NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N;
TISSUE=Mammary tumor;
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).

Comments

FUNCTION: Catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. Possible role in protecting cells from oxidative damage or in regulating iron metabolism. In the liver, converts biliverdin to bilirubin (By similarity).
CATALYTIC ACTIVITY: Reduced riboflavin + NADP⁺ = riboflavin + NADPH.
CATALYTIC ACTIVITY: Bilirubin + NAD(P)⁺ = biliverdin + NAD(P)H.
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).

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

BC006617; AAH06617.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027279; AAH27279.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_659172.1; -.

UniGene

Mm.24021

3D structure databases

HSSP

P30043; 1HDO. [HSSP ENTRY / PDB]

SMR

Q923D2; 1-205.

ModBase

Q923D2.

Organism-specific databases

MGI

MGI:2385271; Blvrb.

Gene expression databases

ArrayExpress

Q923D2; -.

CleanEx

MM_BLVRB; -.

GermOnline

ENSMUSG00000040466; Mus musculus.

Family and domain databases

InterPro

IPR001509; Epimerase_deHydtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01370; Epimerase; 1.
Pfam graphical view of domain structure.

BLOCKS

Q923D2.

Genome annotation databases

Ensembl

ENSMUSG00000040466; Mus musculus. [Contig view]

GeneID

233016; -.

KEGG

mmu:233016; -.

Phylogenomic databases

HOGENOM

Q923D2; -.

HOVERGEN

Q923D2; -.

Other

Blvrb; Mus musculus.

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

Keywords

Cytoplasm; Multifunctional enzyme; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 206`	`205`	`Flavin reductase.`	`PRO_0000064949`
`NP_BIND`	`5 36`	`32`	`NAD or NADP (Potential).`

Sequence information

Length: 206 AA [This is the length of the unprocessed precursor]

Molecular weight: 22197 Da [This is the MW of the unprocessed precursor]

CRC64: EDAEE91F5F39F629 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVKKIAIFG ATGRTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPQPAHV VVGDVRQAAD 

        70         80         90        100        110        120 
VDKTVAGQEA VIVLLGTGND LSPTTVMSEG TRNIVTAMKA HGVDKVVACT SAFLLWDPTK 

       130        140        150        160        170        180 
VPPRLQDVTD DHIRMHKILQ ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD 

       190        200 
LGHFMLRCLT TNEYDGHTTY PSHQYD

Q923D2 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