Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9JII6

- AK1A1_MOUSE

UniProt

Q9JII6 - AK1A1_MOUSE

Protein

Alcohol dehydrogenase [NADP(+)]

Gene

Akr1a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity

    Catalytic activityi

    An alcohol + NADP+ = an aldehyde + NADPH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501Proton donorBy similarity
    Sitei80 – 801Lowers pKa of active site TyrBy similarity
    Binding sitei113 – 1131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 2010NADPSequence Analysis
    Nucleotide bindingi211 – 27363NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. alcohol dehydrogenase (NADP+) activity Source: UniProtKB
    2. alditol:NADP+ 1-oxidoreductase activity Source: MGI
    3. L-glucuronate reductase activity Source: MGI

    GO - Biological processi

    1. aldehyde catabolic process Source: MGI
    2. D-glucuronate catabolic process Source: MGI
    3. L-ascorbic acid biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.2. 3474.
    SABIO-RKQ9JII6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
    Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member A1
    Gene namesi
    Name:Akr1a1
    Synonyms:Akr1a4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1929955. Akr1a1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: MGI
    2. cytosol Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 325324Alcohol dehydrogenase [NADP(+)]PRO_0000124618Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication
    Modified residuei127 – 1271N6-acetyllysine; alternate1 Publication
    Modified residuei127 – 1271N6-succinyllysine; alternate1 Publication
    Modified residuei145 – 1451N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9JII6.
    PaxDbiQ9JII6.
    PRIDEiQ9JII6.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00466128.
    Q9JII6.

    PTM databases

    PhosphoSiteiQ9JII6.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Developmental stagei

    Detected at high levels in several tissues including neural ectoderm, gut endoderm, somites, branchial arches, otic vesicles, limb buds and tail bud.

    Inductioni

    Fear memory increases expression 7-fold.1 Publication

    Gene expression databases

    ArrayExpressiQ9JII6.
    BgeeiQ9JII6.
    GenevestigatoriQ9JII6.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    IntActiQ9JII6. 4 interactions.
    MINTiMINT-1869516.
    STRINGi10090.ENSMUSP00000030455.

    Structurei

    Secondary structure

    1
    325
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73
    Beta strandi13 – 175
    Helixi26 – 3813
    Beta strandi43 – 453
    Helixi48 – 503
    Helixi53 – 6311
    Beta strandi68 – 703
    Helixi72 – 743
    Beta strandi76 – 816
    Helixi83 – 853
    Helixi88 – 10215
    Beta strandi107 – 1137
    Beta strandi115 – 1184
    Beta strandi120 – 1223
    Helixi140 – 15213
    Beta strandi155 – 1573
    Beta strandi159 – 1635
    Helixi166 – 17510
    Beta strandi182 – 1865
    Helixi194 – 2029
    Beta strandi206 – 2116
    Helixi216 – 2216
    Helixi228 – 2303
    Helixi232 – 24110
    Helixi245 – 25511
    Helixi267 – 2737
    Helixi283 – 2908
    Beta strandi302 – 3054
    Beta strandi308 – 3136

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GACX-ray1.64A/B2-325[»]
    ProteinModelPortaliQ9JII6.
    SMRiQ9JII6. Positions 2-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00750000117547.
    HOVERGENiHBG000020.
    InParanoidiQ9JII6.
    KOiK00002.
    OMAiWPYAFER.
    OrthoDBiEOG70KGQF.
    PhylomeDBiQ9JII6.
    TreeFamiTF106492.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9JII6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKHALSAG YRHIDCASVY    50
    GNETEIGEAL KESVGSGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA 100
    DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVRYDSTHY KETWKALEVL 150
    VAKGLVKALG LSNFNSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC 200
    HARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL 250
    RWQVQRKVIC IPKSINPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV 300
    PMITVDGKRV PRDAGHPLYP FNDPY 325
    Length:325
    Mass (Da):36,587
    Last modified:January 23, 2007 - v3
    Checksum:i0097939061DA34CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541T → A in BAB27586. (PubMed:16141072)Curated
    Sequence conflicti60 – 601L → P in BAB27915. (PubMed:16141072)Curated
    Sequence conflicti95 – 951L → I in BAB27883. (PubMed:16141072)Curated
    Sequence conflicti95 – 951L → I in BAB27767. (PubMed:16141072)Curated
    Sequence conflicti120 – 1201R → L in BAB27909. (PubMed:16141072)Curated
    Sequence conflicti284 – 2841E → G in BAB27437. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS18514.1.
    RefSeqiNP_067448.1. NM_021473.3.
    UniGeneiMm.30085.
    Mm.489607.

    Genome annotation databases

    EnsembliENSMUST00000030455; ENSMUSP00000030455; ENSMUSG00000028692.
    GeneIDi58810.
    KEGGimmu:58810.
    UCSCiuc008uha.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS18514.1.
    RefSeqi NP_067448.1. NM_021473.3.
    UniGenei Mm.30085.
    Mm.489607.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GAC X-ray 1.64 A/B 2-325 [» ]
    ProteinModelPortali Q9JII6.
    SMRi Q9JII6. Positions 2-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JII6. 4 interactions.
    MINTi MINT-1869516.
    STRINGi 10090.ENSMUSP00000030455.

    PTM databases

    PhosphoSitei Q9JII6.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00466128.
    Q9JII6.

    Proteomic databases

    MaxQBi Q9JII6.
    PaxDbi Q9JII6.
    PRIDEi Q9JII6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030455 ; ENSMUSP00000030455 ; ENSMUSG00000028692 .
    GeneIDi 58810.
    KEGGi mmu:58810.
    UCSCi uc008uha.2. mouse.

    Organism-specific databases

    CTDi 10327.
    MGIi MGI:1929955. Akr1a1.

    Phylogenomic databases

    eggNOGi COG0656.
    GeneTreei ENSGT00750000117547.
    HOVERGENi HBG000020.
    InParanoidi Q9JII6.
    KOi K00002.
    OMAi WPYAFER.
    OrthoDBi EOG70KGQF.
    PhylomeDBi Q9JII6.
    TreeFami TF106492.

    Enzyme and pathway databases

    BRENDAi 1.1.1.2. 3474.
    SABIO-RK Q9JII6.

    Miscellaneous databases

    NextBioi 314404.
    PROi Q9JII6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JII6.
    Bgeei Q9JII6.
    Genevestigatori Q9JII6.

    Family and domain databases

    Gene3Di 3.20.20.100. 1 hit.
    InterProi IPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view ]
    PANTHERi PTHR11732. PTHR11732. 1 hit.
    Pfami PF00248. Aldo_ket_red. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000097. AKR. 1 hit.
    PRINTSi PR00069. ALDKETRDTASE.
    SUPFAMi SSF51430. SSF51430. 1 hit.
    PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, 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.

    Entry informationi

    Entry nameiAK1A1_MOUSE
    AccessioniPrimary (citable) accession number: Q9JII6
    Secondary accession number(s): Q9CQI5
    , Q9CQT8, Q9CT53, Q9D012, Q9D016, Q9D0I7, Q9D0P3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3