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Protein

3-oxo-5-beta-steroid 4-dehydrogenase

Gene

AKR1D1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.1 Publication

Catalytic activityi

5-beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH.1 Publication
17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH.1 Publication

Enzyme regulationi

Subject to inhibition by high substrate concentrations. Inhibited by testosterone concentrations above 10 µM.1 Publication

Kineticsi

  1. KM=2.7 µM for testosterone1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei26 – 261Substrate
    Binding sitei53 – 531NADP5 Publications
    Active sitei58 – 581Proton donor
    Binding sitei58 – 581Substrate
    Binding sitei89 – 891Substrate
    Binding sitei120 – 1201Substrate
    Binding sitei132 – 1321Substrate
    Binding sitei193 – 1931NADP5 Publications
    Binding sitei230 – 2301Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 265NADP5 Publications
    Nucleotide bindingi169 – 1702NADP5 Publications
    Nucleotide bindingi219 – 2246NADP5 Publications
    Nucleotide bindingi273 – 28311NADP5 PublicationsAdd
    BLAST

    GO - Molecular functioni

    • delta4-3-oxosteroid 5beta-reductase activity Source: UniProtKB-EC
    • steroid binding Source: UniProtKB

    GO - Biological processi

    • androgen metabolic process Source: UniProtKB
    • bile acid biosynthetic process Source: UniProtKB
    • bile acid catabolic process Source: UniProtKB-KW
    • bile acid metabolic process Source: Reactome
    • C21-steroid hormone metabolic process Source: UniProtKB
    • cholesterol catabolic process Source: UniProtKB
    • digestion Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.3.1.3. 2681.
    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.
    SABIO-RKP51857.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxo-5-beta-steroid 4-dehydrogenase (EC:1.3.1.31 Publication)
    Alternative name(s):
    Aldo-keto reductase family 1 member D1
    Delta(4)-3-ketosteroid 5-beta-reductase
    Delta(4)-3-oxosteroid 5-beta-reductase
    Gene namesi
    Name:AKR1D1
    Synonyms:SRD5B1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:388. AKR1D1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Congenital bile acid synthesis defect 2 (CBAS2)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA condition characterized by jaundice, intrahepatic cholestasis and hepatic failure. Patients with this liver disease show absence or low levels of chenodeoxycholic acid and cholic acid in plasma and urine.

    See also OMIM:235555
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061L → F in CBAS2. 1 Publication
    VAR_033007
    Natural varianti133 – 1331P → R in CBAS2. 1 Publication
    VAR_044430
    Natural varianti198 – 1981P → L in CBAS2. 1 Publication
    VAR_033008
    Natural varianti261 – 2611R → C in CBAS2. 1 Publication
    VAR_044431

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi58 – 581Y → A: Loss of activity. 1 Publication
    Mutagenesisi120 – 1201E → A: Loss of activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Intrahepatic cholestasis

    Organism-specific databases

    MIMi235555. phenotype.
    Orphaneti79303. Congenital bile acid synthesis defect type 2.
    PharmGKBiPA24681.

    Chemistry

    DrugBankiDB00548. Azelaic Acid.
    DB01216. Finasteride.

    Polymorphism and mutation databases

    BioMutaiAKR1D1.
    DMDMi1703007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3263263-oxo-5-beta-steroid 4-dehydrogenasePRO_0000124669Add
    BLAST

    Proteomic databases

    MaxQBiP51857.
    PaxDbiP51857.
    PRIDEiP51857.

    PTM databases

    PhosphoSiteiP51857.

    Expressioni

    Tissue specificityi

    Highly expressed in liver. Expressed in testis and weakly in colon.1 Publication

    Gene expression databases

    BgeeiP51857.
    CleanExiHS_AKR1D1.
    ExpressionAtlasiP51857. baseline and differential.
    GenevisibleiP51857. HS.

    Organism-specific databases

    HPAiHPA057002.

    Interactioni

    Protein-protein interaction databases

    BioGridi112596. 6 interactions.
    STRINGi9606.ENSP00000242375.

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 113Combined sources
    Beta strandi17 – 215Combined sources
    Turni29 – 313Combined sources
    Helixi36 – 4712Combined sources
    Beta strandi51 – 533Combined sources
    Helixi56 – 583Combined sources
    Helixi61 – 7313Combined sources
    Helixi79 – 813Combined sources
    Beta strandi83 – 886Combined sources
    Helixi90 – 923Combined sources
    Helixi95 – 973Combined sources
    Helixi98 – 10912Combined sources
    Beta strandi114 – 1207Combined sources
    Helixi147 – 15913Combined sources
    Beta strandi162 – 1709Combined sources
    Helixi173 – 1808Combined sources
    Beta strandi191 – 1955Combined sources
    Helixi203 – 2119Combined sources
    Beta strandi215 – 2206Combined sources
    Turni228 – 2303Combined sources
    Helixi238 – 2403Combined sources
    Helixi242 – 2509Combined sources
    Helixi255 – 26511Combined sources
    Helixi277 – 2848Combined sources
    Helixi293 – 3008Combined sources
    Helixi312 – 3143Combined sources
    Beta strandi321 – 3244Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BURX-ray1.62A/B1-326[»]
    3BUVX-ray1.35A/B1-326[»]
    3BV7X-ray1.79A/B1-326[»]
    3CAQX-ray2.20A/B1-326[»]
    3CASX-ray2.00A/B1-326[»]
    3CAVX-ray1.90A/B1-326[»]
    3CMFX-ray1.90A/B1-326[»]
    3COTX-ray2.03A/B1-326[»]
    3DOPX-ray2.00A/B1-326[»]
    3G1RX-ray1.70A/B1-326[»]
    3UZWX-ray1.89A/B1-326[»]
    3UZXX-ray1.64A/B1-326[»]
    3UZYX-ray1.83A/B1-326[»]
    3UZZX-ray1.82A/B1-326[»]
    ProteinModelPortaliP51857.
    SMRiP51857. Positions 2-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51857.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP51857.
    KOiK00251.
    OMAiLYQNEHE.
    OrthoDBiEOG70KGQF.
    PhylomeDBiP51857.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P51857-1) [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

            10         20         30         40         50
    MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR
    60 70 80 90 100
    HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP
    110 120 130 140 150
    TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT
    160 170 180 190 200
    WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF
    210 220 230 240 250
    TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR
    260 270 280 290 300
    YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE
    310 320
    ALNKNVRFVE LLMWRDHPEY PFHDEY
    Length:326
    Mass (Da):37,377
    Last modified:October 1, 1996 - v1
    Checksum:i1FE02B95398A0A6F
    GO
    Isoform 2 (identifier: P51857-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         286-326: IFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY → VARSS

    Note: No experimental confirmation available.
    Show »
    Length:290
    Mass (Da):32,748
    Checksum:iF2C7686DA906C0EC
    GO
    Isoform 3 (identifier: P51857-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-193: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:285
    Mass (Da):32,890
    Checksum:i5017C36EB0EB13D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141D → V in BAF82114 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061L → F in CBAS2. 1 Publication
    VAR_033007
    Natural varianti133 – 1331P → R in CBAS2. 1 Publication
    VAR_044430
    Natural varianti198 – 1981P → L in CBAS2. 1 Publication
    VAR_033008
    Natural varianti261 – 2611R → C in CBAS2. 1 Publication
    VAR_044431

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei153 – 19341Missing in isoform 3. 1 PublicationVSP_042913Add
    BLAST
    Alternative sequencei286 – 32641IFDFS…FHDEY → VARSS in isoform 2. 1 PublicationVSP_042901Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28339 mRNA. Translation: CAA82193.1.
    AF283659
    , AF283651, AF283652, AF283653, AF283654, AF283655, AF283656, AF283657, AF283658 Genomic DNA. Translation: AAG39381.1.
    AK289425 mRNA. Translation: BAF82114.1.
    AK298421 mRNA. Translation: BAG60645.1.
    AK298428 mRNA. Translation: BAG60650.1.
    AC009263 Genomic DNA. No translation available.
    AC024082 Genomic DNA. No translation available.
    AC083867 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24049.1.
    CH471070 Genomic DNA. Translation: EAW83881.1.
    BC130625 mRNA. Translation: AAI30626.1.
    BC130627 mRNA. Translation: AAI30628.1.
    CCDSiCCDS55169.1. [P51857-2]
    CCDS55170.1. [P51857-3]
    CCDS5846.1. [P51857-1]
    PIRiS41120.
    RefSeqiNP_001177835.1. NM_001190906.1. [P51857-3]
    NP_001177836.1. NM_001190907.1. [P51857-2]
    NP_005980.1. NM_005989.3. [P51857-1]
    UniGeneiHs.201667.
    Hs.740214.

