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Protein

Aldo-keto reductase family 1 member C21

Gene

Akr1c21

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids.5 Publications

Catalytic activityi

Androsterone + NAD(P)+ = 5-alpha-androstane-3,17-dione + NAD(P)H.3 Publications

Enzyme regulationi

Inhibited by high concentrations of substrate.1 Publication

Kineticsi

  1. KM=1.8 µM for NADP2 Publications
  2. KM=19 µM for androstenedione2 Publications
  3. KM=0.5 µM for 5-beta-pregnane-3-alpha,20-alpha-diol2 Publications
  4. KM=0.5 µM for 5-beta-pregnane-3,20-dione2 Publications
  5. KM=0.6 µM for epitestosterone2 Publications
  6. KM=0.3 µM for androst-4-ene-3,17-dione2 Publications

    pH dependencei

    Optimum pH is 10.0.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei31 – 311Substrate
    Binding sitei50 – 501NADP3 Publications
    Active sitei55 – 551Proton donor
    Sitei84 – 841Lowers pKa of active site TyrBy similarity
    Binding sitei117 – 1171Substrate
    Binding sitei190 – 1901NADP3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 245NADP3 Publications
    Nucleotide bindingi166 – 1672NADP3 Publications
    Nucleotide bindingi216 – 2249NADP3 Publications
    Nucleotide bindingi270 – 28011NADP3 PublicationsAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.148. 3474.
    1.1.1.209. 3474.
    1.1.1.50. 3474.
    ReactomeiREACT_283453. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_292237. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_295031. Retinoid metabolism and transport.
    REACT_310468. RA biosynthesis pathway.
    REACT_325766. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_349058. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RKQ91WR5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member C21 (EC:1.1.1.-)
    Alternative name(s):
    17-alpha-hydroxysteroid dehydrogenase
    Short name:
    17-alpha-HSD
    3(or 17)-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.209)
    3-alpha-hydroxysteroid dehydrogenase
    Dihydrodiol dehydrogenase type 1
    Short name:
    DD1
    Dihydrodiol dehydrogenase type 3
    Short name:
    DD3
    Gene namesi
    Name:Akr1c21
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 13

    Organism-specific databases

    MGIiMGI:1924587. Akr1c21.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241A → Y: Reduces enzyme activity and affinity for substrate. Alters the stereospecificity, so that androstenedione is converted to testosterone. 1 Publication
    Mutagenesisi31 – 311K → A: No effect on affinity for androstenedione. Slight increase of catalytic activity. 1 Publication
    Mutagenesisi222 – 2221Q → N: Decreases affinity for NADP. Changes enzyme activity, leading to the production of testosterone and concomitantly reducing the production of epi-testosterone. 1 Publication
    Mutagenesisi224 – 2241Y → D: Decreases affinity for NADP. Changes enzyme activity, leading to the production of testosterone and concomitantly reducing the production of epi-testosterone. 1 Publication
    Mutagenesisi224 – 2241Y → F: No effect on enzyme activity. Decreases affinity for NADP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Aldo-keto reductase family 1 member C21PRO_0000326222Add
    BLAST

    Proteomic databases

    MaxQBiQ91WR5.
    PaxDbiQ91WR5.
    PRIDEiQ91WR5.

    PTM databases

    PhosphoSiteiQ91WR5.

    Expressioni

    Tissue specificityi

    Detected in kidney and brain.2 Publications

    Gene expression databases

    BgeeiQ91WR5.
    CleanExiMM_AKR1C21.
    GenevisibleiQ91WR5. MM.

