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Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1) (Cytochrome P450CMEF) (Cytochrome P450EF)

 CP1B1_MOUSE             Reviewed;         543 AA.
Q64429; Q3UVA8; Q60593; Q64461;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 144.
RecName: Full=Cytochrome P450 1B1;
EC=1.14.14.1;
AltName: Full=CYPIB1;
AltName: Full=Cytochrome P450CMEF;
Short=Cytochrome P450EF;
Name=Cyp1b1; Synonyms=Cyp1-b1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=7772257; DOI=10.1089/dna.1994.13.763;
Shen Z., Liu J., Wells R.L., Elkind M.M.;
"cDNA cloning, sequence analysis, and induction by aryl hydrocarbons
of a murine cytochrome P450 gene, Cyp1b1.";
DNA Cell Biol. 13:763-769(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=8195121;
Savas U., Bhattacharyya K.K., Christou M., Alexander D.L.,
Jefcoate C.R.;
"Mouse cytochrome P-450EF, representative of a new 1B subfamily of
cytochrome P-450s. Cloning, sequence determination, and tissue
expression.";
J. Biol. Chem. 269:14905-14911(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 361-466.
PubMed=7505439; DOI=10.1073/pnas.90.24.11483;
Shen Z., Wells R.L., Liu J., Elkind M.M.;
"Identification of a cytochrome P450 gene by reverse transcription-PCR
using degenerate primers containing inosine.";
Proc. Natl. Acad. Sci. U.S.A. 90:11483-11487(1993).
[6]
ENZYME REGULATION.
PubMed=10037446; DOI=10.1016/S0006-2952(98)00344-X;
Ikegwuonu F.I., Christou M., Jefcoate C.R.;
"Regulation of cytochrome P4501B1 (CYP1B1) in mouse embryo fibroblast
(C3H10T1/2) cells by protein kinase C (PKC).";
Biochem. Pharmacol. 57:619-630(1999).
[7]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15258110; DOI=10.1124/dmd.32.8.840;
Choudhary D., Jansson I., Stoilov I., Sarfarazi M., Schenkman J.B.;
"Metabolism of retinoids and arachidonic acid by human and mouse
cytochrome P450 1b1.";
Drug Metab. Dispos. 32:840-847(2004).
[8]
FUNCTION IN VASCULAR DEVELOPMENT AND ANGIOGENESIS.
PubMed=19005183; DOI=10.1182/blood-2008-03-145219;
Tang Y., Scheef E.A., Wang S., Sorenson C.M., Marcus C.B.,
Jefcoate C.R., Sheibani N.;
"CYP1B1 expression promotes the proangiogenic phenotype of endothelium
through decreased intracellular oxidative stress and thrombospondin-2
expression.";
Blood 113:744-754(2009).
[9]
FUNCTION IN ANGIOGENESIS.
PubMed=20032512; DOI=10.1152/ajpcell.00153.2009;
Tang Y., Scheef E.A., Gurel Z., Sorenson C.M., Jefcoate C.R.,
Sheibani N.;
"CYP1B1 and endothelial nitric oxide synthase combine to sustain
proangiogenic functions of endothelial cells under hyperoxic stress.";
Am. J. Physiol. 298:C665-C678(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
SUBCELLULAR LOCATION.
PubMed=23692925; DOI=10.1016/j.bbrc.2013.05.051;
Dong H., Shertzer H.G., Genter M.B., Gonzalez F.J., Vasiliou V.,
Jefcoate C., Nebert D.W.;
"Mitochondrial targeting of mouse NQO1 and CYP1B1 proteins.";
Biochem. Biophys. Res. Commun. 435:727-732(2013).
[12]
FUNCTION IN VASCULAR HOMEOSTASIS, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=23568032; DOI=10.1038/labinvest.2013.55;
Palenski T.L., Sorenson C.M., Jefcoate C.R., Sheibani N.;
"Lack of Cyp1b1 promotes the proliferative and migratory phenotype of
perivascular supporting cells.";
Lab. Invest. 93:646-662(2013).
[13]
FUNCTION IN TRABECULAR MESHWORK DEVELOPMENT, AND DISRUPTION PHENOTYPE.
PubMed=23979599; DOI=10.1128/MCB.00856-13;
Zhao Y., Wang S., Sorenson C.M., Teixeira L., Dubielzig R.R.,
Peters D.M., Conway S.J., Jefcoate C.R., Sheibani N.;
"Cyp1b1 mediates periostin regulation of trabecular meshwork
development by suppression of oxidative stress.";
Mol. Cell. Biol. 33:4225-4240(2013).
[14]
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:15258110, ECO:0000269|PubMed:19005183,
ECO:0000269|PubMed:20032512, ECO:0000269|PubMed:23568032,
ECO:0000269|PubMed:23821647, ECO:0000269|PubMed:23979599}.
-!- 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};
-!- ENZYME REGULATION: Activated by 2,3,7,8-tetrachlorodibenzo-p-
dioxin (TCDD). Inhibited by 12-O-Tetradecanoylphorbol-13-acetate
and PRKCB. {ECO:0000269|PubMed:10037446}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=392.2 uM for retinol {ECO:0000269|PubMed:15258110};
KM=153.9 uM for retinal {ECO:0000269|PubMed:15258110};
KM=138.9 uM for 7,12-dimethyltetraphene
{ECO:0000269|PubMed:15258110};
KM=500.0 uM for arachidonic acid {ECO:0000269|PubMed:15258110};
Note=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.;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:23692925}; Peripheral membrane protein
{ECO:0000269|PubMed:23692925}. Microsome membrane
{ECO:0000269|PubMed:23692925}; Peripheral membrane protein
{ECO:0000269|PubMed:23692925}. Mitochondrion
{ECO:0000269|PubMed:23692925}.
-!- TISSUE SPECIFICITY: Constitutively expressed in retinal, heart and
