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Q9DB73 (NB5R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-cytochrome b5 reductase 1
Short name=b5R.1
EC=1.6.2.2
Alternative name(s):
NAD(P)H:quinone oxidoreductase type 3 polypeptide A2
Gene names
Name:Cyb5r1
Synonyms:Nqo3a2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction By similarity.

Catalytic activity

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactor

FAD By similarity.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.

Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processsterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay. Source: MGI

   Molecular functioncytochrome-b5 reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9DB73-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9DB73-2)

The sequence of this isoform differs from the canonical sequence as follows:
     159-228: GNFNIQPNKK...DIILREDLEE → ESACVHGCTW...DDPSTVPCLW
     229-305: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305NADH-cytochrome b5 reductase 1
PRO_0000287546

Regions

Transmembrane8 – 2821Helical; Potential
Domain44 – 156113FAD-binding FR-type
Nucleotide binding136 – 16631FAD By similarity
Nucleotide binding175 – 21036FAD By similarity

Natural variations

Alternative sequence159 – 22870GNFNI…EDLEE → ESACVHGCTWAKSPEATMLY GKADFTLWRLPEETYASPSF TKDFPLAKDQKRKLFSSSHG DDPSTVPCLW in isoform 2.
VSP_025557
Alternative sequence229 – 30577Missing in isoform 2.
VSP_025558

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 847B9AAFD99ED035

FASTA30534,135
        10         20         30         40         50         60 
MGIQPSPVLL ASLGVGLLTL LGLALGTYLV RRSRRPQVTL QDPDEKYLLR LLDKTTVSHN 

        70         80         90        100        110        120 
TRRFRFALPT AHHILGLPVG KHVYLSARID GSLVIRPYTP VTSDEDQGYV DLVIKVYLKG 

       130        140        150        160        170        180 
VHPKFPEGGK MSQYLDSLKI GDMVEFRGPS GLLSYAGKGN FNIQPNKKSP PELRVAKKLG 

       190        200        210        220        230        240 
MIAGGTGITP MLQLIRAILK VPEDPTQCFL LFANQTERDI ILREDLEELQ AQYPNRFKLW 

       250        260        270        280        290        300 
FTLDSPPEDW TYSKGFVTAD MIQEHLPAPA EDVLLLLCGP PPMVQLACHP NLDKLGYSQK 


MRFTY

« Hide

Isoform 2 [UniParc].

Checksum: 85FCC210489EDD32
Show »

FASTA22825,305

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Cerebellum.
[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] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Kidney and Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK005159 mRNA. Translation: BAB23850.1.
AK159663 mRNA. Translation: BAE35270.1.
AK167178 mRNA. Translation: BAE39313.1.
BC016266 mRNA. Translation: AAH16266.1.
BC024618 mRNA. Translation: AAH24618.1.
IPIIPI00119131.
IPI00127437.
RefSeqNP_082333.1. NM_028057.2.
UniGeneMm.280230.

3D structure databases

HSSPHSSP built from PDB template 1QX4 based on UniProtKB P20070.
ProteinModelPortalQ9DB73.
SMRQ9DB73. Positions 36-305.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9DB73.

PTM databases

PhosphoSiteQ9DB73.

Proteomic databases

PRIDEQ9DB73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027726; ENSMUSP00000027726; ENSMUSG00000026456.
ENSMUST00000049223; ENSMUSP00000047250; ENSMUSG00000026456.
ENSMUST00000154237; ENSMUSP00000133385; ENSMUSG00000026456.
GeneID72017.
KEGGmmu:72017.
UCSCuc007cru.1. mouse.

Organism-specific databases

CTD51706.
MGIMGI:1919267. Cyb5r1.

Phylogenomic databases

eggNOGroNOG09425.
GeneTreeENSGT00390000008881.
HOGENOMHBG591994.
HOVERGENHBG052580.
InParanoidQ9DB73.
OMALQARYPS.
OrthoDBEOG418BNW.
PhylomeDBQ9DB73.

Gene expression databases

ArrayExpressQ9DB73.
BgeeQ9DB73.
CleanExMM_CYB5R1.
GenevestigatorQ9DB73.

Family and domain databases

InterProIPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001834. NADH-Cyt_B5_reductase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
KOK00326.
PfamPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio335228.
SOURCESearch...

Entry information

Entry nameNB5R1_MOUSE
AccessionPrimary (citable) accession number: Q9DB73
Secondary accession number(s): Q91W81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents