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Showing Protein Cytochrome P450 1B1 (HMDBP13435)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP13435
Secondary Accession Numbers None
Name Cytochrome P450 1B1
Synonyms
  1. CYPIB1
  2. Cytochrome P450RAP
  3. Hydroperoxy icosatetraenoate dehydratase
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 (By similarity). 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:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids including 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 (By similarity). Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity).
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
DNA modification
cellular response to tumor necrosis factor
collagen fibril organization
response to steroid hormone stimulus
positive regulation of angiogenesis
estrogen metabolic process
adrenal gland development
endothelial cell migration
endothelial cell-cell adhesion
retina vasculature development in camera-type eye
arachidonic acid metabolic process
response to dexamethasone stimulus
intrinsic apoptotic signaling pathway in response to oxidative stress
positive regulation vascular endothelial growth factor production
positive regulation of translation
cellular response to organic cyclic compound
regulation of reactive oxygen species metabolic process
positive regulation of DNA biosynthetic process
positive regulation of smooth muscle cell migration
estrous cycle
benzene-containing compound metabolic process
blood vessel morphogenesis
cellular response to cortisol stimulus
cellular response to luteinizing hormone stimulus
cellular response to progesterone stimulus
ganglion development
membrane lipid catabolic process
positive regulation of receptor signaling pathway via JAK-STAT
response to indole-3-methanol
retinal blood vessel morphogenesis
trabecular meshwork development
response to follicle-stimulating hormone stimulus
response to nutrient
negative regulation of cell migration
response to organic cyclic compound
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
male gonad development
negative regulation of cell proliferation
response to estradiol stimulus
response to organic substance
angiogenesis
cellular aromatic compound metabolic process
negative regulation of NF-kappaB transcription factor activity
response to toxin
cellular response to cAMP
toxin metabolic process
response to arsenic-containing substance
cellular response to hydrogen peroxide
nitric oxide biosynthetic process
Cellular Component
mitochondrion
nucleus
endoplasmic reticulum membrane
intracellular membrane-bounded organelle
Molecular Function
iron ion binding
estrogen 16-alpha-hydroxylase activity
hydroperoxy icosatetraenoate dehydratase activity
heme binding
aromatase activity
monooxygenase 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 60555.93
Theoretical pI 8.369
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q64678
UniProtKB/Swiss-Prot Entry Name CP1B1_RAT
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. Bhattacharyya KK, Brake PB, Eltom SE, Otto SA, Jefcoate CR: Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation. J Biol Chem. 1995 May 12;270(19):11595-602. doi: 10.1074/jbc.270.19.11595. [PubMed:7744798 ]
  2. Walker NJ, Gastel JA, Costa LT, Clark GC, Lucier GW, Sutter TR: Rat CYP1B1: an adrenal cytochrome P450 that exhibits sex-dependent expression in livers and kidneys of TCDD-treated animals. Carcinogenesis. 1995 Jun;16(6):1319-27. doi: 10.1093/carcin/16.6.1319. [PubMed:7788849 ]
  3. Mesaros C, Lee SH, Blair IA: Analysis of epoxyeicosatrienoic acids by chiral liquid chromatography/electron capture atmospheric pressure chemical ionization mass spectrometry using [13C]-analog internal standards. Rapid Commun Mass Spectrom. 2010 Nov 30;24(22):3237-47. doi: 10.1002/rcm.4760. [PubMed:20972997 ]
  4. Jacob A, Hartz AM, Potin S, Coumoul X, Yousif S, Scherrmann JM, Bauer B, Decleves X: Aryl hydrocarbon receptor-dependent upregulation of Cyp1b1 by TCDD and diesel exhaust particles in rat brain microvessels. Fluids Barriers CNS. 2011 Aug 25;8:23. doi: 10.1186/2045-8118-8-23. [PubMed:21867498 ]
  5. Deb S, Tai JK, Leung GS, Chang TK, Bandiera SM: Estradiol-mediated suppression of CYP1B1 expression in mouse MA-10 Leydig cells is independent of protein kinase A and estrogen receptor. Mol Cell Biochem. 2011 Dec;358(1-2):387-95. doi: 10.1007/s11010-011-0994-z. Epub 2011 Jul 23. [PubMed:21785971 ]
  6. Brauze D, Rawluszko AA: The effect of aryl hydrocarbon receptor ligands on the expression of polymerase (DNA directed) kappa (Polkappa), polymerase RNA II (DNA directed) polypeptide A (PolR2a), CYP1B1 and CYP1A1 genes in rat liver. Environ Toxicol Pharmacol. 2012 Nov;34(3):819-25. doi: 10.1016/j.etap.2012.09.004. Epub 2012 Sep 16. [PubMed:23026235 ]
  7. 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 ]