    Genome annotation databases

    EnsembliENST00000242375; ENSP00000242375; ENSG00000122787. [P51857-1]
    ENST00000411726; ENSP00000402374; ENSG00000122787. [P51857-3]
    ENST00000432161; ENSP00000389197; ENSG00000122787. [P51857-2]
    GeneIDi6718.
    KEGGihsa:6718.
    UCSCiuc003vtz.3. human. [P51857-1]
    uc011kqe.1. human. [P51857-2]
    uc011kqf.2. human. [P51857-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z28339 mRNA. Translation: CAA82193.1.
    AF283659
    , AF283651, AF283652, AF283653, AF283654, AF283655, AF283656, AF283657, AF283658 Genomic DNA. Translation: AAG39381.1.
    AK289425 mRNA. Translation: BAF82114.1.
    AK298421 mRNA. Translation: BAG60645.1.
    AK298428 mRNA. Translation: BAG60650.1.
    AC009263 Genomic DNA. No translation available.
    AC024082 Genomic DNA. No translation available.
    AC083867 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24049.1.
    CH471070 Genomic DNA. Translation: EAW83881.1.
    BC130625 mRNA. Translation: AAI30626.1.
    BC130627 mRNA. Translation: AAI30628.1.
    CCDSiCCDS55169.1. [P51857-2]
    CCDS55170.1. [P51857-3]
    CCDS5846.1. [P51857-1]
    PIRiS41120.
    RefSeqiNP_001177835.1. NM_001190906.1. [P51857-3]
    NP_001177836.1. NM_001190907.1. [P51857-2]
    NP_005980.1. NM_005989.3. [P51857-1]
    UniGeneiHs.201667.
    Hs.740214.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BURX-ray1.62A/B1-326[»]
    3BUVX-ray1.35A/B1-326[»]
    3BV7X-ray1.79A/B1-326[»]
    3CAQX-ray2.20A/B1-326[»]
    3CASX-ray2.00A/B1-326[»]
    3CAVX-ray1.90A/B1-326[»]
    3CMFX-ray1.90A/B1-326[»]
    3COTX-ray2.03A/B1-326[»]
    3DOPX-ray2.00A/B1-326[»]
    3G1RX-ray1.70A/B1-326[»]
    3UZWX-ray1.89A/B1-326[»]
    3UZXX-ray1.64A/B1-326[»]
    3UZYX-ray1.83A/B1-326[»]
    3UZZX-ray1.82A/B1-326[»]
    ProteinModelPortaliP51857.
    SMRiP51857. Positions 2-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi112596. 6 interactions.
    STRINGi9606.ENSP00000242375.

    Chemistry

    DrugBankiDB00548. Azelaic Acid.
    DB01216. Finasteride.

    PTM databases

    PhosphoSiteiP51857.

    Polymorphism and mutation databases

    BioMutaiAKR1D1.
    DMDMi1703007.

    Proteomic databases

    MaxQBiP51857.
    PaxDbiP51857.
    PRIDEiP51857.

