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Q5RJP0

- ALD1_RAT

UniProt

Q5RJP0 - ALD1_RAT

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Protein

Aldose reductase-related protein 1

Gene

Akr1b7

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes.1 Publication

Catalytic activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.2 Publications

Enzyme regulationi

Inhibited by tolrestat and epalrestat.1 Publication

Kineticsi

  1. KM=1.5 µM for NADPH2 Publications
  2. KM=220 µM for NADH2 Publications
  3. KM=0.16 µM for 4-oxo-2-nonenal2 Publications
  4. KM=37 µM for geraniol2 Publications
  5. KM=1.5 µM for 4-nitrobenzaldehyde2 Publications

pH dependencei

Optimum pH is 6.5-7.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441NADP1 Publication
Active sitei49 – 491Proton donorBy similarity
Sitei78 – 781Lowers pKa of active site TyrBy similarity
Binding sitei184 – 1841NADP1 Publication
Binding sitei273 – 2731NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 212NADP1 Publication
Nucleotide bindingi160 – 1612NADP1 Publication
Nucleotide bindingi210 – 2156NADP1 Publication
Nucleotide bindingi263 – 2697NADP1 Publication

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: RGD
  2. aldo-keto reductase (NADP) activity Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_199015. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase-related protein 1 (EC:1.1.1.21)
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member B7
Aldose reductase-like protein AKR1B14
Gene namesi
Name:Akr1b7
Synonyms:Akr1b14
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi620257. Akr1b7.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi269 – 2691H → F or R: Reduced affinity for NADP. 1 Publication
Mutagenesisi269 – 2691H → M: Strongly reduced affinity for NADP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Aldose reductase-related protein 1PRO_0000415351Add
BLAST

Proteomic databases

PaxDbiQ5RJP0.
PRIDEiQ5RJP0.

Expressioni

Gene expression databases

GenevestigatoriQ5RJP0.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013423.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi12 – 198Combined sources
Helixi27 – 3711Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 493Combined sources
Helixi52 – 6413Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 833Combined sources
Helixi86 – 10015Combined sources
Beta strandi105 – 1117Combined sources
Helixi138 – 15013Combined sources
Beta strandi153 – 1619Combined sources
Helixi164 – 1718Combined sources
Beta strandi182 – 1865Combined sources
Helixi194 – 2018Combined sources
Turni202 – 2043Combined sources
Beta strandi206 – 2105Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25410Combined sources
Turni255 – 2573Combined sources
Helixi267 – 2737Combined sources
Helixi283 – 2908Combined sources
Helixi302 – 3043Combined sources
Helixi311 – 3133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O3RX-ray1.86A/B1-316[»]
3QKZX-ray1.87A/B1-316[»]
ProteinModelPortaliQ5RJP0.
SMRiQ5RJP0. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5RJP0.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiQ5RJP0.
KOiK00011.
OMAiHINCAYV.
OrthoDBiEOG70KGQF.
PhylomeDBiQ5RJP0.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5RJP0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTFVKLRTK AKMPLVGLGT WKSPPGQVKE AVKAAIDAGY RHFDCAYVYQ 
        60         70         80         90        100
NESEVGEAIQ EKIKEKAVRR EDLFIVSKLW STFFEKSLMK EAFQKTLSDL 
       110        120        130        140        150
KLDYLDLYLI HWPQGLQAGK EFLPKDSQGK VLMSKSTFLD AWEGMEELVD 
       160        170        180        190        200
QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC 
       210        220        230        240        250
HSKGIAVIAY SPLGSPDRPY AKPEDPVVLE IPKIKEIAAK HKKTIAQVLI 
       260        270        280        290        300
RFHVQRNVAV IPKSVTLSHI KENIQVFDFQ LSEEDMAAIL SLNRNWRACG 
       310 
LFVTSDEEDF PFHEEY
Length:316
Mass (Da):36,122
Last modified:December 21, 2004 - v1
Checksum:iE5733ADA0ED5FF21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473959 Genomic DNA. Translation: EDM15308.1.
BC086563 mRNA. Translation: AAH86563.1.
RefSeqiNP_446233.2. NM_053781.2.
UniGeneiRn.32702.

Genome annotation databases

EnsembliENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
GeneIDi116463.
KEGGirno:116463.
UCSCiRGD:620257. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 CH473959 Genomic DNA. Translation: EDM15308.1 .
BC086563 mRNA. Translation: AAH86563.1 .
RefSeqi NP_446233.2. NM_053781.2.
UniGenei Rn.32702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O3R X-ray 1.86 A/B 1-316 [» ]
3QKZ X-ray 1.87 A/B 1-316 [» ]
ProteinModelPortali Q5RJP0.
SMRi Q5RJP0. Positions 1-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000013423.

Proteomic databases

PaxDbi Q5RJP0.
PRIDEi Q5RJP0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000013423 ; ENSRNOP00000013423 ; ENSRNOG00000009875 .
GeneIDi 116463.
KEGGi rno:116463.
UCSCi RGD:620257. rat.

Organism-specific databases

CTDi 11997.
RGDi 620257. Akr1b7.

Phylogenomic databases

eggNOGi COG0656.
GeneTreei ENSGT00760000119041.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi Q5RJP0.
KOi K00011.
OMAi HINCAYV.
OrthoDBi EOG70KGQF.
PhylomeDBi Q5RJP0.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_199015. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTracei Q5RJP0.
NextBioi 618984.
PROi Q5RJP0.

Gene expression databases

Genevestigatori Q5RJP0.

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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  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].
    Tissue: Ovary.
  4. "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
    Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
    Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  5. "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
    Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
    Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
+Additional computationally mapped references.

Entry informationi

Entry nameiALD1_RAT
AccessioniPrimary (citable) accession number: Q5RJP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: December 21, 2004
Last modified: January 7, 2015
This is version 74 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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