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Q9JII6

- AK1A1_MOUSE

UniProt

Q9JII6 - AK1A1_MOUSE

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Protein

Alcohol dehydrogenase [NADP(+)]

Gene
Akr1a1, Akr1a4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Proton donor By similarity
Sitei80 – 801Lowers pKa of active site Tyr By similarity
Binding sitei113 – 1131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 2010NADP Reviewed prediction
Nucleotide bindingi211 – 27363NADP By 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
Complete GO annotation...

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
Complete GO annotation...

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.

Family & Domainsi

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541T → A in BAB27586. 1 Publication
Sequence conflicti60 – 601L → P in BAB27915. 1 Publication
Sequence conflicti95 – 951L → I in BAB27883. 1 Publication
Sequence conflicti95 – 951L → I in BAB27767. 1 Publication
Sequence conflicti120 – 1201R → L in BAB27909. 1 Publication
Sequence conflicti284 – 2841E → G in BAB27437. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 115 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

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