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Q91WR5

- AK1CL_MOUSE

UniProt

Q91WR5 - AK1CL_MOUSE

Protein

Aldo-keto reductase family 1 member C21

Gene

Akr1c21

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (18 Mar 2008)
      Previous versions | rss
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    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

    1. aldo-keto reductase (NADP) activity Source: MGI
    2. androsterone dehydrogenase activity Source: UniProtKB
    3. steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: MGI

    GO - Biological processi

    1. steroid biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    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: Chromosome 13

    Organism-specific databases

    MGIiMGI:1924587. Akr1c21.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.
    GenevestigatoriQ91WR5.

    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 – 93
    Beta strandi15 – 228
    Beta strandi27 – 293
    Helixi33 – 4412
    Beta strandi48 – 503
    Helixi53 – 553
    Helixi58 – 7013
    Helixi76 – 783
    Beta strandi80 – 856
    Helixi87 – 893
    Turni92 – 943
    Helixi95 – 10612
    Beta strandi111 – 1177
    Beta strandi121 – 1233
    Beta strandi125 – 1295
    Helixi144 – 15613
    Beta strandi159 – 1679
    Helixi170 – 1778
    Beta strandi187 – 1926
    Beta strandi194 – 1974
    Helixi200 – 2089
    Beta strandi212 – 2165
    Turni225 – 2273
    Helixi228 – 2314
    Helixi235 – 2373
    Helixi239 – 24810
    Helixi252 – 26110
    Turni262 – 2643
    Beta strandi266 – 2694
    Helixi274 – 2807
    Helixi281 – 2855
    Helixi290 – 2978
    Helixi309 – 3113
    Beta strandi318 – 3214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00750000117516.
    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

    MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD    50
    SASVYNTEDH VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE 100
    RSLQKLQFDY VDLYLIHYPM ALKPGEENFP VDEHGKLIFD RVDLCATWEA 150
    MEKCKDAGLT KSIGVSNFNY RQLEMILNKP GLKYKPVCNQ VECHPYLNQM 200
    KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV LGSMAKKYNR 250
    TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN 300
    RNMRYIPAAI FKGHPNWPFL DEY 323
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS26225.1.
    RefSeqi NP_084177.2. NM_029901.2.
    UniGenei Mm.27085.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HE5 X-ray 2.90 A/B/C/D 1-323 [» ]
    2HE8 X-ray 1.90 A/B 1-323 [» ]
    2HEJ X-ray 1.35 A/B 1-323 [» ]
    2IPF X-ray 1.85 A/B 6-323 [» ]
    2IPG X-ray 1.90 A/B 5-323 [» ]
    2P5N X-ray 1.80 A/B 1-323 [» ]
    3CV6 X-ray 2.10 A/B 1-323 [» ]
    3FJN X-ray 2.30 A/B 1-323 [» ]
    DisProti DP00690.
    ProteinModelPortali Q91WR5.
    SMRi Q91WR5. Positions 6-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000021628.

    Chemistry

    ChEMBLi CHEMBL1075270.

    PTM databases

    PhosphoSitei Q91WR5.

    Proteomic databases

    MaxQBi Q91WR5.
    PaxDbi Q91WR5.
    PRIDEi Q91WR5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021628 ; ENSMUSP00000021628 ; ENSMUSG00000021207 .
    GeneIDi 77337.
    KEGGi mmu:77337.
    UCSCi uc007pjr.1. mouse.

    Organism-specific databases

    CTDi 77337.
    MGIi MGI:1924587. Akr1c21.

    Phylogenomic databases

    eggNOGi COG0656.
    GeneTreei ENSGT00750000117516.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi Q91WR5.
    OMAi NTEDHVG.
    OrthoDBi EOG70KGQF.
    PhylomeDBi Q91WR5.
    TreeFami TF106492.

    Enzyme and pathway databases

    SABIO-RK Q91WR5.

    Miscellaneous databases

    EvolutionaryTracei Q91WR5.
    NextBioi 346785.
    PROi Q91WR5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91WR5.
    CleanExi MM_AKR1C21.
    Genevestigatori Q91WR5.

    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 PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 94 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