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Q64429

- CP1B1_MOUSE

UniProt

Q64429 - CP1B1_MOUSE

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Protein

Cytochrome P450 1B1

Gene

Cyp1b1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

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

Cofactori

Heme group.By similarity

Enzyme regulationi

Activated by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Inhibited by 12-O-Tetradecanoylphorbol-13-acetate and PRKCB.1 Publication

Kineticsi

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.

  1. KM=392.2 µM for retinol1 Publication
  2. KM=153.9 µM for retinal1 Publication
  3. KM=138.9 µM for 7,12-dimethyltetraphene1 Publication
  4. KM=500.0 µM for arachidonic acid1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi470 – 4701Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. aromatase activity Source: UniProtKB-EC
  2. heme binding Source: UniProtKB
  3. iron ion binding Source: InterPro
  4. monooxygenase activity Source: UniProtKB
  5. 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 Source: MGI

GO - Biological processi

  1. angiogenesis Source: MGI
  2. arachidonic acid metabolic process Source: UniProtKB
  3. blood vessel morphogenesis Source: UniProtKB
  4. cell adhesion Source: UniProtKB
  5. cellular aromatic compound metabolic process Source: MGI
  6. cellular response to hydrogen peroxide Source: UniProtKB
  7. cellular response to organic cyclic compound Source: MGI
  8. collagen fibril organization Source: UniProtKB
  9. endothelial cell-cell adhesion Source: MGI
  10. endothelial cell migration Source: UniProtKB
  11. estrogen metabolic process Source: UniProtKB
  12. intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
  13. membrane lipid catabolic process Source: UniProtKB
  14. negative regulation of cell adhesion mediated by integrin Source: UniProtKB
  15. negative regulation of cell migration Source: UniProtKB
  16. negative regulation of cell proliferation Source: UniProtKB
  17. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  18. nitric oxide biosynthetic process Source: UniProtKB
  19. positive regulation of angiogenesis Source: UniProtKB
  20. positive regulation of apoptotic process Source: UniProtKB
  21. positive regulation of gene expression involved in extracellular matrix organization Source: UniProtKB
  22. positive regulation of JAK-STAT cascade Source: UniProtKB
  23. positive regulation vascular endothelial growth factor production Source: UniProtKB
  24. regulation of reactive oxygen species metabolic process Source: UniProtKB
  25. response to toxic substance Source: MGI
  26. retinal blood vessel morphogenesis Source: UniProtKB
  27. retinal metabolic process Source: UniProtKB
  28. retina vasculature development in camera-type eye Source: MGI
  29. retinol metabolic process Source: UniProtKB
  30. steroid metabolic process Source: UniProtKB
  31. toxin metabolic process Source: MGI
  32. trabecular meshwork development Source: UniProtKB
  33. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196570. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
REACT_196572. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_227038. Endogenous sterols.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 1B1 (EC:1.14.14.1)
Alternative name(s):
CYPIB1
Cytochrome P450CMEF
Short name:
Cytochrome P450EF
Gene namesi
Name:Cyp1b1
Synonyms:Cyp1-b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:88590. Cyp1b1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication. Microsome membrane 1 Publication; Peripheral membrane protein 1 Publication. Mitochondrion 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Severe ocular drainage structure abnormalities, significant elevated intraocular pressure.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Cytochrome P450 1B1PRO_0000051661Add
BLAST

Proteomic databases

MaxQBiQ64429.
PaxDbiQ64429.
PRIDEiQ64429.

PTM databases

PhosphoSiteiQ64429.

Expressioni

Tissue specificityi

Constitutively expressed in retinal, heart and kidney pericytes cells.1 Publication

Inductioni

By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).1 Publication

Gene expression databases

BgeeiQ64429.
ExpressionAtlasiQ64429. baseline and differential.
GenevestigatoriQ64429.

Structurei

3D structure databases

ProteinModelPortaliQ64429.
SMRiQ64429. Positions 68-530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118992.
HOGENOMiHOG000036991.
HOVERGENiHBG106944.
InParanoidiQ64429.
KOiK07410.
OMAiNEPSKMS.
OrthoDBiEOG7RBZ85.
TreeFamiTF105095.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64429-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSLSADSP QQLSSLSTQQ TTLLLLFSVL AAVHLGQWLL RQWQRKPWSS
60 70 80 90 100
PPGPFPWPLI GNAAAVGQAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE
110 120 130 140 150
SAIHQALVQQ GSIFADRPPF ASFRVVSGGR SLAFGHYSEH WKTQRRSAYS
160 170 180 190 200
TMRAFSTRHP RSRGLLEGHA LAEARELVAV LVRRCAGGAF LDPTQPVIVA
210 220 230 240 250
VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL VDVLPWLQLF
260 270 280 290 300
PNPVRTTFRK FEQLNRNFSN FVLDKFLRHR ESLVPGAAPR DMTDAFILSA
310 320 330 340 350
EKKASGAPGD DSSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP
360 370 380 390 400
DVQARVQAEL DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FSSFLPVTIP
410 420 430 440 450
HATTANTFVL GYYIPKNTVV FVNQWSVNHD PAKWPNPEDF DPARFLDKDG
460 470 480 490 500
FINKALASSV MIFSVGKRRC IGEELSKMLL FLFISILAHQ CNFKANQNES
510 520 530 540
SNMSFSYGLT IKPKSFRIHV SLRESMELLD NAVKKLQTEE GCK
Length:543
Mass (Da):60,537
Last modified:July 27, 2011 - v3
Checksum:i7C89B4312CB5BC4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951Q → P in CAA55205. (PubMed:8195121)Curated
Sequence conflicti307 – 3071A → D in CAA55205. (PubMed:8195121)Curated
Sequence conflicti328 – 3281F → G in CAA55205. (PubMed:8195121)Curated
Sequence conflicti457 – 4571A → T in CAA55205. (PubMed:8195121)Curated
Sequence conflicti516 – 5161F → V in CAA55205. (PubMed:8195121)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28986.1.
PIRiA53790.
RefSeqiNP_034124.1. NM_009994.1.
UniGeneiMm.214016.

Genome annotation databases

EnsembliENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
GeneIDi13078.
KEGGimmu:13078.
UCSCiuc008dqc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28986.1.
PIRi A53790.
RefSeqi NP_034124.1. NM_009994.1.
UniGenei Mm.214016.

3D structure databases

ProteinModelPortali Q64429.
SMRi Q64429. Positions 68-530.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q64429.

Proteomic databases

MaxQBi Q64429.
PaxDbi Q64429.
PRIDEi Q64429.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000024894 ; ENSMUSP00000024894 ; ENSMUSG00000024087 .
GeneIDi 13078.
KEGGi mmu:13078.
UCSCi uc008dqc.1. mouse.

Organism-specific databases

CTDi 1545.
MGIi MGI:88590. Cyp1b1.

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00760000118992.
HOGENOMi HOG000036991.
HOVERGENi HBG106944.
InParanoidi Q64429.
KOi K07410.
OMAi NEPSKMS.
OrthoDBi EOG7RBZ85.
TreeFami TF105095.

Enzyme and pathway databases

Reactomei REACT_196570. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
REACT_196572. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_227038. Endogenous sterols.

Miscellaneous databases

NextBioi 283028.
PROi Q64429.
SOURCEi Search...

Gene expression databases

Bgeei Q64429.
ExpressionAtlasi Q64429. baseline and differential.
Genevestigatori Q64429.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiCP1B1_MOUSE
AccessioniPrimary (citable) accession number: Q64429
Secondary accession number(s): Q3UVA8, Q60593, Q64461
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3