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Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1)

 CP1B1_HUMAN             Reviewed;         543 AA.
Q16678; Q5TZW8; Q93089; Q9H316;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
25-OCT-2017, entry version 200.
RecName: Full=Cytochrome P450 1B1;
EC=1.14.14.1 {ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:22888116};
AltName: Full=CYPIB1;
Name=CYP1B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
PubMed=8175734;
Sutter T.R., Tang Y.M., Hayes C.L., Wo Y.-Y.P., Jabs E.W., Li X.,
Yin H., Cody C.W., Greenlee W.F.;
"Complete cDNA sequence of a human dioxin-inducible mRNA identifies a
new gene subfamily of cytochrome P450 that maps to chromosome 2.";
J. Biol. Chem. 269:13092-13099(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8910454; DOI=10.1074/jbc.271.45.28324;
Tang Y.M., Wo Y.-Y.P., Stewart J., Hawkins A.L., Griffin C.A.,
Sutter T.R., Greenlee W.F.;
"Isolation and characterization of the human cytochrome P450 CYP1B1
gene.";
J. Biol. Chem. 271:28324-28330(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Gorry M.C., Zhang Y., Marks J.J., Suppe B., Hart P.S., Cortelli J.R.,
Pallos D., Hart T.C.;
"Physical/genetic map of the 2p22-2p21 region on chromosome 2.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-453.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-48; SER-119;
ASN-206; LEU-266; VAL-432 AND SER-453.
NIEHS SNPs program;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, AND VARIANT GLY-48.
Guillemette C.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
CHARACTERIZATION OF VARIANTS SER-119 AND VAL-432.
PubMed=10426814; DOI=10.1093/carcin/20.8.1607;
Shimada T., Watanabe J., Kawajiri K., Sutter T.R., Guengerich F.P.,
Gillam E.M.J., Inoue K.;
"Catalytic properties of polymorphic human cytochrome P450 1B1
variants.";
Carcinogenesis 20:1607-1613(1999).
[9]
INVOLVEMENT IN ASGD6.
PubMed=11403040; DOI=10.1136/jmg.38.5.324;
Vincent A., Billingsley G., Priston M., Williams-Lyn D.,
Sutherland J., Glaser T., Oliver E., Walter M.A., Heathcote G.,
Levin A., Heon E.;
"Phenotypic heterogeneity of CYP1B1: mutations in a patient with
Peters' anomaly.";
J. Med. Genet. 38:324-326(2001).
[10]
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).
[11]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND FUNCTION.
PubMed=22888116; DOI=10.1093/jb/mvs087;
Jang H.H., Kim S.Y., Kang J.Y., Park S.H., Ryu S.H., Ahn T., Yun C.H.;
"Increase of human CYP1B1 activities by acidic phospholipids and
kinetic deuterium isotope effects on CYP1B1 substrate oxidation.";
J. Biochem. 152:433-442(2012).
[12]
MUTAGENESIS OF VAL-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).
[13]
ENZYME REGULATION.
PubMed=22935222; DOI=10.1017/S0007114512003595;
Poon C.H., Wong T.Y., Wang Y., Tsuchiya Y., Nakajima M., Yokoi T.,
Leung L.K.;
"The citrus flavanone naringenin suppresses CYP1B1 transactivation
through antagonising xenobiotic-responsive element binding.";
Br. J. Nutr. 109:1598-1605(2013).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 51-543 IN COMPLEX WITH HEME
AND THE INHIBITOR ALPHA-NAPHTOFLAVONE, AND COFACTOR.
PubMed=21147782; DOI=10.1074/jbc.M110.204420;
Wang A., Savas U., Stout C.D., Johnson E.F.;
"Structural characterization of the complex between alpha-
naphthoflavone and human cytochrome P450 1B1.";
J. Biol. Chem. 286:5736-5743(2011).
[15]
VARIANTS GLC3A GLU-61; ASN-374 AND TRP-469.
PubMed=9463332; DOI=10.1086/301725;
Bejjani B.A., Lewis R.A., Tomey K.F., Anderson K.L., Dueker D.K.,
Jabak M., Astle W.F., Otterud B., Leppert M., Lupski J.R.;
"Mutations in CYP1B1, the gene for cytochrome P4501B1, are the
predominant cause of primary congenital glaucoma in Saudi Arabia.";
Am. J. Hum. Genet. 62:325-333(1998).
[16]
VARIANT GLC3A TRP-365, AND VARIANTS CYS-57; GLU-61; TRP-365; LEU-379;
LYS-387; HIS-390; VAL-432; LEU-437 AND TRP-469.
PubMed=9497261; DOI=10.1086/301764;
Stoilov I., Akarsu A.N., Alozie I., Child A., Barsoum-Homsy M.,
Turacli M.E., Or M., Lewis R.A., Ozdemir N., Brice G., Aktan S.G.,
Chevrette L., Coca-Prados M., Sarfarazi M.;
"Sequence analysis and homology modeling suggest that primary
congenital glaucoma on 2p21 results from mutations disrupting either
the hinge region or the conserved core structures of cytochrome
P4501B1.";
Am. J. Hum. Genet. 62:573-584(1998).
[17]
VARIANTS VAL-432 AND SER-453.
PubMed=9823305;
Bailey L.R., Roodi N., Dupont W.D., Parl F.F.;
"Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid
receptor status in breast cancer.";
Cancer Res. 58:5038-5041(1998).
[18]
ERRATUM.
Bailey L.R., Roodi N., Dupont W.D., Parl F.F.;
Cancer Res. 59:1388-1388(1999).
[19]
VARIANT GLC3A LYS-387.
PubMed=10227395;
Plasilova M., Stoilov I., Sarfarazi M., Kadasi L., Ferakova E.,
Ferak V.;
"Identification of a single ancestral CYP1B1 mutation in Slovak
Gypsies (Roms) affected with primary congenital glaucoma.";
J. Med. Genet. 36:290-294(1999).
[20]
VARIANTS GLC3A GLU-61; PRO-77; 269-SER--PHE-271 DEL; HIS-368; ASN-374;
SER-390 AND TRP-469, AND VARIANTS GLY-48; SER-119; VAL-432 AND
SER-453.
PubMed=10655546; DOI=10.1093/hmg/9.3.367;
Bejjani B.A., Stockton D.W., Lewis R.A., Tomey K.F., Dueker D.K.,
Jabak M., Astle W.F., Lupski J.R.;
"Multiple CYP1B1 mutations and incomplete penetrance in an inbred
population segregating primary congenital glaucoma suggest frequent de
novo events and a dominant modifier locus.";
Hum. Mol. Genet. 9:367-374(2000).
[21]
ERRATUM.
Bejjani B.A., Stockton D.W., Lewis R.A., Tomey K.F., Dueker D.K.,
Jabak M., Astle W.F., Lupski J.R.;
Hum. Mol. Genet. 9:1141-1141(2000).
[22]
VARIANT GLC3A MET-364.
PubMed=11184479; DOI=10.1076/1381-6810(200009)2131-ZFT191;
Ohtake Y., Kubota R., Tanino T., Miyata H., Mashima Y.;
"Novel compound heterozygous mutations in the cytochrome P4501B1 gene
(CYP1B1) in a Japanese patient with primary congenital glaucoma.";
Ophthalmic Genet. 21:191-193(2000).
[23]
VARIANTS SER-119 AND VAL-432, AND ASSOCIATION WITH BREAST OR LUNG
CANCER.
PubMed=10739169; DOI=10.1097/00008571-200002000-00004;
Watanabe J., Shimada T., Gillam E.M., Ikuta T., Suemasu K.,
Higashi Y., Gotoh O., Kawajiri K.;
"Association of CYP1B1 genetic polymorphism with incidence to breast
and lung cancer.";
Pharmacogenetics 10:25-33(2000).
[24]
VARIANTS GLC3A VAL-192; ILE-198; LEU-320; PHE-330; MET-364; GLN-444
AND GLY-499, AND VARIANTS GLY-48; SER-119 AND VAL-432.
PubMed=11527932;
Mashima Y., Suzuki Y., Sergeev Y., Ohtake Y., Tanino T., Kimura I.,
Miyata H., Aihara M., Tanihara H., Inatani M., Azuma N., Iwata T.,
Araie M.;
"Novel cytochrome P4501B1 (CYP1B1) gene mutations in Japanese patients
with primary congenital glaucoma.";
Invest. Ophthalmol. Vis. Sci. 42:2211-2216(2001).
[25]
ERRATUM.
Mashima Y., Suzuki Y., Sergeev Y., Ohtake Y., Tanino T., Kimura I.,
Miyata H., Aihara M., Tanihara H., Inatani M., Azuma N., Iwata T.,
Araie M.;
Invest. Ophthalmol. Vis. Sci. 42:2775-2775(2001).
