CPLM-021756

Genbank Nucleotide ID

Alcohol dehydrogenase [NADP(+)]

Protein Synonyms/Alias

Aldehyde reductase; Aldo-keto reductase family 1 member A1

Mus musculus (Mouse)

Position	Peptide	Type	References
127	RGDNPFPKNADGTVR	acetylation	[1]
141	RYDSTHYKETWKALE	acetylation	[1]
240	VVLALAEKHGRSPAQ	ubiquitination	[2]
257	LRWQVQRKVICIPKS	acetylation	[3]
263	RKVICIPKSINPSRI	acetylation	[1, 3, 4, 5, 6]
263	RKVICIPKSINPSRI	ubiquitination	[2]
294	KQLDALNKNWRYIVP	ubiquitination	[2]
308	PMITVDGKRVPRDAG	ubiquitination	[2]

[1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]

Functional Description

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).

NP_BIND 11 20 NADP (Potential).
NP_BIND 211 273 NADP (By similarity).
ACT_SITE 50 50 Proton donor (By similarity).
BINDING 113 113 Substrate (By similarity).
MOD_RES 2 2 N-acetylthreonine.

3D-structure; Acetylation; Complete proteome; Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0016324; C:apical plasma membrane; IDA:MGI.
GO:0005829; C:cytosol; IDA:MGI.
GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:MGI.
GO:0047939; F:L-glucuronate reductase activity; IDA:MGI.
GO:0046185; P:aldehyde catabolic process; IDA:MGI.
GO:0042840; P:D-glucuronate catabolic process; IDA:MGI.
GO:0019853; P:L-ascorbic acid biosynthetic process; IDA:MGI.

IPR001395; Aldo/ket_red.
IPR018170; Aldo/ket_reductase_CS.
IPR020471; Aldo/keto_reductase_subgr.
IPR023210; NADP_OxRdtase_dom.

PF00248; Aldo_ket_red

PS00798; ALDOKETO_REDUCTASE_1
PS00062; ALDOKETO_REDUCTASE_2
PS00063; ALDOKETO_REDUCTASE_3

PR00069; ALDKETRDTASE.