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Q64429 (CP1B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 1B1
EC=1.14.14.1
Alternative name(s):
CYPIB1
Cytochrome P450CMEF
Short name=Cytochrome P450EF
Gene names
Name:Cyp1b1
Synonyms:Cyp1-b1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Catalytic activity

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Induction

By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from mutant phenotype PubMed 19005183. Source: MGI

cellular aromatic compound metabolic process

Inferred from direct assay PubMed 1910294. Source: MGI

endothelial cell migration

Inferred from mutant phenotype PubMed 19005183. Source: MGI

endothelial cell-cell adhesion

Inferred from mutant phenotype PubMed 19005183. Source: MGI

response to toxin

Inferred from mutant phenotype PubMed 16377763. Source: MGI

retina vasculature development in camera-type eye

Inferred from mutant phenotype PubMed 19005183. Source: MGI

toxin metabolic process

Inferred from mutant phenotype PubMed 10051580PubMed 17166882. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen

Inferred from direct assay PubMed 9367523. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543Cytochrome P450 1B1
PRO_0000051661

Sites

Metal binding4701Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1951Q → P in CAA55205. Ref.2
Sequence conflict3071A → D in CAA55205. Ref.2
Sequence conflict3281F → G in CAA55205. Ref.2
Sequence conflict4571A → T in CAA55205. Ref.2
Sequence conflict5161F → V in CAA55205. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q64429 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 7C89B4312CB5BC4A

FASTA54360,537
        10         20         30         40         50         60 
MATSLSADSP QQLSSLSTQQ TTLLLLFSVL AAVHLGQWLL RQWQRKPWSS PPGPFPWPLI 

        70         80         90        100        110        120 
GNAAAVGQAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE SAIHQALVQQ GSIFADRPPF 

       130        140        150        160        170        180 
ASFRVVSGGR SLAFGHYSEH WKTQRRSAYS TMRAFSTRHP RSRGLLEGHA LAEARELVAV 

       190        200        210        220        230        240 
LVRRCAGGAF LDPTQPVIVA VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL 

       250        260        270        280        290        300 
VDVLPWLQLF PNPVRTTFRK FEQLNRNFSN FVLDKFLRHR ESLVPGAAPR DMTDAFILSA 

       310        320        330        340        350        360 
EKKASGAPGD DSSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP DVQARVQAEL 

       370        380        390        400        410        420 
DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FSSFLPVTIP HATTANTFVL GYYIPKNTVV 

       430        440        450        460        470        480 
FVNQWSVNHD PAKWPNPEDF DPARFLDKDG FINKALASSV MIFSVGKRRC IGEELSKMLL 

       490        500        510        520        530        540 
FLFISILAHQ CNFKANQNES SNMSFSYGLT IKPKSFRIHV SLRESMELLD NAVKKLQTEE 


GCK

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning, sequence analysis, and induction by aryl hydrocarbons of a murine cytochrome P450 gene, Cyp1b1."
Shen Z., Liu J., Wells R.L., Elkind M.M.
DNA Cell Biol. 13:763-769(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[2]"Mouse cytochrome P-450EF, representative of a new 1B subfamily of cytochrome P-450s. Cloning, sequence determination, and tissue expression."
Savas U., Bhattacharyya K.K., Christou M., Alexander D.L., Jefcoate C.R.
J. Biol. Chem. 269:14905-14911(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Identification of a cytochrome P450 gene by reverse transcription-PCR using degenerate primers containing inosine."
Shen Z., Wells R.L., Liu J., Elkind M.M.
Proc. Natl. Acad. Sci. U.S.A. 90:11483-11487(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 361-466.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U03283 mRNA. Translation: AAC52141.1.
X78445 mRNA. Translation: CAA55205.1.
AK137461 mRNA. Translation: BAE23362.1.
CH466537 Genomic DNA. Translation: EDL38490.1.
U02479 mRNA. Translation: AAC52131.1.
IPIIPI00316177.
PIRA53790.
RefSeqNP_034124.1. NM_009994.1.
UniGeneMm.214016.

3D structure databases

ProteinModelPortalQ64429.
SMRQ64429. Positions 68-530.
ModBaseSearch...

PTM databases

PhosphoSiteQ64429.

Proteomic databases

PaxDbQ64429.
PRIDEQ64429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
GeneID13078.
KEGGmmu:13078.

Organism-specific databases

CTD1545.
MGIMGI:88590. Cyp1b1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00680000099714.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidQ3UVA8.
KOK07410.
OMANEPSKMS.
OrthoDBEOG48WC1T.

Gene expression databases

ArrayExpressQ64429.
BgeeQ64429.
GenevestigatorQ64429.
GermOnlineENSMUSG00000024087. Mus musculus.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283028.
SOURCESearch...

Entry information

Entry nameCP1B1_MOUSE
AccessionPrimary (citable) accession number: Q64429
Secondary accession number(s): Q3UVA8, Q60593, Q64461
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 109 of the entry and version 3 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents