ENSG00000196139. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P42330.

ChEMBL

CHEMBL4681.

DrugBank

DB01093. Dimethyl sulfoxide.
DB00157. NADH.

EvolutionaryTrace

P42330.

GenomeRNAi

8644.

NextBio

32407.

SOURCE

Search...

Entry information

Entry name

AK1C3_HUMAN

Accession

Primary (citable) accession number: P42330
Secondary accession number(s): A8K2V0 , 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:	May 1, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.