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Q9JII6

- AK1A1_MOUSE

UniProt

Q9JII6 - AK1A1_MOUSE

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Protein

Alcohol dehydrogenase [NADP(+)]

Gene

Akr1a1

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).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
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
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
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

BgeeiQ9JII6.
ExpressionAtlasiQ9JII6. baseline and differential.
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 – 73Combined sources
Beta strandi13 – 175Combined sources
Helixi26 – 3813Combined sources
Beta strandi43 – 453Combined sources
Helixi48 – 503Combined sources
Helixi53 – 6311Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Helixi83 – 853Combined sources
Helixi88 – 10215Combined sources
Beta strandi107 – 1137Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi120 – 1223Combined sources
Helixi140 – 15213Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi159 – 1635Combined sources
Helixi166 – 17510Combined sources
Beta strandi182 – 1865Combined sources
Helixi194 – 2029Combined sources
Beta strandi206 – 2116Combined sources
Helixi216 – 2216Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25511Combined sources
Helixi267 – 2737Combined sources
Helixi283 – 2908Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi308 – 3136Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GACX-ray1.64A/B2-325[»]
ProteinModelPortaliQ9JII6.
SMRiQ9JII6. Positions 1-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
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

        10         20         30         40         50
MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKHALSAG YRHIDCASVY
60 70 80 90 100
GNETEIGEAL KESVGSGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA
110 120 130 140 150
DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVRYDSTHY KETWKALEVL
160 170 180 190 200
VAKGLVKALG LSNFNSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC
210 220 230 240 250
HARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL
260 270 280 290 300
RWQVQRKVIC IPKSINPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV
310 320
PMITVDGKRV PRDAGHPLYP FNDPY
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GAC X-ray 1.64 A/B 2-325 [» ]
ProteinModelPortali Q9JII6.
SMRi Q9JII6. Positions 1-325.
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 ENSGT00760000119041.
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

Bgeei Q9JII6.
ExpressionAtlasi Q9JII6. baseline and differential.
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: November 26, 2014
This is version 118 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