[1]	NUCLEOTIDE SEQUENCE. TISSUE=Vas deferens; DOI=10.1016/0960-0760(92)90445-O; PubMed=1637719 [NCBI, ExPASy, EBI, Israel, Japan] Pailhoux E.A., Veyssiere G.M., Fabre S., Tournaire C., Jean C.G.; "The genomic organization and DNA sequence of the mouse vas deferens androgen regulated protein gene."; J. Steroid Biochem. Mol. Biol. 42:561-568(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CD-1; TISSUE=Vas deferens; PubMed=2123194 [NCBI, ExPASy, EBI, Israel, Japan] Pailhoux E.A., Martinez A., Veyssiere G.M., Jean C.G.; "Androgen-dependent protein from mouse vas deferens. cDNA cloning and protein homology with the aldo-keto reductase superfamily."; J. Biol. Chem. 265:19932-19936(1990).

Comments

FUNCTION: The role of MVDP in sperm maturation and storage may be related to its potential capacity to produce fructose, or MVDP may play an osmoregulatory role by producing sorbitol.
CATALYTIC ACTIVITY: Alditol + NAD(P)⁺ = aldose + NAD(P)H.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
INDUCTION: Castration resulted in a marked decrease in the level of the mRNA coding for the protein, whereas administration of testosterone to castrated males resulted in a marked increase.
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

M81448; AAA39774.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05663; AAA39773.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A37990; A37990.

NP_033861.2; -.

3D structure databases

HSSP

P45377; 1FRB. [HSSP ENTRY / PDB]

P21300; 1-316.

2D gel databases

P21300; -.

Organism-specific databases

MGI

MGI:101918; Akr1b7.

Gene expression databases

ArrayExpress

P21300; -.

CleanEx

MM_AKR1B7; -.

GermOnline

ENSMUSG00000052131; 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:0044255;	Biological process: cellular lipid metabolic process (traceable author statement from MGI).
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

P21300.

Genome annotation databases

Ensembl

ENSMUSG00000052131; Mus musculus. [Contig view]

GeneID

11997; -.

KEGG

mmu:11997; -.

Phylogenomic databases

HOGENOM

P21300; -.

HOVERGEN

P21300; -.

Other

NextBio

280181; -.

SOURCE

Akr1b7; Mus musculus.

UniRef

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

Keywords

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 1.`	`PRO_0000124629`
`NP_BIND`	`211 273`	`63`	`NADP (By similarity).`
`ACT_SITE`	`49 49`		`Proton donor (By similarity).`
`BINDING`	`111 111`		`Substrate (By similarity).`
`SITE`	`78 78`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`CONFLICT`	`94 94`		`Q -> D (in Ref. 2; AAA39773).`

Sequence information

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

Molecular weight: 35988 Da [This is the MW of the unprocessed precursor]

CRC64: 6BC46B6076969742 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATFVELSTK AKMPLVGLGT WKSSPGQVKE AVKAAIDAGY RHIDCAYVYH NENEVGEAIQ 

        70         80         90        100        110        120 
EKIKENAVKR EDLFIVSKLW ATFFEKSLVK KAFQNTLSDL KLDYLDLYLV HWPQGFQAGN 

       130        140        150        160        170        180 
ALLPKDNKGK VLLSKSTFLD AWEAMEELVD QGLVKALGIS NFNHFQIERL LNKPGLKHKP 

       190        200        210        220        230        240 
VTNQIESHPY LTQEKLIQYC QSKGIAVTAY SPLGSPDRPY AKPEDPVVME IPKIKEIAAK 

       250        260        270        280        290        300 
HKKTVAQVLI RFHVQRNVVV IPKSVTPSRI QENLQVFDFQ LSEEDMAAIL SFNRNWRACD 

       310 
LLDARTEEDY PFHEEY

P21300 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