Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9JII6 (AK1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 325324Alcohol dehydrogenase [NADP(+)]
PRO_0000124618

Regions

Nucleotide binding11 – 2010NADP Potential
Nucleotide binding211 – 27363NADP By similarity

Sites

Active site501Proton donor By similarity
Binding site1131Substrate By similarity
Site801Lowers pKa of active site Tyr By similarity

Amino acid modifications

Modified residue21N-acetylthreonine Ref.4
Modified residue1271N6-acetyllysine; alternate Ref.7
Modified residue1271N6-succinyllysine; alternate Ref.7
Modified residue1451N6-succinyllysine Ref.7

Experimental info

Sequence conflict541T → A in BAB27586. Ref.2
Sequence conflict601L → P in BAB27915. Ref.2
Sequence conflict951L → I in BAB27883. Ref.2
Sequence conflict951L → I in BAB27767. Ref.2
Sequence conflict1201R → L in BAB27909. Ref.2
Sequence conflict2841E → G in BAB27437. Ref.2

Secondary structure

........................................................... 325
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9JII6 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0097939061DA34CB

FASTA32536,587
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+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.
RefSeqNP_067448.1. NM_021473.3.
UniGeneMm.30085.
Mm.489607.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GACX-ray1.64A/B2-325[»]
ProteinModelPortalQ9JII6.
SMRQ9JII6. Positions 2-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JII6. 4 interactions.
MINTMINT-1869516.
STRING10090.ENSMUSP00000030455.

PTM databases

PhosphoSiteQ9JII6.

2D gel databases

REPRODUCTION-2DPAGEIPI00466128.
Q9JII6.

Proteomic databases

PaxDbQ9JII6.
PRIDEQ9JII6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030455; ENSMUSP00000030455; ENSMUSG00000028692.
GeneID58810.
KEGGmmu:58810.
UCSCuc008uha.2. mouse.

Organism-specific databases

CTD10327.
MGIMGI:1929955. Akr1a1.

Phylogenomic databases

eggNOGCOG0656.
GeneTreeENSGT00750000117547.
HOVERGENHBG000020.
InParanoidQ9JII6.
KOK00002.
OMAWPYAFER.
OrthoDBEOG70KGQF.
PhylomeDBQ9JII6.
TreeFamTF106492.

Enzyme and pathway databases

BRENDA1.1.1.2. 3474.
SABIO-RKQ9JII6.

Gene expression databases

ArrayExpressQ9JII6.
BgeeQ9JII6.
GenevestigatorQ9JII6.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314404.
PROQ9JII6.
SOURCESearch...

Entry information

Entry nameAK1A1_MOUSE
AccessionPrimary (citable) accession number: Q9JII6
Secondary accession number(s): Q9CQI5 expand/collapse secondary AC list , Q9CQT8, Q9CT53, Q9D012, Q9D016, Q9D0I7, Q9D0P3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot