Reviewed, UniProtKB/Swiss-Prot Q9JII6 (AK1A1_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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 aldehydes to their corresponding alcohols 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	Direct protein sequencing
Gene Ontology (GO)
Biological process	D-glucuronate catabolic process Inferred from direct assay. Source: MGI L-ascorbic acid biosynthetic process Inferred from direct assay. Source: MGI aldehyde catabolic process Inferred from direct assay. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apical plasma membrane Inferred from direct assay. Source: MGI cytosol Inferred from direct assay. Source: MGI
Molecular function	L-glucuronate reductase activity Inferred from direct assay. Source: MGI alcohol dehydrogenase (NADP+) activity Ref.1 Non-traceable author statement. Source: UniProtKB aldehyde reductase activity Ref.1 Inferred from direct assay. 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

Sequences

	Sequence		Length	Mass (Da)
	Q9JII6-1 [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: 10842086] [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: 16141072] [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: 15489334] [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: 11533224] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Mm.30085
3D structure databases
HSSP	HSSP built from PDB template 2ALR based on UniProtKB P14550.
SMR	Q9JII6. Positions 3-325.
ModBase	Search...
PTM databases
PhosphoSite	Q9JII6.
2-D gel databases
REPRODUCTION-2DPAGE	Q9JII6.
Proteomic databases
PRIDE	Q9JII6.
Genome annotation databases
Ensembl	ENSMUSG00000028692. Mus musculus. [Contig view]
GeneID	58810.
KEGG	mmu:58810.
Organism-specific databases
MGI	MGI:1929955. Akr1a4.
Phylogenomic databases
HOVERGEN	Q9JII6.
OMA	Q9JII6. WRHPDEP.
Gene expression databases
ArrayExpress	Q9JII6.
Bgee	Q9JII6.
GermOnline	ENSMUSG00000028692. Mus musculus.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit. PS00063. ALDOKETO_REDUCTASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)