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UniProtKB/Swiss-Prot entry Q9JII6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1A1_MOUSE
Primary accession number Q9JII6
Secondary accession numbers Q9CQI5 Q9CQT8 Q9CT53 Q9D012 Q9D016 Q9D0I7 Q9D0P3
Integrated into Swiss-Prot on August 30, 2002
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 63)
Name and origin of the protein
Protein name Alcohol dehydrogenase [NADP+]
Synonyms EC 1.1.1.2
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene name
Name: Akr1a1
Synonyms: Akr1a4
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Embryo;
DOI=10.1016/S0925-4773(00)00293-8; PubMed=10842086 [NCBI, ExPASy, EBI, Israel, Japan]
Allan D., Lohnes D.;
"Cloning and developmental expression of mouse aldehyde reductase (AKR1A4).";
Mech. Dev. 94:271-275(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Embryo, and Tongue;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Mammary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-13 AND 244-251, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Liver;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 204-218; 222-240 AND 313-325, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[6]
INDUCTION.
DOI=10.1101/lm.39401; PubMed=11533224 [NCBI, ExPASy, EBI, Israel, Japan]
Stork O., Stork S., Pape H.-C., Obata K.;
"Identification of genes expressed in the amygdala during the formation of fear memory.";
Learn. Memory 8:209-219(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF225564; AAF67111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011906; BAB27907.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK009462; BAB26303.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011321; BAB27543.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011794; BAB27846.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011908; BAB27909.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011918; BAB27915.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011856; BAB27883.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011667; BAB27767.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011388; BAB27586.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011157; BAB27437.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011209; BAB27469.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005162; BAB23853.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK011221; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
BC039926; AAH39926.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_067448.1; -.
UniGene Mm.30085
3D structure databases
HSSP P14550; 2ALR. [HSSP ENTRY / PDB]
SMR Q9JII6; 3-325.
ModBase Q9JII6.
PTM databases
PhosphoSite Q9JII6; -.
2D gel databases
REPRODUCTION-2DPAGE Q9JII6; -.
Organism-specific databases
MGI MGI:1929955; Akr1a4.
Gene expression databases
ArrayExpress Q9JII6; -.
GermOnline ENSMUSG00000028692; Mus musculus.
Ontologies
GO
GO:0016324; Cellular component: apical plasma membrane (inferred from direct assay from MGI).
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0008106; Molecular function: alcohol dehydrogenase (NADP+) activity (non-traceable author statement from UniProtKB).
GO:0004032; Molecular function: aldehyde reductase activity (inferred from direct assay from MGI).
GO:0047939; Molecular function: L-glucuronate reductase activity (inferred from direct assay from MGI).
GO:0046185; Biological process: aldehyde catabolic process (inferred from direct assay from MGI).
GO:0042840; Biological process: D-glucuronate catabolic process (inferred from direct assay from MGI).
GO:0019853; Biological process: L-ascorbic acid biosynthetic process (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
BLOCKS Q9JII6.
Genome annotation databases
Ensembl ENSMUSG00000028692; Mus musculus. [Contig view]
GeneID 58810; -.
KEGG mmu:58810; -.
Phylogenomic databases
HOVERGEN Q9JII6; -.
Other
SOURCE Akr1a1; Mus musculus.
ProtoNet Q9JII6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   325  324     Alcohol dehydrogenase [NADP+]. PRO_0000124618
NP_BIND   11    20  10     NADP (Potential). 
NP_BIND   211   273  63     NADP (By similarity). 
ACT_SITE   50    50        Proton donor (By similarity). 
BINDING   113   113        Substrate (By similarity). 
SITE   80    80  1     Lowers pKa of active site Tyr (By similarity). 
MOD_RES   2     2        N-acetylthreonine. 
CONFLICT   54    54        T -> A (in Ref. 2; BAB27586). 
CONFLICT   60    60        L -> P (in Ref. 2; BAB27915). 
CONFLICT   95    95        L -> I (in Ref. 2; BAB27883/BAB27767). 
CONFLICT   120   120        R -> L (in Ref. 2; BAB27909). 
CONFLICT   284   284        E -> G (in Ref. 2; BAB27437). 
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 36587 Da [This is the MW of the unprocessed precursor] CRC64: 0097939061DA34CB [This is a checksum on the sequence]
        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 

Q9JII6 in FASTA format

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