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Showing Protein Cytochrome P450 1B1 (HMDBP13436)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP13436
Secondary Accession Numbers None
Name Cytochrome P450 1B1
Synonyms
  1. CYPIB1
  2. Cytochrome P450CMEF
  3. Hydroperoxy icosatetraenoate dehydratase
  4. Cytochrome P450EF
Gene Name CYP1B1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (By similarity). Exhibits catalytic activity for the formation of hydroxyestrogens from 17beta-estradiol (E2), namely 2- and 4-hydroxy E2 (PubMed:23821647). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (By similarity). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:15258110). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:15258110). Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (By similarity). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (By similarity). Plays an important role in retinal vascular development. Under ambient/hyperoxic O2 conditions, promotes angiogenesis and capillary morphogenesis of retinal endothelial cells and pericytes, likely by metabolizing the oxygenated products symptomatic of oxidative stress (PubMed:19005183, PubMed:20032512, PubMed:23568032). Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (PubMed:23979599).
Pathways
  • arachidonate metabolism
  • Chemical carcinogenesis - DNA adducts
  • Chemical carcinogenesis - reactive oxygen species
  • Chemical carcinogenesis - receptor activation
  • Metabolism of xenobiotics by cytochrome P450
  • MicroRNAs in cancer
  • Ovarian steroidogenesis
  • retinol metabolism
  • Steroid hormone biosynthesis
  • Tryptophan metabolism
Reactions Not Available
GO Classification
Biological Process
positive regulation of translation
toxin metabolic process
collagen fibril organization
positive regulation of angiogenesis
estrogen metabolic process
endothelial cell migration
endothelial cell-cell adhesion
retina vasculature development in camera-type eye
arachidonic acid metabolic process
intrinsic apoptotic signaling pathway in response to oxidative stress
positive regulation vascular endothelial growth factor production
regulation of reactive oxygen species metabolic process
cellular response to organic cyclic compound
DNA modification
positive regulation of DNA biosynthetic process
positive regulation of smooth muscle cell migration
benzene-containing compound metabolic process
blood vessel morphogenesis
membrane lipid catabolic process
positive regulation of receptor signaling pathway via JAK-STAT
retinal blood vessel morphogenesis
trabecular meshwork development
cellular response to hydrogen peroxide
negative regulation of cell migration
positive regulation of reactive oxygen species metabolic process
negative regulation of cell adhesion mediated by integrin
cell adhesion
xenobiotic metabolic process
positive regulation of apoptotic process
retinol metabolic process
steroid metabolic process
retinal metabolic process
negative regulation of cell proliferation
angiogenesis
cellular aromatic compound metabolic process
nitric oxide biosynthetic process
negative regulation of NF-kappaB transcription factor activity
response to toxin
Cellular Component
mitochondrion
intracellular membrane-bounded organelle
nucleus
endoplasmic reticulum membrane
Molecular Function
hydroperoxy icosatetraenoate dehydratase activity
estrogen 16-alpha-hydroxylase activity
heme binding
iron ion binding
monooxygenase activity
aromatase activity
oxidoreductase activity
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
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 543
Molecular Weight 60536.73
Theoretical pI 8.429
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q64429
UniProtKB/Swiss-Prot Entry Name CP1B1_MOUSE
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, 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 SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, 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 KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, 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 SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, 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: The transcriptional landscape of the mammalian genome. Science. 2005 Sep 2;309(5740):1559-63. [PubMed:16141072 ]
  2. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  3. Nishida CR, Everett S, Ortiz de Montellano PR: Specificity determinants of CYP1B1 estradiol hydroxylation. Mol Pharmacol. 2013 Sep;84(3):451-8. doi: 10.1124/mol.113.087700. Epub 2013 Jul 2. [PubMed:23821647 ]
  4. Shen Z, Liu J, Wells RL, Elkind MM: cDNA cloning, sequence analysis, and induction by aryl hydrocarbons of a murine cytochrome P450 gene, Cyp1b1. DNA Cell Biol. 1994 Jul;13(7):763-9. doi: 10.1089/dna.1994.13.763. [PubMed:7772257 ]
  5. Savas U, Bhattacharyya KK, Christou M, Alexander DL, Jefcoate CR: Mouse cytochrome P-450EF, representative of a new 1B subfamily of cytochrome P-450s. Cloning, sequence determination, and tissue expression. J Biol Chem. 1994 May 27;269(21):14905-11. [PubMed:8195121 ]
  6. Shen Z, Wells RL, Liu J, Elkind MM: Identification of a cytochrome P450 gene by reverse transcription--PCR using degenerate primers containing inosine. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11483-7. doi: 10.1073/pnas.90.24.11483. [PubMed:7505439 ]
  7. Choudhary D, Jansson I, Stoilov I, Sarfarazi M, Schenkman JB: Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1. Drug Metab Dispos. 2004 Aug;32(8):840-7. doi: 10.1124/dmd.32.8.840. [PubMed:15258110 ]
  8. Tang Y, Scheef EA, Wang S, Sorenson CM, Marcus CB, Jefcoate CR, Sheibani N: CYP1B1 expression promotes the proangiogenic phenotype of endothelium through decreased intracellular oxidative stress and thrombospondin-2 expression. Blood. 2009 Jan 15;113(3):744-54. doi: 10.1182/blood-2008-03-145219. Epub 2008 Nov 12. [PubMed:19005183 ]
  9. Tang Y, Scheef EA, Gurel Z, Sorenson CM, Jefcoate CR, Sheibani N: CYP1B1 and endothelial nitric oxide synthase combine to sustain proangiogenic functions of endothelial cells under hyperoxic stress. Am J Physiol Cell Physiol. 2010 Mar;298(3):C665-78. doi: 10.1152/ajpcell.00153.2009. Epub 2009 Dec 23. [PubMed:20032512 ]
  10. Dong H, Shertzer HG, Genter MB, Gonzalez FJ, Vasiliou V, Jefcoate C, Nebert DW: Mitochondrial targeting of mouse NQO1 and CYP1B1 proteins. Biochem Biophys Res Commun. 2013 Jun 14;435(4):727-32. doi: 10.1016/j.bbrc.2013.05.051. Epub 2013 May 18. [PubMed:23692925 ]
  11. Zhao Y, Wang S, Sorenson CM, Teixeira L, Dubielzig RR, Peters DM, Conway SJ, Jefcoate CR, Sheibani N: Cyp1b1 mediates periostin regulation of trabecular meshwork development by suppression of oxidative stress. Mol Cell Biol. 2013 Nov;33(21):4225-40. doi: 10.1128/MCB.00856-13. Epub 2013 Aug 26. [PubMed:23979599 ]