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Q64429 (CP1B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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

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 lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Catalytic activity

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

Cofactor

Heme group By similarity.

Enzyme regulation

Activated by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Inhibited by 12-O-Tetradecanoylphorbol-13-acetate and PRKCB. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Mitochondrion Ref.10.

Tissue specificity

Constitutively expressed in retinal, heart and kidney pericytes cells. Ref.11

Induction

By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Ref.6 Ref.11

Disruption phenotype

Severe ocular drainage structure abnormalities, significant elevated intraocular pressure. Ref.12

Sequence similarities

Belongs to the cytochrome P450 family.

Biophysicochemical properties

Kinetic parameters:

kcat is 0.04 min(-1) for retinol, 0.08 min(-1) for retinal, 1.24 min(-1) for 7,12-dimethyltetraphene, 0.13 min(-1) for arachidonic acid.

KM=392.2 µM for retinol Ref.7

KM=153.9 µM for retinal

KM=138.9 µM for 7,12-dimethyltetraphene

KM=500.0 µM for arachidonic acid

Ontologies

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

Inferred from mutant phenotype. Source: UniProtKB

blood vessel morphogenesis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cell adhesion

Inferred from mutant phenotype Ref.12. Source: UniProtKB

cellular aromatic compound metabolic process

Inferred from direct assay PubMed 1910294. Source: MGI

cellular response to organic cyclic compound

Inferred from sequence orthology PubMed 23275542. Source: MGI

collagen fibril organization

Inferred from mutant phenotype Ref.12. Source: UniProtKB

endothelial cell migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

endothelial cell-cell adhesion

Inferred from mutant phenotype Ref.8. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype Ref.11Ref.12. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cell adhesion mediated by integrin

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

nitric oxide biosynthetic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

phagocytosis

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of JAK-STAT cascade

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of gene expression involved in extracellular matrix organization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation vascular endothelial growth factor production

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

response to toxic substance

Inferred from mutant phenotype PubMed 16377763. Source: MGI

retina vasculature development in camera-type eye

Inferred from mutant phenotype Ref.8. Source: MGI

retinal blood vessel morphogenesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

steroid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

toxin metabolic process

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

trabecular meshwork development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

xenobiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

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.
[6]"Regulation of cytochrome P4501B1 (CYP1B1) in mouse embryo fibroblast (C3H10T1/2) cells by protein kinase C (PKC)."
Ikegwuonu F.I., Christou M., Jefcoate C.R.
Biochem. Pharmacol. 57:619-630(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[7]"Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1."
Choudhary D., Jansson I., Stoilov I., Sarfarazi M., Schenkman J.B.
Drug Metab. Dispos. 32:840-847(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"CYP1B1 expression promotes the proangiogenic phenotype of endothelium through decreased intracellular oxidative stress and thrombospondin-2 expression."
Tang Y., Scheef E.A., Wang S., Sorenson C.M., Marcus C.B., Jefcoate C.R., Sheibani N.
Blood 113:744-754(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VASCULAR DEVELOPMENT AND ANGIOGENESIS.
[9]"CYP1B1 and endothelial nitric oxide synthase combine to sustain proangiogenic functions of endothelial cells under hyperoxic stress."
Tang Y., Scheef E.A., Gurel Z., Sorenson C.M., Jefcoate C.R., Sheibani N.
Am. J. Physiol. 298:C665-C678(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ANGIOGENESIS.
[10]"Mitochondrial targeting of mouse NQO1 and CYP1B1 proteins."
Dong H., Shertzer H.G., Genter M.B., Gonzalez F.J., Vasiliou V., Jefcoate C., Nebert D.W.
Biochem. Biophys. Res. Commun. 435:727-732(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Lack of Cyp1b1 promotes the proliferative and migratory phenotype of perivascular supporting cells."
Palenski T.L., Sorenson C.M., Jefcoate C.R., Sheibani N.
Lab. Invest. 93:646-662(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VASCULAR HOMEOSTASIS, TISSUE SPECIFICITY, INDUCTION.
[12]"Cyp1b1 mediates periostin regulation of trabecular meshwork development by suppression of oxidative stress."
Zhao Y., Wang S., Sorenson C.M., Teixeira L., Dubielzig R.R., Peters D.M., Conway S.J., Jefcoate C.R., Sheibani N.
Mol. Cell. Biol. 33:4225-4240(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRABECULAR MESHWORK DEVELOPMENT, DISRUPTION PHENOTYPE.
[13]"Specificity determinants of CYP1B1 estradiol hydroxylation."
Nishida C.R., Everett S., Ortiz de Montellano P.R.
Mol. Pharmacol. 84:451-458(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ESTROGEN METABOLISM.
+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.
CCDSCCDS28986.1.
PIRA53790.
RefSeqNP_034124.1. NM_009994.1.
UniGeneMm.214016.

3D structure databases

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

PTM databases

PhosphoSiteQ64429.

Proteomic databases

PaxDbQ64429.
PRIDEQ64429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
GeneID13078.
KEGGmmu:13078.
UCSCuc008dqc.1. mouse.

Organism-specific databases

CTD1545.
MGIMGI:88590. Cyp1b1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidQ3UVA8.
KOK07410.
OMANEPSKMS.
OrthoDBEOG7RBZ85.
TreeFamTF105095.

Gene expression databases

ArrayExpressQ64429.
BgeeQ64429.
GenevestigatorQ64429.

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. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283028.
PROQ64429.
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: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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