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P45377

- ALD2_MOUSE

UniProt

P45377 - ALD2_MOUSE

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Protein

Aldose reductase-related protein 2

Gene

Akr1b8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton donor
Sitei78 – 781Lowers pKa of active site TyrBy similarity
Binding sitei111 – 1111Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 27363NADP1 PublicationAdd
BLAST

GO - Molecular functioni

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_198569. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase-related protein 2 (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
Aldehyde reductase
Fibroblast growth factor-regulated protein
Protein FR-1
Gene namesi
Name:Akr1b8
Synonyms:Fgfrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:107673. Akr1b8.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Aldose reductase-related protein 2PRO_0000124631Add
BLAST

Proteomic databases

MaxQBiP45377.
PaxDbiP45377.
PRIDEiP45377.

2D gel databases

REPRODUCTION-2DPAGEIPI00273096.
P45377.

PTM databases

PhosphoSiteiP45377.

Expressioni

Inductioni

By FGF-1.

Gene expression databases

BgeeiP45377.
GenevestigatoriP45377.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiP45377. 1 interaction.
MINTiMINT-4087589.
STRINGi10090.ENSMUSP00000040244.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Beta strandi12 – 165
Helixi25 – 3713
Beta strandi42 – 443
Helixi47 – 493
Helixi52 – 6413
Helixi70 – 723
Beta strandi74 – 796
Helixi81 – 833
Helixi86 – 10015
Beta strandi105 – 1106
Helixi138 – 15013
Beta strandi153 – 1619
Helixi164 – 1718
Beta strandi182 – 1865
Helixi194 – 2029
Beta strandi206 – 2116
Turni228 – 2303
Helixi232 – 2409
Helixi245 – 25410
Turni255 – 2573
Helixi267 – 2748
Helixi283 – 2908
Helixi302 – 3043

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FRBX-ray1.70A2-316[»]
ProteinModelPortaliP45377.
SMRiP45377. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45377.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP45377.
KOiK00011.
OMAiYAYCNEN.
OrthoDBiEOG70KGQF.
PhylomeDBiP45377.
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.

P45377-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATFVELSTK AKMPIVGLGT WKSPPNQVKE AVKAAIDAGY RHIDCAYAYC
60 70 80 90 100
NENEVGEAIQ EKIKEKAVQR EDLFIVSKLW PTCFEKKLLK EAFQKTLTDL
110 120 130 140 150
KLDYLDLYLI HWPQGLQPGK ELFPKDDQGR ILTSKTTFLE AWEGMEELVD
160 170 180 190 200
QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC
210 220 230 240 250
HSKGISVTAY SPLGSPDRPS AKPEDPSLLE DPKIKEIAAK HEKTSAQVLI
260 270 280 290 300
RFHIQRNVVV IPKSVTPSRI QENIQVFDFQ LSDEEMATIL SFNRNWRACL
310
LPETVNMEEY PYDAEY
Length:316
Mass (Da):36,121
Last modified:January 23, 2007 - v2
Checksum:i0C6F0A7BA806497C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421E → K in AAH05789. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04204 mRNA. Translation: AAA16953.1.
BC005789 mRNA. Translation: AAH05789.1.
CCDSiCCDS19991.1.
PIRiA53440.
RefSeqiNP_032038.1. NM_008012.1.
UniGeneiMm.5378.

Genome annotation databases

EnsembliENSMUST00000038406; ENSMUSP00000040244; ENSMUSG00000029762.
GeneIDi14187.
KEGGimmu:14187.
UCSCiuc009bgz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04204 mRNA. Translation: AAA16953.1 .
BC005789 mRNA. Translation: AAH05789.1 .
CCDSi CCDS19991.1.
PIRi A53440.
RefSeqi NP_032038.1. NM_008012.1.
UniGenei Mm.5378.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FRB X-ray 1.70 A 2-316 [» ]
ProteinModelPortali P45377.
SMRi P45377. Positions 2-315.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P45377. 1 interaction.
MINTi MINT-4087589.
STRINGi 10090.ENSMUSP00000040244.

PTM databases

PhosphoSitei P45377.

2D gel databases

REPRODUCTION-2DPAGE IPI00273096.
P45377.

Proteomic databases

MaxQBi P45377.
PaxDbi P45377.
PRIDEi P45377.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038406 ; ENSMUSP00000040244 ; ENSMUSG00000029762 .
GeneIDi 14187.
KEGGi mmu:14187.
UCSCi uc009bgz.1. mouse.

Organism-specific databases

CTDi 14187.
MGIi MGI:107673. Akr1b8.

Phylogenomic databases

eggNOGi COG0656.
GeneTreei ENSGT00760000119041.
HOGENOMi HOG000250272.
HOVERGENi HBG000020.
InParanoidi P45377.
KOi K00011.
OMAi YAYCNEN.
OrthoDBi EOG70KGQF.
PhylomeDBi P45377.
TreeFami TF106492.

Enzyme and pathway databases

Reactomei REACT_198569. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTracei P45377.
NextBioi 285402.
PROi P45377.
SOURCEi Search...

Gene expression databases

Bgeei P45377.
Genevestigatori P45377.

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. "A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase."
    Donohue P.J., Alberts G.F., Hampton B.S., Winkles J.A.
    J. Biol. Chem. 269:8604-8609(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "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.
  3. "1.7-A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor."
    Wilson D.K., Nakano T., Petrash M., Quiocho F.A.
    Biochemistry 34:14323-14330(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR.

Entry informationi

Entry nameiALD2_MOUSE
AccessioniPrimary (citable) accession number: P45377
Secondary accession number(s): Q99JN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 119 of the entry and version 2 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