Sequence of AK1C2_HUMAN
EC Number:1.1.1.357
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+
General information:
Sequence
0 MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID SAHVYNNEEQ
60 VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV
120 SVKPGEEVIP KDENGKILFD TVDLCATWEA MEKCKDAGLA KSIGVSNFNH RLLEMILNKP
180 GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV
240 LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
300 RNVRYLTLDI FAGPPNYPFS DEY
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
581948
Qin K.-N.,New M.I.,Cheng K.-C.
Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase.
J. Steroid Biochem. Mol. Biol.
46
673-679
1993
581949
Ciaccio P.J.,Tew K.D.
cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase.
Biochim. Biophys. Acta
1186
129-132
1994
581950
Qin K.-N.,Khanna M.,Cheng K.-C.
Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein.
Gene
149
357-361
1994
581951
Dufort I.,Soucy P.,Labrie F.,Luu-The V.
Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids.
Biochem. Biophys. Res. Commun.
228
474-479
1996
581952
Shiraishi H.,Ishikura S.,Matsuura K.,Deyashiki Y.,Ninomiya M.,Sakai S.,Hara A.
Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA.
Biochem. J.
334
399-405
1998
581953
Nishizawa M.,Nakajima T.,Yasuda K.,Kanzaki H.,Sasaguri Y.,Watanabe K.,Ito S.
Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes.
Genes Cells
5
111-125
2000
581954
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.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
581956
Deloukas P.,Earthrowl M.E.,Grafham D.V.,Rubenfield M.,French L.,Steward C.A.,Sims S.K.,Jones M.C.,Searle S.,Scott C.,Howe K.,Hunt S.E.,Andrews T.D.,Gilbert J.G.R.,Swarbreck D.,Ashurst J.L.,Taylor A.,Battles J.,Bird C.P.,Ainscough R.,Almeida J.P.,Ashwell R.I.S.,Ambrose K.D.,Babbage A.K.,Bagguley C.L.,Bailey J.,Banerjee R.,Bates K.,Beasley H.,Bray-Allen S.,Brown A.J.,Brown J.Y.,Burford D.C.,Burrill W.,Burton J.,Cahill P.,Camire D.,Carter N.P.,Chapman J.C.,Clark S.Y.,Clarke G.,Clee C.M.,Clegg S.,Corby N.,Coulson A.,Dhami P.,Dutta I.,Dunn M.,Faulkner L.,Frankish A.,Frankland J.A.,Garner P.,Garnett J.,Gribble S.,Griffiths C.,Grocock R.,Gustafson E.,Hammond S.,Harley J.L.,Hart E.,Heath P.D.,Ho T.P.,Hopkins B.,Horne J.,Howden P.J.,Huckle E.,Hynds C.,Johnson C.,Johnson D.,Kana A.,Kay M.,Kimberley A.M.,Kershaw J.K.,Kokkinaki M.,Laird G.K.,Lawlor S.,Lee H.M.,Leongamornlert D.A.,Laird G.,Lloyd C.,Lloyd D.M.,Loveland J.,Lovell J.,McLaren S.,McLay K.E.,McMurray A.,Mashreghi-Mohammadi M.,Matthews L.,Milne S.,Nickerson T.,Nguyen M.,Overton-Larty E.,Palmer S.A.,Pearce A.V.,Peck A.I.,Pelan S.,Phillimore B.,Porter K.,Rice C.M.,Rogosin A.,Ross M.T.,Sarafidou T.,Sehra H.K.,Shownkeen R.,Skuce C.D.,Smith M.,Standring L.,Sycamore N.,Tester J.,Thorpe A.,Torcasso W.,Tracey A.,Tromans A.,Tsolas J.,Wall M.,Walsh J.,Wang H.,Weinstock K.,West A.P.,Willey D.L.,Whitehead S.L.,Wilming L.,Wray P.W.,Young L.,Chen Y.,Lovering R.C.,Moschonas N.K.,Siebert R.,Fechtel K.,Bentley D.,Durbin R.M.,Hubbard T.,Doucette-Stamm L.,Beck S.,Smith D.R.,Rogers J.
The DNA sequence and comparative analysis of human chromosome 10.
Nature
429
375-381
2004
581957
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
581958
Hara A.,Matsuura K.,Tamada Y.,Sato K.,Miyabe Y.,Deyashiki Y.,Ishida N.
Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells.
Biochem. J.
313
373-376
1996
581959
Stolz A.,Hammond L.,Lou H.,Takikawa H.,Ronk M.,Shively J.E.
cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family.
J. Biol. Chem.
268
10448-10457
1993
581960
Penning T.M.,Burczynski M.E.,Jez J.M.,Hung C.F.,Lin H.K.,Ma H.,Moore M.,Palackal N.,Ratnam K.
Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones.
Biochem. J.
351
67-77
2000
581961
Steckelbroeck S.,Jin Y.,Gopishetty S.,Oyesanmi B.,Penning T.M.
Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action.
J. Biol. Chem.
279
10784-10795
2004
581962
Jin Y.,Duan L.,Lee S.H.,Kloosterboer H.J.,Blair I.A.,Penning T.M.
Human cytosolic hydroxysteroid dehydrogenases of the aldo-ketoreductase superfamily catalyze reduction of conjugated steroids: implications for phase I and phase II steroid hormone metabolism.
J. Biol. Chem.
284
10013-10022
2009
581963
Fluck C.E.,Meyer-Boni M.,Pandey A.V.,Kempna P.,Miller W.L.,Schoenle E.J.,Biason-Lauber A.
Why boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiation.
Am. J. Hum. Genet.
89
201-218
2011
581964
Jin Y.,Stayrook S.E.,Albert R.H.,Palackal N.T.,Penning T.M.,Lewis M.
Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate.
Biochemistry
40
10161-10168
2001
581965
Nahoum V.,Gangloff A.,Legrand P.,Zhu D.-W.,Cantin L.,Zhorov B.S.,Luu-The V.,Labrie F.,Breton R.,Lin S.X.
Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution.
J. Biol. Chem.
276
42091-42098
2001
581966
Couture J.F.,de Jesus-Tran K.P.,Roy A.M.,Cantin L.,Cote P.L.,Legrand P.,Luu-The V.,Labrie F.,Breton R.
Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an 'induced-fit' mechanism and a conserved basic motif involved in the binding of androgen.
Protein Sci.
14
1485-1497
2005
581967
Faucher F.,Pereira de Jesus-Tran K.,Cantin L.,Luu-The V.,Labrie F.,Breton R.
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.
J. Mol. Biol.
364
747-763
2006
581968
Faucher F.,Cantin L.,Pereira de Jesus-Tran K.,Lemieux M.,Luu-The V.,Labrie F.,Breton R.
Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding.
J. Mol. Biol.
369
525-540
2007
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