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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

  1. alditol:NADP+ 1-oxidoreductase activity Source: MGI
  2. aldo-keto reductase (NADP) activity Source: MGI
  3. androsterone dehydrogenase (B-specific) activity Source: MGI
  4. androsterone dehydrogenase activity Source: UniProtKB
  5. bile acid binding Source: MGI
  6. carboxylic acid binding Source: MGI
  7. ketosteroid monooxygenase activity Source: MGI
  8. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: MGI
  9. phenanthrene 9,10-monooxygenase activity Source: MGI
  10. steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: MGI
  11. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: MGI

GO - Biological processi

  1. steroid biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_198569. Retinoid metabolism and transport.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
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. cytosol Source: MGI
  2. extracellular vesicular exosome Source: MGI
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.
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 – 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

ReactomeiREACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_198569. Retinoid metabolism and transport.
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
SABIO-RKQ91WR5.

Miscellaneous databases

EvolutionaryTraceiQ91WR5.
NextBioi346785.
PROiQ91WR5.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WR5.
CleanExiMM_AKR1C21.
GenevestigatoriQ91WR5.

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: March 4, 2015
This is version 99 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.