Q9JII6 (AK1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase [NADP(+)]
EC=1.1.1.2

Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member A1

Gene names

Name:	Akr1a1
Synonyms:	Akr1a4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	An alcohol + NADP+ = an aldehyde + NADPH.
Subunit structure	Monomer By similarity.
Tissue specificity	Widely expressed. Ref.1
Developmental stage	Detected at high levels in several tissues including neural ectoderm, gut endoderm, somites, branchial arches, otic vesicles, limb buds and tail bud.
Induction	Fear memory increases expression 7-fold. Ref.6
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	D-glucuronate catabolic process Inferred from direct assay PubMed 15769935. Source: MGI L-ascorbic acid biosynthetic process Inferred from direct assay PubMed 15769935. Source: MGI aldehyde catabolic process Inferred from direct assay PubMed 15769935. Source: MGI
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 15769935. Source: MGI cytosol Inferred from direct assay PubMed 15769935. Source: MGI
Molecular_function	L-glucuronate reductase activity Inferred from direct assay PubMed 15769935. Source: MGI alditol:NADP+ 1-oxidoreductase activity Inferred from direct assay PubMed 14667815PubMed 15769935. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 325

324

Alcohol dehydrogenase [NADP(+)]

PRO_0000124618

Regions

Nucleotide binding

11 – 20

10

NADP Potential

Nucleotide binding

211 – 273

63

NADP By similarity

Sites

Active site

50

1

Proton donor By similarity

Binding site

113

1

Substrate By similarity

Site

80

1

Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.4

Experimental info

Sequence conflict

54

1

T → A in BAB27586. Ref.2

Sequence conflict

60

1

L → P in BAB27915. Ref.2

Sequence conflict

95

1

L → I in BAB27883. Ref.2

Sequence conflict

95

1

L → I in BAB27767. Ref.2

Sequence conflict

120

1

R → L in BAB27909. Ref.2

Sequence conflict

284

1

E → G in BAB27437. Ref.2

Secondary structure

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325

Helix Strand Turn

Details...

Beta strand

5 – 7

3

Beta strand

13 – 17

5

Helix

26 – 38

13

Beta strand

43 – 45

3

Helix

48 – 50

3

Helix

53 – 63

11

Beta strand

68 – 70

3

Helix

72 – 74

3

Beta strand

76 – 81

6

Helix

83 – 85

3

Helix

88 – 102

15

Beta strand

107 – 113

7

Beta strand

115 – 118

4

Beta strand

120 – 122

3

Helix

140 – 152

13

Beta strand

155 – 157

3

Beta strand

159 – 163

5

Helix

166 – 175

10

Beta strand

182 – 186

5

Helix

194 – 202

9

Beta strand

206 – 211

6

Helix

216 – 221

6

Helix

228 – 230

3

Helix

232 – 241

10

Helix

245 – 255

11

Helix

267 – 273

7

Helix

283 – 290

8

Beta strand

302 – 305

4

Beta strand

308 – 313

6

Sequences

	Sequence		Length	Mass (Da)
	Q9JII6 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0097939061DA34CB	FASTA	325	36,587
	10 20 30 40 50 60 MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKHALSAG YRHIDCASVY GNETEIGEAL 70 80 90 100 110 120 KESVGSGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER 130 140 150 160 170 180 GDNPFPKNAD GTVRYDSTHY KETWKALEVL VAKGLVKALG LSNFNSRQID DVLSVASVRP 190 200 210 220 230 240 AVLQVECHPY LAQNELIAHC HARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK 250 260 270 280 290 300 HGRSPAQILL RWQVQRKVIC IPKSINPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV 310 320 PMITVDGKRV PRDAGHPLYP FNDPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and developmental expression of mouse aldehyde reductase (AKR1A4)." Allan D., Lohnes D. Mech. Dev. 94:271-275(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Embryo.
[2]	"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: Cerebellum, Embryo and Tongue.
[3]	"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: Mammary gland.
[4]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13 AND 244-251, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[5]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 204-218; 222-240 AND 313-325, MASS SPECTROMETRY. Tissue: Hippocampus.
[6]	"Identification of genes expressed in the amygdala during the formation of fear memory." Stork O., Stork S., Pape H.-C., Obata K. Learn. Memory 8:209-219(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF225564 mRNA. Translation: AAF67111.1.
AK011906 mRNA. Translation: BAB27907.1.
AK009462 mRNA. Translation: BAB26303.1.
AK011321 mRNA. Translation: BAB27543.1.
AK011794 mRNA. Translation: BAB27846.1.
AK011908 mRNA. Translation: BAB27909.1.
AK011918 mRNA. Translation: BAB27915.1.
AK011856 mRNA. Translation: BAB27883.1.
AK011667 mRNA. Translation: BAB27767.1.
AK011388 mRNA. Translation: BAB27586.1.
AK011157 mRNA. Translation: BAB27437.1.
AK011209 mRNA. Translation: BAB27469.1.
AK005162 mRNA. Translation: BAB23853.1.
AK011221 mRNA. No translation available.
BC039926 mRNA. Translation: AAH39926.1.

IPI

IPI00466128.

RefSeq

NP_067448.1. NM_021473.3.

UniGene

Mm.30085.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GAC	X-ray	1.64	A/B	2-325	[»]

ProteinModelPortal

Q9JII6.

SMR

Q9JII6. Positions 2-325.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000030455.

PTM databases

PhosphoSite

Q9JII6.

2D gel databases

REPRODUCTION-2DPAGE

IPI00466128.
Q9JII6.

Proteomic databases

PaxDb

Q9JII6.

PRIDE

Q9JII6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030455; ENSMUSP00000030455; ENSMUSG00000028692.

GeneID

58810.

KEGG

mmu:58810.

Organism-specific databases

CTD

10327.

MGI

MGI:1929955. Akr1a1.

Phylogenomic databases

eggNOG

COG0656.

GeneTree

ENSGT00550000074107.

HOVERGEN

HBG000020.

InParanoid

Q9JII6.

KO

K00002.

OMA

ICYDSTH.

OrthoDB

EOG4J118N.

Enzyme and pathway databases

BRENDA

1.1.1.2. 3474.

SABIO-RK

Q9JII6.

Gene expression databases

ArrayExpress

Q9JII6.

Bgee

Q9JII6.

Genevestigator

Q9JII6.

GermOnline

ENSMUSG00000028692. Mus musculus.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

314404.

SOURCE

Search...

Entry information

Entry name

AK1A1_MOUSE

Accession

Primary (citable) accession number: Q9JII6
Secondary accession number(s): Q9CQI5 , Q9CQT8, Q9CT53, Q9D012, Q9D016, Q9D0I7, Q9D0P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program