[26]
VARIANT POAG PHE-345, VARIANT GLC1A HIS-368, AND VARIANT VAL-432.
PubMed=11774072; DOI=10.1086/338709;
Vincent A.L., Billingsley G., Buys Y., Levin A.V., Priston M.,
Trope G., Williams-Lyn D., Heon E.;
"Digenic inheritance of early-onset glaucoma: CYP1B1, a potential
modifier gene.";
Am. J. Hum. Genet. 70:448-460(2002).
[27]
VARIANTS GLC3A GLU-61; LEU-193; LYS-229 AND HIS-368, AND VARIANTS
GLY-48; SER-184 AND VAL-432.
PubMed=11980847;
Panicker S.G., Reddy A.B.M., Mandal A.K., Ahmed N., Nagarajaram H.A.,
Hasnain S.E., Balasubramanian D.;
"Identification of novel mutations causing familial primary congenital
glaucoma in Indian pedigrees.";
Invest. Ophthalmol. Vis. Sci. 43:1358-1366(2002).
[28]
VARIANTS GLC3A HIS-368; LYS-387; LEU-437 AND GLY-443, AND VARIANTS
GLY-48; SER-119; VAL-432 AND SER-453.
PubMed=12036985;
Stoilov I.R., Costa V.P., Vasconcellos J.P.C., Melo M.B.,
Betinjane A.J., Carani J.C.E., Oltrogge E.V., Sarfarazi M.;
"Molecular genetics of primary congenital glaucoma in Brazil.";
Invest. Ophthalmol. Vis. Sci. 43:1820-1827(2002).
[29]
VARIANTS GLY-48; SER-119; VAL-432; GLY-443 AND SER-453.
PubMed=11854439; DOI=10.1124/mol.61.3.586;
Aklillu E., Oscarson M., Hidestrand M., Leidvik B., Otter C.,
Ingelman-Sundberg M.;
"Functional analysis of six different polymorphic CYP1B1 enzyme
variants found in an Ethiopian population.";
Mol. Pharmacol. 61:586-594(2002).
[30]
VARIANTS GLC3A ARG-144 AND CYS-445.
PubMed=14640114; DOI=10.1007/s00439-003-1035-0;
Chakrabarti S., Komatireddy S., Mandal A.K., Balasubramanian D.;
"Gene symbol: CYP1B1. Disease: glaucoma, primary congenital.";
Hum. Genet. 113:556-558(2003).
[31]
VARIANTS GLC3A LYS-229; ARG-232; LYS-387; SER-390; SER-399 AND
TYR-423, AND VARIANTS GLY-48; SER-119; VAL-432 AND SER-453.
PubMed=14635112; DOI=10.1002/humu.9197;
Colomb E., Kaplan J., Garchon H.-J.;
"Novel cytochrome P450 1B1 (CYP1B1) mutations in patients with primary
congenital glaucoma in France.";
Hum. Mutat. 22:496-496(2003).
[32]
VARIANTS GLC3A ILE-215; 355-ARG--ALA-358 DEL AND MET-364, AND VARIANTS
GLY-48; SER-119; VAL-432 AND SER-453.
PubMed=12525557; DOI=10.1136/jmg.40.1.e9;
Sitorus R., Ardjo S.M., Lorenz B., Preising M.;
"CYP1B1 gene analysis in primary congenital glaucoma in Indonesian and
European patients.";
J. Med. Genet. 40:E9-E9(2003).
[33]
VARIANTS POAG ASN-81; LYS-229; ARG-232; SER-269--PHE-271 DEL; LYS-387;
HIS-390; TYR-423 AND GLY-443, VARIANTS GLC3A ARG-232; LYS-387 AND
TYR-423, AND VARIANTS GLY-48; SER119; VAL-432 AND SER-453.
PubMed=15342693; DOI=10.1136/jmg.2004.020024;
Melki R., Colomb E., Lefort N., Brezin A.P., Garchon H.-J.;
"CYP1B1 mutations in French patients with early-onset primary open-
angle glaucoma.";
J. Med. Genet. 41:647-651(2004).
[34]
VARIANTS GLC3A PRO-77; PRO-115; ARG-132; PRO-144; LEU-193; LYS-229;
ARG-239; HIS-368; HIS-390; CYS-390; LEU-437 AND ASP-466, AND VARIANTS
GLY-48; SER-119; VAL-432 AND SER-453.