    Protocols and materials databases

    DNASUi6718.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000242375; ENSP00000242375; ENSG00000122787. [P51857-1]
    ENST00000411726; ENSP00000402374; ENSG00000122787. [P51857-3]
    ENST00000432161; ENSP00000389197; ENSG00000122787. [P51857-2]
    GeneIDi6718.
    KEGGihsa:6718.
    UCSCiuc003vtz.3. human. [P51857-1]
    uc011kqe.1. human. [P51857-2]
    uc011kqf.2. human. [P51857-3]

    Organism-specific databases

    CTDi6718.
    GeneCardsiGC07P137687.
    HGNCiHGNC:388. AKR1D1.
    HPAiHPA057002.
    MIMi235555. phenotype.
    604741. gene.
    neXtProtiNX_P51857.
    Orphaneti79303. Congenital bile acid synthesis defect type 2.
    PharmGKBiPA24681.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP51857.
    KOiK00251.
    OMAiLYQNEHE.
    OrthoDBiEOG70KGQF.
    PhylomeDBiP51857.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BRENDAi1.3.1.3. 2681.
    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.
    SABIO-RKP51857.

    Miscellaneous databases

    EvolutionaryTraceiP51857.
    GenomeRNAii6718.
    NextBioi26206.
    PROiP51857.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP51857.
    CleanExiHS_AKR1D1.
    ExpressionAtlasiP51857. baseline and differential.
    GenevisibleiP51857. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme."
      Kondo K.-H., Kai M.-H., Setoguchi Y., Eggertsen G., Sjoeblom P., Setoguchi T., Okuda K., Bjoerkhem I.
      Eur. J. Biochem. 219:357-363(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme."
      Charbonneau A., The V.L.
      Biochim. Biophys. Acta 1517:228-235(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.
    3. "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; 2 AND 3).
      Tissue: Liver and Mammary gland.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "The crystal structure of human Delta4-3-ketosteroid 5beta-reductase defines the functional role of the residues of the catalytic tetrad in the steroid double bond reduction mechanism."
      Faucher F., Cantin L., Luu-The V., Labrie F., Breton R.
      Biochemistry 47:8261-8270(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP.
    11. "Crystal structures of human Delta4-3-ketosteroid 5beta-reductase (AKR1D1) reveal the presence of an alternative binding site responsible for substrate inhibition."
      Faucher F., Cantin L., Luu-The V., Labrie F., Breton R.
      Biochemistry 47:13537-13546(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP.
    12. "Crystal structure of human liver delta(4)-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis."
      Di Costanzo L., Drury J.E., Penning T.M., Christianson D.W.
      J. Biol. Chem. 283:16830-16839(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEXES WITH NADP; TESTOSTERONE; PROGESTERONE AND CORTISONE, MUTAGENESIS OF TYR-58 AND GLU-120, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Inhibition of human steroid 5beta-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex."
      Drury J.E., Di Costanzo L., Penning T.M., Christianson D.W.
      J. Biol. Chem. 284:19786-19790(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NADP.
    14. "Structure and catalytic mechanism of human steroid 5beta-reductase (AKR1D1)."
      Di Costanzo L., Drury J.E., Christianson D.W., Penning T.M.
      Mol. Cell. Endocrinol. 301:191-198(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP.
    15. "Conversion of human steroid 5beta-reductase (AKR1D1) into 3beta-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering."
      Chen M., Drury J.E., Christianson D.W., Penning T.M.
      J. Biol. Chem. 287:16609-16622(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH NADP AND TESTOSTERONE.
    16. "Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5beta-reductase, in hepatitis and liver failure in infancy."
      Lemonde H.A., Custard E.J., Bouquet J., Duran M., Overmars H., Scambler P.J., Clayton P.T.
      Gut 52:1494-1499(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CBAS2 PHE-106 AND LEU-198.
    17. "SRD5B1 (AKR1D1) gene analysis in delta(4)-3-oxosteroid 5beta-reductase deficiency: evidence for primary genetic defect."
      Gonzales E., Cresteil D., Baussan C., Dabadie A., Gerhardt M.F., Jacquemin E.
      J. Hepatol. 40:716-718(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CBAS2 ARG-133 AND CYS-261.

    Entry informationi

    Entry nameiAK1D1_HUMAN
    AccessioniPrimary (citable) accession number: P51857
    Secondary accession number(s): A1L4P6
    , A8K060, B4DPN3, B4DPN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: June 24, 2015
    This is version 134 of the entry and version 1 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 7
      Human chromosome 7: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.