[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; PubMed=7510692 [NCBI, ExPASy, EBI, Israel, Japan] Donohue P.J., Alberts G.F., Hampton B.S., Winkles J.A.; "A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase."; J. Biol. Chem. 269:8604-8609(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADPH AND INHIBITOR. DOI=10.1021/bi00044a009; PubMed=7578036 [NCBI, ExPASy, EBI, Israel, Japan] Wilson D.K., Nakano T., Petrash M., Quiocho F.A.; "1.7-A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor."; Biochemistry 34:14323-14330(1995).

Comments

CATALYTIC ACTIVITY: Alditol + NAD(P)⁺ = aldose + NAD(P)H.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
INDUCTION: By FGF-1.
SIMILARITY: Belongs to the aldo/keto reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U04204; AAA16953.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005789; AAH05789.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A53440; A53440.

NP_032038.1; -.

3D structure databases

PDB

1FRB; X-ray; 1.70 A; A=1-316.

[ExPASy / RCSB / EBI]

1FRB; -.

PTM databases

P45377; -.

2D gel databases

REPRODUCTION-2DPAGE

P45377; -.

Organism-specific databases

MGI

MGI:107673; Akr1b8.

Gene expression databases

ArrayExpress

P45377; -.

GermOnline

ENSMUSG00000029762; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004032;	Molecular function: aldehyde reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.100; Aldo/ket_red; 1.

PANTHER

PTHR11732; Aldo/ket_red; 1.

Pfam

PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00069; ALDKETRDTASE.

ProDom

PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.

ProtoNet

P45377.

Genome annotation databases

Ensembl

ENSMUSG00000029762; Mus musculus. [Contig view]

GeneID

14187; -.

KEGG

mmu:14187; -.

Phylogenomic databases

HOGENOM

P45377; -.

HOVERGEN

P45377; -.

Other

LinkHub

P45377; -.

NextBio

285402; -.

SOURCE

Akr1b8; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 316`	`315`	`Aldose reductase-related protein 2.`	`PRO_0000124631`
`NP_BIND`	`211 273`	`63`	`NADP.`
`ACT_SITE`	`49 49`		`Proton donor.`
`BINDING`	`111 111`		`Substrate.`
`SITE`	`78 78`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`CONFLICT`	`242 242`		`E -> K (in Ref. 2; AAH05789).`
`STRAND`	`4 6`	`3`
`STRAND`	`12 16`	`5`
`HELIX`	`25 37`	`13`
`STRAND`	`42 44`	`3`
`HELIX`	`47 49`	`3`
`HELIX`	`52 64`	`13`
`HELIX`	`70 72`	`3`
`STRAND`	`74 79`	`6`
`HELIX`	`81 83`	`3`
`HELIX`	`86 100`	`15`
`STRAND`	`105 110`	`6`
`HELIX`	`138 150`	`13`
`STRAND`	`153 161`	`9`
`HELIX`	`164 171`	`8`
`STRAND`	`182 186`	`5`
`HELIX`	`194 202`	`9`
`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`

Sequence information

Length: 316 AA [This is the length of the unprocessed precursor]

Molecular weight: 36121 Da [This is the MW of the unprocessed precursor]

CRC64: 0C6F0A7BA806497C [This is a checksum on the sequence]

        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

P45377 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools