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Q8CG76

- ARK72_MOUSE

UniProt

Q8CG76 - ARK72_MOUSE

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Protein
Aflatoxin B1 aldehyde reductase member 2
Gene
Akr7a2, Afar, Akr7a5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen By similarity.1 Publication

Catalytic activityi

4-hydroxybutanoate + NADP+ = succinate semialdehyde + NADPH.1 Publication

Enzyme regulationi

Inhibited by citrate, succinate and tartrate.1 Publication

Kineticsi

  1. KM=19.8 µM for succinic semialdehyde1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801NADP
Active sitei85 – 851Proton donor
Sitei113 – 1131Lowers pKa of active site Tyr By similarityBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei205 – 2051NADP
Binding sitei258 – 2581NADP
Binding sitei268 – 2681Substrate
Binding sitei271 – 2711Substrate
Binding sitei367 – 3671Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1802NADP
Nucleotide bindingi234 – 24411NADPBy similarity
Add
BLAST
Nucleotide bindingi326 – 3349NADP

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

SABIO-RKQ8CG76.

Names & Taxonomyi

Protein namesi
Recommended name:
Aflatoxin B1 aldehyde reductase member 2 (EC:1.1.1.n11)
Alternative name(s):
Succinic semialdehyde reductase
Short name:
SSA reductase
Gene namesi
Name:Akr7a2
Synonyms:Afar, Akr7a5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:107796. Akr7a5.

Subcellular locationi

Golgi apparatus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Aflatoxin B1 aldehyde reductase member 2
PRO_0000070376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361N6-acetyllysine1 Publication
Modified residuei244 – 2441N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8CG76.
PaxDbiQ8CG76.
PRIDEiQ8CG76.

2D gel databases

REPRODUCTION-2DPAGEQ8CG76.

PTM databases

PhosphoSiteiQ8CG76.

Expressioni

Tissue specificityi

Expressed in liver, kidney, testis and brain with low levels in skeletal muscle, spleen, heart and lung.1 Publication

Gene expression databases

BgeeiQ8CG76.
GenevestigatoriQ8CG76.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ8CG76. 3 interactions.
MINTiMINT-1869477.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 515
Turni56 – 583
Helixi61 – 7313
Beta strandi78 – 803
Helixi85 – 884
Helixi89 – 957
Beta strandi109 – 1146
Turni117 – 1204
Helixi124 – 13714
Beta strandi143 – 1486
Helixi157 – 16913
Beta strandi172 – 1809
Helixi183 – 19614
Beta strandi201 – 2077
Helixi214 – 2163
Helixi219 – 2268
Beta strandi229 – 2335
Helixi237 – 2426
Helixi247 – 2504
Turni251 – 2533
Beta strandi260 – 2623
Helixi265 – 2728
Helixi275 – 29218
Helixi293 – 2953
Helixi299 – 30911
Helixi315 – 3173
Beta strandi320 – 3234
Helixi328 – 33710
Helixi345 – 35814
Helixi359 – 3613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C91X-ray2.30A/B/C/D/E/F/G/H/I/J30-367[»]
ProteinModelPortaliQ8CG76.
SMRiQ8CG76. Positions 43-367.

Miscellaneous databases

EvolutionaryTraceiQ8CG76.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250286.
HOVERGENiHBG050576.
InParanoidiA2AMV3.
KOiK15303.
OMAiCTVKIAT.
OrthoDBiEOG77127F.
TreeFamiTF329173.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
SUPFAMiSSF51430. SSF51430. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CG76-1 [UniParc]FASTAAdd to Basket

« Hide

MLRAASRAVG RAAVRSAQRS GTSVGRPLAM SRPPPPRAAS GAPLRPATVL    50
GTMEMGRRMD ASASAASVRA FLERGHSELD TAFMYCDGQS ENILGGLGLG 100
LGSGDCTVKI ATKANPWEGK SLKPDSIRSQ LETSLKRLQC PRVDLFYLHA 150
PDHSTPVEET LRACHQLHQE GKFVELGLSN YASWEVAEIC TLCKSNGWIL 200
PTVYQGMYNA TTRQVEAELL PCLRHFGLRF YAYNPLAGGL LTGKYKYEDK 250
DGKQPVGRFF GNNWAETYRN RFWKEHHFEA IALVEKALQT TYGTNAPRMT 300
SAALRWMYHH SQLQGTRGDA VILGMSSLEQ LEQNLAATEE GPLEPAVVEA 350
FDQAWNMVAH ECPNYFR 367
Length:367
Mass (Da):40,612
Last modified:July 27, 2011 - v3
Checksum:i1123BD7028D3FBDF
GO

Sequence cautioni

The sequence AAH31857.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAC81077.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAC81078.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → G in BAE25302. 1 Publication
Sequence conflicti9 – 91V → G in BAE25302. 1 Publication
Sequence conflicti12 – 121A → V in BAE25302. 1 Publication
Sequence conflicti17 – 171A → G in BAE25302. 1 Publication
Sequence conflicti127 – 1271I → V in AAH31857. 1 Publication
Sequence conflicti127 – 1271I → V in CAC81078. 1 Publication
Sequence conflicti162 – 1621R → C in AAO38437. 1 Publication
Sequence conflicti354 – 3541A → G in AAH31857. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK143203 mRNA. Translation: BAE25302.1.
AL807811 Genomic DNA. Translation: CAM18543.1.
BC031857 mRNA. Translation: AAH31857.1. Different initiation.
AJ271800 mRNA. Translation: CAC81077.1. Different initiation.
AJ271801 mRNA. Translation: CAC81078.1. Different initiation.
AF525358 mRNA. Translation: AAO38437.2.
BK000393 mRNA. Translation: DAA00087.1.
CCDSiCCDS18844.1.
RefSeqiNP_079613.3. NM_025337.3.
UniGeneiMm.482154.

Genome annotation databases

EnsembliENSMUST00000073787; ENSMUSP00000073459; ENSMUSG00000028743.
GeneIDi110198.
KEGGimmu:110198.
UCSCiuc008vmc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK143203 mRNA. Translation: BAE25302.1 .
AL807811 Genomic DNA. Translation: CAM18543.1 .
BC031857 mRNA. Translation: AAH31857.1 . Different initiation.
AJ271800 mRNA. Translation: CAC81077.1 . Different initiation.
AJ271801 mRNA. Translation: CAC81078.1 . Different initiation.
AF525358 mRNA. Translation: AAO38437.2 .
BK000393 mRNA. Translation: DAA00087.1 .
CCDSi CCDS18844.1.
RefSeqi NP_079613.3. NM_025337.3.
UniGenei Mm.482154.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C91 X-ray 2.30 A/B/C/D/E/F/G/H/I/J 30-367 [» ]
ProteinModelPortali Q8CG76.
SMRi Q8CG76. Positions 43-367.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CG76. 3 interactions.
MINTi MINT-1869477.

PTM databases

PhosphoSitei Q8CG76.

2D gel databases

REPRODUCTION-2DPAGE Q8CG76.

Proteomic databases

MaxQBi Q8CG76.
PaxDbi Q8CG76.
PRIDEi Q8CG76.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000073787 ; ENSMUSP00000073459 ; ENSMUSG00000028743 .
GeneIDi 110198.
KEGGi mmu:110198.
UCSCi uc008vmc.2. mouse.

Organism-specific databases

CTDi 110198.
MGIi MGI:107796. Akr7a5.

Phylogenomic databases

eggNOGi COG0667.
GeneTreei ENSGT00550000074567.
HOGENOMi HOG000250286.
HOVERGENi HBG050576.
InParanoidi A2AMV3.
KOi K15303.
OMAi CTVKIAT.
OrthoDBi EOG77127F.
TreeFami TF329173.

Enzyme and pathway databases

SABIO-RK Q8CG76.

Miscellaneous databases

EvolutionaryTracei Q8CG76.
NextBioi 363519.
PROi Q8CG76.
SOURCEi Search...

Gene expression databases

Bgeei Q8CG76.
Genevestigatori Q8CG76.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
SUPFAMi SSF51430. SSF51430. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: Eye.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] OF 5-367.
    Strain: FVB/N.
    Tissue: Liver.
  4. "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells."
    Praml C., Savelyeva L., Schwab M.
    Oncogene 22:4765-4773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-367.
    Strain: BALB/c.
  5. "Characterisation of a novel mouse liver aldo-keto reductase AKR7A5."
    Hinshelwood A., McGarvie G., Ellis E.
    FEBS Lett. 523:213-218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-367, TISSUE SPECIFICITY.
    Strain: CD-1.
    Tissue: Liver.
  6. Ellis E.M., Hinshelwood A., McGarvie G.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 127 AND 162.
  7. "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins."
    Kelly V.P., Sherratt P.J., Crouch D.H., Hayes J.D.
    Biochem. J. 366:847-861(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of mouse succinic semialdehyde reductase AKR7A5: structural basis for substrate specificity."
    Zhu X., Lapthorn A.J., Ellis E.M.
    Biochemistry 45:1562-1570(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-367 IN COMPLEX WITH NADP AND THE INHIBITOR TARTRATE, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiARK72_MOUSE
AccessioniPrimary (citable) accession number: Q8CG76
Secondary accession number(s): A2AMV3
, Q3UPU2, Q8CG77, Q8JZQ8, Q9D157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 107 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, 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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