    Interactioni

    Subunit structurei

    Monomer.5 Publications

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000021628.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Beta strandi15 – 228Combined sources
    Beta strandi27 – 293Combined sources
    Helixi33 – 4412Combined sources
    Beta strandi48 – 503Combined sources
    Helixi53 – 553Combined sources
    Helixi58 – 7013Combined sources
    Helixi76 – 783Combined sources
    Beta strandi80 – 856Combined sources
    Helixi87 – 893Combined sources
    Turni92 – 943Combined sources
    Helixi95 – 10612Combined sources
    Beta strandi111 – 1177Combined sources
    Beta strandi121 – 1233Combined sources
    Beta strandi125 – 1295Combined sources
    Helixi144 – 15613Combined sources
    Beta strandi159 – 1679Combined sources
    Helixi170 – 1778Combined sources
    Beta strandi187 – 1926Combined sources
    Beta strandi194 – 1974Combined sources
    Helixi200 – 2089Combined sources
    Beta strandi212 – 2165Combined sources
    Turni225 – 2273Combined sources
    Helixi228 – 2314Combined sources
    Helixi235 – 2373Combined sources
    Helixi239 – 24810Combined sources
    Helixi252 – 26110Combined sources
    Turni262 – 2643Combined sources
    Beta strandi266 – 2694Combined sources
    Helixi274 – 2807Combined sources
    Helixi281 – 2855Combined sources
    Helixi290 – 2978Combined sources
    Helixi309 – 3113Combined sources
    Beta strandi318 – 3214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HE5X-ray2.90A/B/C/D1-323[»]
    2HE8X-ray1.90A/B1-323[»]
    2HEJX-ray1.35A/B1-323[»]
    2IPFX-ray1.85A/B6-323[»]
    2IPGX-ray1.90A/B5-323[»]
    2P5NX-ray1.80A/B1-323[»]
    3CV6X-ray2.10A/B1-323[»]
    3FJNX-ray2.30A/B1-323[»]
    DisProtiDP00690.
    ProteinModelPortaliQ91WR5.
    SMRiQ91WR5. Positions 6-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ91WR5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ91WR5.
    OMAiNTEDHVG.
    OrthoDBiEOG70KGQF.
    PhylomeDBiQ91WR5.
    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.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q91WR5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD
    60 70 80 90 100
    SASVYNTEDH VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE
    110 120 130 140 150
    RSLQKLQFDY VDLYLIHYPM ALKPGEENFP VDEHGKLIFD RVDLCATWEA
    160 170 180 190 200
    MEKCKDAGLT KSIGVSNFNY RQLEMILNKP GLKYKPVCNQ VECHPYLNQM
    210 220 230 240 250
    KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV LGSMAKKYNR
    260 270 280 290 300
    TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN
    310 320
    RNMRYIPAAI FKGHPNWPFL DEY
    Length:323
    Mass (Da):36,877
    Last modified:March 18, 2008 - v2
    Checksum:i0D598A0559EFBF11
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271L → V in BAD18929 (PubMed:15577209).Curated
    Sequence conflicti27 – 271L → V in AAH13531 (PubMed:15489334).Curated
    Sequence conflicti27 – 271L → V in AAH91761 (PubMed:15489334).Curated
    Sequence conflicti60 – 601H → R in BAD18929 (PubMed:15577209).Curated
    Sequence conflicti60 – 601H → R in AAH13531 (PubMed:15489334).Curated
    Sequence conflicti60 – 601H → R in AAH91761 (PubMed:15489334).Curated
    Sequence conflicti91 – 911H → R in BAD18929 (PubMed:15577209).Curated
    Sequence conflicti91 – 911H → R in AAH13531 (PubMed:15489334).Curated
    Sequence conflicti91 – 911H → R in AAH91761 (PubMed:15489334).Curated
    Sequence conflicti100 – 1001E → V in BAD18929 (PubMed:15577209).Curated
    Sequence conflicti100 – 1001E → V in AAH13531 (PubMed:15489334).Curated
    Sequence conflicti100 – 1001E → V in AAH91761 (PubMed:15489334).Curated
    Sequence conflicti170 – 1701Y → S in BAD18929 (PubMed:15577209).Curated
    Sequence conflicti170 – 1701Y → S in AAH13531 (PubMed:15489334).Curated
    Sequence conflicti170 – 1701Y → S in AAH91761 (PubMed:15489334).Curated
    Sequence conflicti294 – 2941K → E in AAH61057 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB178898 mRNA. Translation: BAD18929.1.
    AY742217 mRNA. Translation: AAW65159.1.
    AK020439 mRNA. Translation: BAB32101.1.
    BC013531 mRNA. Translation: AAH13531.1.
    BC061057 mRNA. Translation: AAH61057.1.
    BC091761 mRNA. Translation: AAH91761.1.
    CCDSiCCDS26225.1.
    RefSeqiNP_084177.2. NM_029901.2.
    UniGeneiMm.27085.

