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Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1) (Cytochrome P450RAP)

 CP1B1_RAT               Reviewed;         543 AA.
Q64678;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 132.
RecName: Full=Cytochrome P450 1B1;
EC=1.14.14.1;
AltName: Full=CYPIB1;
AltName: Full=Cytochrome P450RAP;
Name=Cyp1b1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley;
PubMed=7744798; DOI=10.1074/jbc.270.19.11595;
Bhattacharyya K.K., Brake P.B., Eltom S.E., Otto S.A., Jefcoate C.R.;
"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. 270:11595-11602(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7788849; DOI=10.1093/carcin/16.6.1319;
Walker N.J., Gastel J.A., Costa L.T., Clark G.C., Lucier G.W.,
Sutter T.R.;
"Rat CYP1B1: an adrenal cytochrome P450 that exhibits sex-dependent
expression in livers and kidneys of TCDD-treated animals.";
Carcinogenesis 16:1319-1327(1995).
[3]
INDUCTION.
PubMed=21867498; DOI=10.1186/2045-8118-8-23;
Jacob A., Hartz A.M., Potin S., Coumoul X., Yousif S.,
Scherrmann J.M., Bauer B., Decleves X.;
"Aryl hydrocarbon receptor-dependent upregulation of Cyp1b1 by TCDD
and diesel exhaust particles in rat brain microvessels.";
Fluids Barriers CNS 8:23-23(2011).
[4]
INDUCTION.
PubMed=21785971; DOI=10.1007/s11010-011-0994-z;
Deb S., Tai J.K., Leung G.S., Chang T.K., Bandiera S.M.;
"Estradiol-mediated suppression of CYP1B1 expression in mouse MA-10
Leydig cells is independent of protein kinase A and estrogen
receptor.";
Mol. Cell. Biochem. 358:387-395(2011).
[5]
INDUCTION.
PubMed=23026235; DOI=10.1016/j.etap.2012.09.004;
Brauze D., Rawluszko A.A.;
"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. 34:819-825(2012).
[6]
MUTAGENESIS OF LEU-395, AND FUNCTION IN ESTROGEN METABOLISM.
PubMed=23821647; DOI=10.1124/mol.113.087700;
Nishida C.R., Everett S., Ortiz de Montellano P.R.;
"Specificity determinants of CYP1B1 estradiol hydroxylation.";
Mol. Pharmacol. 84:451-458(2013).
-!- 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.
{ECO:0000269|PubMed:23821647}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
Mitochondrion {ECO:0000250}.
-!- INDUCTION: By polycyclic aromatic hydrocarbons (PAH), beta-
naphthoflavone and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Up-
regulated by diesel exhaust particles (DEP). Decreased by
estradiol (at protein level). {ECO:0000269|PubMed:21785971,
ECO:0000269|PubMed:21867498, ECO:0000269|PubMed:23026235}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X83867; CAA58748.1; -; mRNA.
EMBL; U09540; AAA79864.1; -; mRNA.
PIR; I48130; I48130.
RefSeq; NP_037072.1; NM_012940.2.
UniGene; Rn.10125; -.
ProteinModelPortal; Q64678; -.
SMR; Q64678; -.
STRING; 10116.ENSRNOP00000061222; -.
SwissLipids; SLP:000001591; -.
iPTMnet; Q64678; -.
PhosphoSitePlus; Q64678; -.
PaxDb; Q64678; -.
PRIDE; Q64678; -.
GeneID; 25426; -.
KEGG; rno:25426; -.
UCSC; RGD:2460; rat.
CTD; 1545; -.
RGD; 2460; Cyp1b1.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; Q64678; -.
KO; K07410; -.
PhylomeDB; Q64678; -.
PRO; PR:Q64678; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IDA:RGD.
GO; GO:0030325; P:adrenal gland development; IEP:RGD.
GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
GO; GO:0042537; P:benzene-containing compound metabolic process; IDA:RGD.
GO; GO:0048514; P:blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0006725; P:cellular aromatic compound metabolic process; IDA:RGD.
GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
GO; GO:0071387; P:cellular response to cortisol stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IEP:RGD.
GO; GO:0071393; P:cellular response to progesterone stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
GO; GO:0006304; P:DNA modification; IMP:RGD.
GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IDA:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0061548; P:ganglion development; IEP:RGD.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0046466; P:membrane lipid catabolic process; ISS:UniProtKB.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0006809; P:nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEP:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:RGD.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0032354; P:response to follicle-stimulating hormone; IEP:RGD.
GO; GO:0071680; P:response to indole-3-methanol; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0061304; P:retinal blood vessel morphogenesis; ISS:UniProtKB.
GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB.
GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
GO; GO:0002930; P:trabecular meshwork development; ISS:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
InterPro; IPR032971; CYP1B1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
PANTHER; PTHR24299:SF16; PTHR24299:SF16; 1.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Heme; Iron; Membrane; Metal-binding; Microsome; Mitochondrion;
Monooxygenase; Oxidoreductase; Reference proteome.
CHAIN 1 543 Cytochrome P450 1B1.
/FTId=PRO_0000051662.
METAL 470 470 Iron (heme axial ligand). {ECO:0000250}.
SITE 395 395 Major determinant of CYP1B1 17beta-
estradiol hydroxylation regiospecificity.
MUTAGEN 395 395 L->V: Shifts the 4OH E2:2OH E2
hydroxylation ratio from 0.38 to 1.8. Has
the 4OH-hydroxylation specificity of the
human enzyme.
{ECO:0000269|PubMed:23821647}.
SEQUENCE 543 AA; 60557 MW; 8D144B0000D5F095 CRC64;
MATSLSADSP QQLSSLSTQQ TILLLLVSVL AIVHLGQWLL RQWRRKPWSS PPGPFPWPLI
GNAASVGRAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE SAIHQALVQQ GGVFADRPPF
ASFRVVSGGR SLAFGHYSER WKERRRAAYG TMRAFSTRHP RSRGLLEGHA LGEARELVAV
LVRRCAGGAC LDPTQPIIVA VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL
VDVMPWLQLF PNPVRTIFRE FEQINRNFSN FVLDKFLRHR ESLVPGAAPR DMMDAFILSA
EKKATGDPGD SPSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP DVQARVQAEL
DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FTSFLPVTLP HATTANTFVL GYYIPKNTVV
FVNQWSVNHD PAKWSNPEDF DPARFLDKDG FINKALASSV MIFSVGKRRC IGEELSKTLL
FLFISILAHQ CNFKANQNEP SNMSFSYGLS IKPKSFKIHV SLRESMKLLD SAVEKLQAEE
ACQ


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