kidney pericytes cells. {ECO:0000269|PubMed:23568032}.
-!- INDUCTION: By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-
tetrachlorodibenzo-p-dioxin (TCDD). {ECO:0000269|PubMed:23568032}.
-!- DISRUPTION PHENOTYPE: Severe ocular drainage structure
abnormalities, significant elevated intraocular pressure.
{ECO:0000269|PubMed:23979599}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; U03283; AAC52141.1; -; mRNA.
EMBL; X78445; CAA55205.1; -; mRNA.
EMBL; AK137461; BAE23362.1; -; mRNA.
EMBL; CH466537; EDL38490.1; -; Genomic_DNA.
EMBL; U02479; AAC52131.1; -; mRNA.
CCDS; CCDS28986.1; -.
PIR; A53790; A53790.
RefSeq; NP_034124.1; NM_009994.1.
UniGene; Mm.214016; -.
ProteinModelPortal; Q64429; -.
SMR; Q64429; -.
STRING; 10090.ENSMUSP00000024894; -.
iPTMnet; Q64429; -.
PhosphoSitePlus; Q64429; -.
MaxQB; Q64429; -.
PaxDb; Q64429; -.
PRIDE; Q64429; -.
Ensembl; ENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
GeneID; 13078; -.
KEGG; mmu:13078; -.
UCSC; uc008dqc.1; mouse.
CTD; 1545; -.
MGI; MGI:88590; Cyp1b1.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140831; -.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; Q64429; -.
KO; K07410; -.
OMA; AVCFGCR; -.
OrthoDB; EOG091G0BT8; -.
TreeFam; TF105095; -.
Reactome; R-MMU-211976; Endogenous sterols.
Reactome; R-MMU-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
Reactome; R-MMU-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
SABIO-RK; Q64429; -.
PRO; PR:Q64429; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024087; -.
Genevisible; Q64429; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
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:0016712; F: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; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
GO; GO:0006725; P:cellular aromatic compound metabolic process; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
GO; GO:0071603; P:endothelial cell-cell adhesion; IMP:MGI.
GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:UniProtKB.
GO; GO:0046466; P:membrane lipid catabolic process; IMP:UniProtKB.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IMP:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:UniProtKB.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IMP:MGI.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:MGI.
GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:UniProtKB.
GO; GO:0042574; P:retinal metabolic process; IDA:UniProtKB.
GO; GO:0042572; P:retinol metabolic process; IDA:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; ISS:UniProtKB.
GO; GO:0009404; P:toxin metabolic process; IMP:MGI.
GO; GO:0002930; P:trabecular meshwork development; IMP:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR032971; CYP1B1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
PANTHER; PTHR24299:SF2; PTHR24299:SF2; 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; Endoplasmic reticulum; Heme; Iron; Membrane;
Metal-binding; Microsome; Mitochondrion; Monooxygenase;
Oxidoreductase; Reference proteome.
CHAIN 1 543 Cytochrome P450 1B1.
/FTId=PRO_0000051661.
METAL 470 470 Iron (heme axial ligand). {ECO:0000250}.
CONFLICT 195 195 Q -> P (in Ref. 2; CAA55205).
{ECO:0000305}.
CONFLICT 307 307 A -> D (in Ref. 2; CAA55205).
{ECO:0000305}.
CONFLICT 328 328 F -> G (in Ref. 2; CAA55205).
{ECO:0000305}.
CONFLICT 457 457 A -> T (in Ref. 2; CAA55205).
{ECO:0000305}.
CONFLICT 516 516 F -> V (in Ref. 2; CAA55205).
{ECO:0000305}.
SEQUENCE 543 AA; 60537 MW; 7C89B4312CB5BC4A CRC64;
MATSLSADSP QQLSSLSTQQ TTLLLLFSVL AAVHLGQWLL RQWQRKPWSS PPGPFPWPLI
GNAAAVGQAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE SAIHQALVQQ GSIFADRPPF
ASFRVVSGGR SLAFGHYSEH WKTQRRSAYS TMRAFSTRHP RSRGLLEGHA LAEARELVAV
LVRRCAGGAF LDPTQPVIVA VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL
VDVLPWLQLF PNPVRTTFRK FEQLNRNFSN FVLDKFLRHR ESLVPGAAPR DMTDAFILSA
EKKASGAPGD DSSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP DVQARVQAEL
DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FSSFLPVTIP HATTANTFVL GYYIPKNTVV
FVNQWSVNHD PAKWPNPEDF DPARFLDKDG FINKALASSV MIFSVGKRRC IGEELSKMLL
FLFISILAHQ CNFKANQNES SNMSFSYGLT IKPKSFRIHV SLRESMELLD NAVKKLQTEE
GCK


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U1557p CLIA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
U1557r CLIA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557r ELISA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557r ELISA kit 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557p ELISA kit 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
EIAAB08924 Cyp2c13,Cyp2c-13,CYPIIC13,Cytochrome P450 2C13, male-specific,Cytochrome P-450g,Cytochrome P450-G,Cytochrome P450-UT-5,Rat,Rattus norvegicus
E1557b ELISA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T


 

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