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P42330

- AK1C3_HUMAN

UniProt

P42330 - AK1C3_HUMAN

Protein

Aldo-keto reductase family 1 member C3

Gene

AKR1C3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    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 activityi

    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 regulationi

    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).

    Kineticsi

    1. KM=142.1 µM for progesterone1 Publication
    2. KM=2.37 µM for 5-alpha-dihydrotestosterone1 Publication
    3. KM=1.0 µM for androstanediol1 Publication

    Vmax=20.1 nmol/min/mg enzyme with progesterone as substrate1 Publication

    Vmax=1.8 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone as substrate1 Publication

    Vmax=4.4 nmol/min/mg enzyme with androstanediol as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei54 – 541Important for substrate specificityBy similarity
    Active sitei55 – 551Proton donorBy similarity
    Sitei84 – 841Lowers pKa of active site TyrBy similarity
    Binding sitei117 – 1171SubstrateBy similarity
    Sitei227 – 2271Involved in ligand recognition and product release
    Sitei306 – 3061Involved in ligand recognition and product release

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 2210NADPSequence Analysis
    Nucleotide bindingi217 – 28064NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity Source: UniProtKB
    2. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    3. aldo-keto reductase (NADP) activity Source: UniProtKB
    4. androsterone dehydrogenase activity Source: UniProtKB
    5. delta4-3-oxosteroid 5beta-reductase activity Source: UniProtKB
    6. dihydrotestosterone 17-beta-dehydrogenase activity Source: UniProtKB
    7. geranylgeranyl reductase activity Source: UniProtKB
    8. indanol dehydrogenase activity Source: UniProtKB-EC
    9. ketoreductase activity Source: UniProtKB
    10. ketosteroid monooxygenase activity Source: UniProtKB
    11. oxidoreductase activity Source: InterPro
    12. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    13. phenanthrene 9,10-monooxygenase activity Source: UniProtKB
    14. prostaglandin D2 11-ketoreductase activity Source: UniProtKB-EC
    15. prostaglandin F receptor activity Source: UniProtKB
    16. prostaglandin-F synthase activity Source: UniProtKB-EC
    17. retinal dehydrogenase activity Source: UniProtKB
    18. retinol dehydrogenase activity Source: UniProtKB
    19. testosterone 17-beta-dehydrogenase (NADP+) activity Source: UniProtKB-EC
    20. testosterone dehydrogenase (NAD+) activity Source: UniProtKB-EC
    21. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. cellular response to cadmium ion Source: UniProtKB
    3. cellular response to calcium ion Source: UniProtKB
    4. cellular response to corticosteroid stimulus Source: UniProtKB
    5. cellular response to jasmonic acid stimulus Source: UniProtKB
    6. cellular response to prostaglandin stimulus Source: UniProtKB
    7. cellular response to reactive oxygen species Source: UniProtKB
    8. cellular response to starvation Source: UniProtKB
    9. cyclooxygenase pathway Source: Reactome
    10. daunorubicin metabolic process Source: UniProtKB
    11. doxorubicin metabolic process Source: UniProtKB
    12. farnesol catabolic process Source: UniProtKB
    13. G-protein coupled receptor signaling pathway Source: UniProtKB
    14. keratinocyte differentiation Source: UniProtKB
    15. male gonad development Source: UniProtKB
    16. multicellular organismal macromolecule metabolic process Source: UniProtKB
    17. negative regulation of retinoic acid biosynthetic process Source: UniProtKB
    18. oxidation-reduction process Source: UniProtKB
    19. phototransduction, visible light Source: Reactome
    20. positive regulation of cell death Source: UniProtKB
    21. positive regulation of cell proliferation Source: UniProtKB
    22. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    23. positive regulation of protein kinase B signaling Source: UniProtKB
    24. positive regulation of reactive oxygen species metabolic process Source: UniProtKB
    25. progesterone metabolic process Source: UniProtKB
    26. prostaglandin metabolic process Source: UniProtKB
    27. protein import into nucleus, translocation Source: UniProtKB
    28. regulation of retinoic acid receptor signaling pathway Source: UniProtKB
    29. regulation of testosterone biosynthetic process Source: UniProtKB
    30. renal absorption Source: UniProtKB
    31. response to nutrient Source: UniProtKB
    32. response to prostaglandin Source: UniProtKB
    33. retinal metabolic process Source: UniProtKB
    34. retinoid metabolic process Source: Reactome
    35. small molecule metabolic process Source: Reactome
    36. steroid metabolic process Source: UniProtKB
    37. testosterone biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_24968. Retinoid metabolism and transport.
    SABIO-RKP42330.