PubMed=15475877;
Reddy A.B.M., Kaur K., Mandal A.K., Panicker S.G., Thomas R.,
Hasnain S.E., Balasubramanian D., Chakrabarti S.;
"Mutation spectrum of the CYP1B1 gene in Indian primary congenital
glaucoma patients.";
Mol. Vis. 10:696-702(2004).
[35]
VARIANT GLC3A CYS-390.
PubMed=15255109; DOI=10.1076/opge.25.1.3.28999;
Curry S.M., Daou A.G., Hermanns P., Molinari A., Lewis R.A.,
Bejjani B.A.;
"Cytochrome P4501B1 mutations cause only part of primary congenital
glaucoma in Ecuador.";
Ophthalmic Genet. 25:3-9(2004).
[36]
VARIANTS GLC3A GLU-61; HIS-368 AND THR-388, AND VARIANT GLY-422.
PubMed=16490498; DOI=10.1016/j.ajo.2005.11.001;
Alfadhli S., Behbehani A., Elshafey A., Abdelmoaty S., Al-Awadi S.;
"Molecular and clinical evaluation of primary congenital glaucoma in
Kuwait.";
Am. J. Ophthalmol. 141:512-516(2006).
[37]
VARIANTS POAG CYS-57; LYS-229; HIS-368; LEU-515; THR-523 AND GLY-530,
AND VARIANTS GLY-48; SER-119; VAL-432; SER-453 AND ALA-518.
PubMed=16688110;
Acharya M., Mookherjee S., Bhattacharjee A., Bandyopadhyay A.K.,
Daulat Thakur S.K., Bhaduri G., Sen A., Ray K.;
"Primary role of CYP1B1 in Indian juvenile-onset POAG patients.";
Mol. Vis. 12:399-404(2006).
[38]
VARIANTS GLC3A GLU-61; ASN-81; LYS-229; LEU-343 DEL; HIS-368; LYS-387
AND TRP-469.
PubMed=16735994;
Chavarria-Soley G., Michels-Rautenstrauss K., Pasutto F., Flikier D.,
Flikier P., Cirak S., Bejjani B., Winters D.L., Lewis R.A., Mardin C.,
Reis A., Rautenstrauss B.;
"Primary congenital glaucoma and Rieger's anomaly: extended haplotypes
reveal founder effects for eight distinct CYP1B1 mutations.";
Mol. Vis. 12:523-531(2006).
[39]
VARIANTS POAG TRP-28; GLU-61; ASN-81; TRP-145; LYS-229; PHE-409 AND
GLY-443, AND VARIANTS LEU-52; HIS-144; PRO-189 AND SER-330.
PubMed=16862072;
Lopez-Garrido M.-P., Sanchez-Sanchez F., Lopez-Martinez F.,
Aroca-Aguilar J.-D., Blanco-Marchite C., Coca-Prados M., Escribano J.;
"Heterozygous CYP1B1 gene mutations in Spanish patients with primary
open-angle glaucoma.";
Mol. Vis. 12:748-755(2006).
[40]
CHARACTERIZATION OF VARIANTS GLC3A GLU-61; SER-203; LYS-229 AND
LEU-343 DEL, AND CHARACTERIZATION OF VARIANT POAG ASN-81.
PubMed=18470941; DOI=10.1002/humu.20786;
Chavarria-Soley G., Sticht H., Aklillu E., Ingelman-Sundberg M.,
Pasutto F., Reis A., Rautenstrauss B.;
"Mutations in CYP1B1 cause primary congenital glaucoma by reduction of
either activity or abundance of the enzyme.";
Hum. Mutat. 29:1147-1153(2008).
-!- 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:10426814, ECO:0000269|PubMed:15258110,
ECO:0000269|PubMed:22888116, ECO:0000269|PubMed:23821647}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:22888116}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:21147782};
-!- ENZYME REGULATION: Enzyme activity is increased by liposomes
containing anionic phospholipids, phosphatidic acid and
cardiolipin. Inhibited by naringenin with an IC(50) of 5 uM.