    Genome annotation databases

    EnsembliENSMUST00000021628; ENSMUSP00000021628; ENSMUSG00000021207.
    GeneIDi77337.
    KEGGimmu:77337.
    UCSCiuc007pjr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB178898 mRNA. Translation: BAD18929.1.
    AY742217 mRNA. Translation: AAW65159.1.
    AK020439 mRNA. Translation: BAB32101.1.
    BC013531 mRNA. Translation: AAH13531.1.
    BC061057 mRNA. Translation: AAH61057.1.
    BC091761 mRNA. Translation: AAH91761.1.
    CCDSiCCDS26225.1.
    RefSeqiNP_084177.2. NM_029901.2.
    UniGeneiMm.27085.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HE5X-ray2.90A/B/C/D1-323[»]
    2HE8X-ray1.90A/B1-323[»]
    2HEJX-ray1.35A/B1-323[»]
    2IPFX-ray1.85A/B6-323[»]
    2IPGX-ray1.90A/B5-323[»]
    2P5NX-ray1.80A/B1-323[»]
    3CV6X-ray2.10A/B1-323[»]
    3FJNX-ray2.30A/B1-323[»]
    DisProtiDP00690.
    ProteinModelPortaliQ91WR5.
    SMRiQ91WR5. Positions 6-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000021628.

    Chemistry

    BindingDBiQ91WR5.
    ChEMBLiCHEMBL1075270.

    PTM databases

    PhosphoSiteiQ91WR5.

    Proteomic databases

    MaxQBiQ91WR5.
    PaxDbiQ91WR5.
    PRIDEiQ91WR5.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000021628; ENSMUSP00000021628; ENSMUSG00000021207.
    GeneIDi77337.
    KEGGimmu:77337.
    UCSCiuc007pjr.1. mouse.

    Organism-specific databases

    CTDi77337.
    MGIiMGI:1924587. Akr1c21.

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ91WR5.
    OMAiNTEDHVG.
    OrthoDBiEOG70KGQF.
    PhylomeDBiQ91WR5.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BRENDAi1.1.1.148. 3474.
    1.1.1.209. 3474.
    1.1.1.50. 3474.
    ReactomeiREACT_283453. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_292237. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    REACT_295031. Retinoid metabolism and transport.
    REACT_310468. RA biosynthesis pathway.
    REACT_325766. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_349058. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    SABIO-RKQ91WR5.

    Miscellaneous databases

    EvolutionaryTraceiQ91WR5.
    NextBioi346785.
    PROiQ91WR5.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ91WR5.
    CleanExiMM_AKR1C21.
    GenevisibleiQ91WR5. MM.

    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.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family."
      Ishikura S., Usami N., Nakajima S., Shiraishi H., El-Kabbani O., Hara A.
      Biol. Pharm. Bull. 27:1939-1945(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: ICR.
      Tissue: Kidney.
    2. "Characterization of 17alpha-hydroxysteroid dehydrogenase activity (17-alpha-HSD) and its involvement in the biosynthesis of epitestosterone."
      Bellemare V., Faucher F., Breton R., Luu-The V.
      BMC Biochem. 6:12-12(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    4. "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].
      Strain: FVB/N.
      Tissue: Kidney.
    5. "Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme."
      Faucher F., Pereira de Jesus-Tran K., Cantin L., Luu-The V., Labrie F., Breton R.
      J. Mol. Biol. 364:747-763(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, MUTAGENESIS OF ALA-24.
    6. "Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme."
      Dhagat U., Carbone V., Chung R.P.-T., Schulze-Briese C., Endo S., Hara A., El-Kabbani O.
      Acta Crystallogr. F 63:825-830(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADP.
    7. "Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding."
      Faucher F., Cantin L., Pereira de Jesus-Tran K., Lemieux M., Luu-The V., Labrie F., Breton R.
      J. Mol. Biol. 369:525-540(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 6-323 IN COMPLEX WITH EPITESTOSTERONE, MUTAGENESIS OF LYS-31, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION.
    8. "Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate."
      Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.
      Acta Crystallogr. D 65:257-265(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP.
    9. "Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme."
      Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.
      Acta Crystallogr. D 66:198-204(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ASP-224, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF GLN-222 AND TYR-224.

    Entry informationi

    Entry nameiAK1CL_MOUSE
    AccessioniPrimary (citable) accession number: Q91WR5
    Secondary accession number(s): Q6P8V0, Q9CX32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 18, 2008
    Last modified: June 24, 2015
    This is version 102 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.