    Names & Taxonomyi

    Protein namesi
    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 (EC:1.1.1.357)
    Short name:
    3-alpha-HSD type 2
    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 (EC:1.1.1.188)
    Short name:
    PGFS
    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 namesi
    Name:AKR1C3
    Synonyms:DDH1, HSD17B5, KIAA0119, PGFS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:386. AKR1C3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. intracellular Source: LIFEdb
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751K → E: No effect on 17beta-HSD activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24679.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Aldo-keto reductase family 1 member C3PRO_0000124638Add
    BLAST

    Proteomic databases

    MaxQBiP42330.
    PaxDbiP42330.
    PRIDEiP42330.

    2D gel databases

    DOSAC-COBS-2DPAGEP42330.

    PTM databases

    PhosphoSiteiP42330.

    Expressioni

    Tissue specificityi

    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.6 Publications

    Gene expression databases

    ArrayExpressiP42330.
    BgeeiP42330.
    CleanExiHS_AKR1C3.
    GenevestigatoriP42330.

    Organism-specific databases

    HPAiCAB010874.

    Interactioni

    Protein-protein interaction databases

    BioGridi114196. 5 interactions.
    IntActiP42330. 5 interactions.
    MINTiMINT-1379107.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Beta strandi15 – 228
    Helixi33 – 4412
    Beta strandi48 – 503
    Helixi53 – 553
    Helixi58 – 7013
    Helixi76 – 783
    Beta strandi80 – 856
    Helixi87 – 893
    Helixi92 – 943
    Helixi95 – 10612
    Beta strandi111 – 1166
    Beta strandi124 – 1263
    Beta strandi133 – 1353
    Helixi144 – 15613
    Beta strandi159 – 1679
    Helixi170 – 1778
    Beta strandi187 – 1926
    Helixi200 – 2089
    Beta strandi212 – 2176
    Turni225 – 2273
    Helixi235 – 2373
    Helixi239 – 24810
    Helixi252 – 26211
    Beta strandi266 – 2705
    Helixi274 – 2807
    Helixi281 – 2855
    Helixi290 – 2978
    Helixi309 – 3124
    Helixi318 – 3203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP42330.
    SMRiP42330. Positions 6-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42330.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    HOVERGENiHBG000020.
    InParanoidiP42330.
    KOiK04119.
    OMAiFDIVDLC.
    PhylomeDBiP42330.
    TreeFamiTF106492.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42330-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID    50
    SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE 100
    NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA 150
    MEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNRS 200
    KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR 250
    TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD 300
    RNLHYFNSDS FASHPNYPYS DEY 323
    Length:323
    Mass (Da):36,853
    Last modified:October 5, 2010 - v4
    Checksum:i86A7690D9498C6FD
    GO
    Isoform 2 (identifier: P42330-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-119: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:204
    Mass (Da):23,364
    Checksum:i02F3AC7C2BB5BF78
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31S → P no nucleotide entry (PubMed:7626489)Curated
    Sequence conflicti6 – 61Q → K no nucleotide entry (PubMed:7626489)Curated
    Sequence conflicti38 – 381T → S in AAF07272. (PubMed:10557352)Curated
    Sequence conflicti75 – 751K → E in AAD14011. (PubMed:8274401)Curated
    Sequence conflicti75 – 751K → E no nucleotide entry (PubMed:7626489)Curated
    Sequence conflicti75 – 751K → M in AAB41916. (PubMed:7650035)Curated
    Sequence conflicti89 – 891F → S in AAF07272. (PubMed:10557352)Curated
    Sequence conflicti270 – 2701K → R in AAF07272. (PubMed:10557352)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51H → Q.7 Publications
    Corresponds to variant rs12529 [ dbSNP | Ensembl ].
    VAR_013288
    Natural varianti66 – 661R → Q.
    Corresponds to variant rs35961894 [ dbSNP | Ensembl ].
    VAR_032767
    Natural varianti77 – 771E → G.
    Corresponds to variant rs41306308 [ dbSNP | Ensembl ].
    VAR_061001
    Natural varianti170 – 1701R → C.
    Corresponds to variant rs35575889 [ dbSNP | Ensembl ].
    VAR_032768
    Natural varianti175 – 1751M → I No effect on 17beta-HSD activity. 2 Publications
    Corresponds to variant rs1131132 [ dbSNP | Ensembl ].
    VAR_013289
    Natural varianti180 – 1801P → S.
    Corresponds to variant rs34186955 [ dbSNP | Ensembl ].
    VAR_032769