{ECO:0000269|PubMed:22888116, ECO:0000269|PubMed:22935222}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.0 uM for 17-beta-estradiol {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=17.0 uM for testosterone {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=24.0 uM for progesterone {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=18.5 uM for retinol {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=8.5 uM for retinal {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=29.8 uM for arachidonic acid {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
KM=212.8 uM for 7,12-dimethyltetraphene
{ECO:0000269|PubMed:10426814, ECO:0000269|PubMed:15258110};
Vmax=14.95 nmol/min/mg enzyme for 17-beta-estradiol 4-
hydroxylation {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
Vmax=6.9 nmol/min/mg enzyme for 17-beta-estradiol 2-
hydroxylation {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
Vmax=36.16 nmol/min/mg enzyme for testosterone 6-beta-
hydroxylation {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
Vmax=9.86 nmol/min/mg enzyme for progesterone 6-beta-
hydroxylation {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
Vmax=37.80 nmol/min/mg enzyme for progesterone 16-alpha-
hydroxylation {ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:15258110};
Note=kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal,
2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for
arachidonic acid.;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
Mitochondrion {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in many tissues.
{ECO:0000269|PubMed:8175734}.
-!- INDUCTION: By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-
tetrachlorodibenzo-p-dioxin (TCDD). {ECO:0000269|PubMed:8175734}.
-!- POLYMORPHISM: Various CYP1B1 alleles are known. The sequence shown
is that of allele CYP1B1*1.
-!- DISEASE: Anterior segment dysgenesis 6 (ASGD6) [MIM:617315]: A
form of anterior segment dysgenesis, a group of defects affecting
anterior structures of the eye including cornea, iris, lens,
trabecular meshwork, and Schlemm canal. Anterior segment
dysgeneses result from abnormal migration or differentiation of
the neural crest derived mesenchymal cells that give rise to
components of the anterior chamber during eye development.
Different anterior segment anomalies may exist alone or in
combination, including iris hypoplasia, enlarged or reduced
corneal diameter, corneal vascularization and opacity, posterior
embryotoxon, corectopia, polycoria, abnormal iridocorneal angle,
ectopia lentis, and anterior synechiae between the iris and
posterior corneal surface. Clinical conditions falling within the
phenotypic spectrum of anterior segment dysgeneses include
aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters
anomaly, and iridogoniodysgenesis. ASGD6 patients predominantly
manifest Peters anomaly. Peters anomaly consists of corneal
leukoma, defects in the posterior structures of the cornea such as
absence of the posterior corneal stroma and Descemet membrane, and
a variable degree of iridocorneal and/or keratolenticular
adhesions. Over 50% of patients develop glaucoma in childhood.
{ECO:0000269|PubMed:11403040}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Glaucoma 3, primary congenital, A (GLC3A) [MIM:231300]:
An autosomal recessive form of primary congenital glaucoma (PCG).
PCG is characterized by marked increase of intraocular pressure at
birth or early childhood, large ocular globes (buphthalmos) and
corneal edema. It results from developmental defects of the
trabecular meshwork and anterior chamber angle of the eye that
prevent adequate drainage of aqueous humor.
{ECO:0000269|PubMed:10227395, ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:11184479, ECO:0000269|PubMed:11527932,
ECO:0000269|PubMed:11980847, ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:12525557, ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:14640114, ECO:0000269|PubMed:15255109,
ECO:0000269|PubMed:15342693, ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16490498, ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:18470941, ECO:0000269|PubMed:9463332,
ECO:0000269|PubMed:9497261}. Note=The disease is caused by
mutations affecting distinct genetic loci, including the gene
represented in this entry.
-!- DISEASE: Glaucoma, primary open angle (POAG) [MIM:137760]: A
complex and genetically heterogeneous ocular disorder
characterized by a specific pattern of optic nerve and visual
field defects. The angle of the anterior chamber of the eye is
open, and usually the intraocular pressure is increased. However,
glaucoma can occur at any intraocular pressure. The disease is
generally asymptomatic until the late stages, by which time
significant and irreversible optic nerve damage has already taken
place. In some cases, POAG shows digenic inheritance involving
mutations in CYP1B1 and MYOC genes. {ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:15342693, ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:16862072, ECO:0000269|PubMed:18470941}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. CYP1B1 mutations
have been reported to pose a significant risk for early-onset POAG
and also modify glaucoma phenotype in patients who do not carry a
MYOC mutation (PubMed:15342693). {ECO:0000269|PubMed:15342693}.
