Reviewed, UniProtKB/Swiss-Prot P45377 (ALD2_MOUSE)

Names and origin

Protein names

Recommended name:
    Aldose reductase-related protein 2
      Short name=AR
    EC=1.1.1.21
Alternative name(s):
    Aldehyde reductase
    Fibroblast growth factor-regulated protein
    Protein FR-1

Gene names

Name:	Akr1b8
Synonyms:	Fgfrp

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Alditol + NAD(P)+ = aldose + NAD(P)H.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	By FGF-1.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 316

315

Aldose reductase-related protein 2

PRO_0000124631

Regions

Nucleotide binding

211 – 273

63

NADP

Sites

Active site

49

1

Proton donor

Binding site

111

1

Substrate

Site

78

1

Lowers pKa of active site Tyr By similarity

Experimental info

Sequence conflict

242

1

E → K in AAH05789. Ref.2

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Beta strand

12 – 16

5

Helix

25 – 37

13

Beta strand

42 – 44

3

Helix

47 – 49

3

Helix

52 – 64

13

Helix

70 – 72

3

Beta strand

74 – 79

6

Helix

81 – 83

3

Helix

86 – 100

15

Beta strand

105 – 110

6

Helix

138 – 150

13

Beta strand

153 – 161

9

Helix

164 – 171

8

Beta strand

182 – 186

5

Helix

194 – 202

9

Beta strand

206 – 211

6

Turn

228 – 230

3

Helix

232 – 240

9

Helix

245 – 254

10

Turn

255 – 257

3

Helix

267 – 274

8

Helix

283 – 290

8

Helix

302 – 304

3

Sequences

	Sequence		Length	Mass (Da)
	P45377-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0C6F0A7BA806497C	FASTA	316	36,121
	10 20 30 40 50 60 MATFVELSTK AKMPIVGLGT WKSPPNQVKE AVKAAIDAGY RHIDCAYAYC NENEVGEAIQ 70 80 90 100 110 120 EKIKEKAVQR EDLFIVSKLW PTCFEKKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK 130 140 150 160 170 180 ELFPKDDQGR ILTSKTTFLE AWEGMEELVD QGLVKALGVS NFNHFQIERL LNKPGLKHKP 190 200 210 220 230 240 VTNQVECHPY LTQEKLIQYC HSKGISVTAY SPLGSPDRPS AKPEDPSLLE DPKIKEIAAK 250 260 270 280 290 300 HEKTSAQVLI RFHIQRNVVV IPKSVTPSRI QENIQVFDFQ LSDEEMATIL SFNRNWRACL 310 LPETVNMEEY PYDAEY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7510692] [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: 15489334] [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: 7578036] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U04204 mRNA. Translation: AAA16953.1.
BC005789 mRNA. Translation: AAH05789.1.

IPI

IPI00273096.

PIR

A53440.

RefSeq

NP_032038.1.

UniGene

Mm.5378

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FRB	X-ray	1.70	A	2-316	[»]

ModBase

Search...

PTM databases

PhosphoSite

P45377.

2-D gel databases

REPRODUCTION-2DPAGE

P45377.

Proteomic databases

PRIDE

P45377.

Genome annotation databases

Ensembl

ENSMUSG00000029762. Mus musculus. [Contig view]

GeneID

14187.

KEGG

mmu:14187.

Organism-specific databases

MGI

MGI:107673. Akr1b8.

Phylogenomic databases

HOGENOM

P45377.

HOVERGEN

P45377.

OMA

P45377. PAHIVEN.

Enzyme and pathway databases

BRENDA

1.1.1.21. 244.

Gene expression databases

ArrayExpress

P45377.

Bgee

P45377.

GermOnline

ENSMUSG00000029762. Mus musculus.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

285402.

SOURCE

Search...

Entry information

Entry name

ALD2_MOUSE

Accession

Primary (citable) accession number: P45377
Secondary accession number(s): Q99JN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)