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 119119Missing in isoform 2. 1 PublicationVSP_055798Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    AK296829 mRNA. Translation: BAG59399.1.
    AL391427 Genomic DNA. No translation available.
    CH471072 Genomic DNA. Translation: EAW86454.1.
    BC001479 mRNA. Translation: AAH01479.1.
    BC019230 mRNA. Translation: AAH19230.1.
    CCDSiCCDS7063.1.
    PIRiB57407.
    I73674.
    RefSeqiNP_001240837.1. NM_001253908.1.
    NP_003730.4. NM_003739.5.
    UniGeneiHs.78183.

    Genome annotation databases

    EnsembliENST00000380554; ENSP00000369927; ENSG00000196139. [P42330-1]
    ENST00000439082; ENSP00000401327; ENSG00000196139. [P42330-2]
    GeneIDi8644.
    KEGGihsa:8644.
    UCSCiuc001ihr.3. human.

    Polymorphism databases

    DMDMi308153646.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    AK296829 mRNA. Translation: BAG59399.1 .
    AL391427 Genomic DNA. No translation available.
    CH471072 Genomic DNA. Translation: EAW86454.1 .
    BC001479 mRNA. Translation: AAH01479.1 .
    BC019230 mRNA. Translation: AAH19230.1 .
    CCDSi CCDS7063.1.
    PIRi B57407.
    I73674.
    RefSeqi NP_001240837.1. NM_001253908.1.
    NP_003730.4. NM_003739.5.
    UniGenei Hs.78183.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    4H7C X-ray 1.97 A 1-323 [» ]
    4HMN X-ray 2.40 A 1-323 [» ]
    ProteinModelPortali P42330.
    SMRi P42330. Positions 6-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114196. 5 interactions.
    IntActi P42330. 5 interactions.
    MINTi MINT-1379107.

    Chemistry

    BindingDBi P42330.
    ChEMBLi CHEMBL4681.
    DrugBanki DB00905. Bimatoprost.
    DB00997. Doxorubicin.

    PTM databases

    PhosphoSitei P42330.

    Polymorphism databases

    DMDMi 308153646.

    2D gel databases

    DOSAC-COBS-2DPAGE P42330.

    Proteomic databases

    MaxQBi P42330.
    PaxDbi P42330.
    PRIDEi P42330.

    Protocols and materials databases

    DNASUi 8644.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380554 ; ENSP00000369927 ; ENSG00000196139 . [P42330-1 ]
    ENST00000439082 ; ENSP00000401327 ; ENSG00000196139 . [P42330-2 ]
    GeneIDi 8644.
    KEGGi hsa:8644.
    UCSCi uc001ihr.3. human.

    Organism-specific databases

    CTDi 8644.
    GeneCardsi GC10P005077.
    HGNCi HGNC:386. AKR1C3.
    HPAi CAB010874.
    MIMi 603966. gene.
    neXtProti NX_P42330.
    PharmGKBi PA24679.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOVERGENi HBG000020.
    InParanoidi P42330.
    KOi K04119.
    OMAi FDIVDLC.
    PhylomeDBi P42330.
    TreeFami TF106492.

    Enzyme and pathway databases

    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_24968. Retinoid metabolism and transport.
    SABIO-RK P42330.

    Miscellaneous databases

    EvolutionaryTracei P42330.
    GeneWikii AKR1C3.
    GenomeRNAii 8644.
    NextBioi 32407.
    PROi P42330.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42330.
    Bgeei P42330.
    CleanExi HS_AKR1C3.
    Genevestigatori P42330.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    PANTHERi PTHR11732. PTHR11732. 1 hit.
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000097. AKR. 1 hit.
    PRINTSi PR00069. ALDKETRDTASE.
    SUPFAMi SSF51430. SSF51430. 1 hit.
    PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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] (ISOFORM 1).
      Tissue: Colon and Urinary bladder.
    15. "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.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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.
    18. "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.
    19. "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.

    Entry informationi

    Entry nameiAK1C3_HUMAN
    AccessioniPrimary (citable) accession number: P42330
    Secondary accession number(s): A8K2V0
    , B4DL37, Q5T2L1, Q96DJ1, Q96KI8, Q99530, Q9UCX1, Q9UII3, Q9UKL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 159 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3