-!- DISEASE: Glaucoma 1, open angle, A (GLC1A) [MIM:137750]: A form of
primary open angle glaucoma (POAG). POAG is characterized by a
specific pattern of optic nerve and visual field defects. The
angle of the anterior chamber of the eye is open, and usually the
intraocular pressure is increased. However, glaucoma can occur at
any intraocular pressure. The disease is generally asymptomatic
until the late stages, by which time significant and irreversible
optic nerve damage has already taken place.
{ECO:0000269|PubMed:11774072}. Note=The gene represented in this
entry acts as a disease modifier. Digenic mutations in CYP1B1 and
MYOC have been found in a family segregating both primary adult-
onset and juvenile forms of open angle glaucoma (PubMed:11774072).
All affected family members with mutations in both MYOC and CYP1B1
had juvenile glaucoma, whereas those with only the MYOC mutation
had the adult-onset form (PubMed:11774072).
{ECO:0000269|PubMed:11774072}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP1B1 alleles;
URL="http://www.cypalleles.ki.se/cyp1b1.htm";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp1b1/";
-----------------------------------------------------------------------
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EMBL; U03688; AAA19567.1; -; mRNA.
EMBL; U56438; AAC50809.1; -; Genomic_DNA.
EMBL; AF450132; AAM50512.1; -; Genomic_DNA.
EMBL; AF450131; AAM50512.1; JOINED; Genomic_DNA.
EMBL; BT019979; AAV38782.1; -; mRNA.
EMBL; AY393998; AAQ87875.1; -; Genomic_DNA.
EMBL; BC012049; AAH12049.1; -; mRNA.
EMBL; AF171066; AAG43404.1; -; Genomic_DNA.
CCDS; CCDS1793.1; -.
PIR; A54116; A54116.
RefSeq; NP_000095.2; NM_000104.3.
UniGene; Hs.154654; -.
PDB; 3PM0; X-ray; 2.70 A; A=51-543.
PDBsum; 3PM0; -.
ProteinModelPortal; Q16678; -.
SMR; Q16678; -.
BioGrid; 107925; 2.
IntAct; Q16678; 2.
STRING; 9606.ENSP00000260630; -.
BindingDB; Q16678; -.
ChEMBL; CHEMBL4878; -.
DrugBank; DB02342; 2-Methoxyestradiol.
DrugBank; DB00613; Amodiaquine.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB00121; Biotin.
DrugBank; DB00201; Caffeine.
DrugBank; DB00363; Clozapine.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB01248; Docetaxel.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00783; Estradiol.
DrugBank; DB00655; Estrone.
DrugBank; DB00499; Flutamide.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB00448; Lansoprazole.
DrugBank; DB01065; Melatonin.
DrugBank; DB01204; Mitoxantrone.
DrugBank; DB00338; Omeprazole.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB01229; Paclitaxel.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01087; Primaquine.
DrugBank; DB01168; Procarbazine.
DrugBank; DB00396; Progesterone.
DrugBank; DB00818; Propofol.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB00624; Testosterone.
DrugBank; DB00277; Theophylline.
GuidetoPHARMACOLOGY; 1320; -.
SwissLipids; SLP:000001331; -.
iPTMnet; Q16678; -.
PhosphoSitePlus; Q16678; -.
BioMuta; CYP1B1; -.
DMDM; 48429256; -.
EPD; Q16678; -.
MaxQB; Q16678; -.
PaxDb; Q16678; -.
PeptideAtlas; Q16678; -.
PRIDE; Q16678; -.
DNASU; 1545; -.
Ensembl; ENST00000610745; ENSP00000478561; ENSG00000138061.
Ensembl; ENST00000614273; ENSP00000483678; ENSG00000138061.
GeneID; 1545; -.
KEGG; hsa:1545; -.
UCSC; uc032njx.2; human.
CTD; 1545; -.
DisGeNET; 1545; -.
EuPathDB; HostDB:ENSG00000138061.11; -.
GeneCards; CYP1B1; -.
GeneReviews; CYP1B1; -.
H-InvDB; HIX0001979; -.
HGNC; HGNC:2597; CYP1B1.
HPA; CAB011705; -.
HPA; HPA026863; -.
MalaCards; CYP1B1; -.
MIM; 137750; phenotype.
MIM; 137760; phenotype.
MIM; 231300; phenotype.
MIM; 601771; gene.
MIM; 617315; phenotype.
neXtProt; NX_Q16678; -.
OpenTargets; ENSG00000138061; -.
Orphanet; 98976; Congenital glaucoma.
Orphanet; 98977; Juvenile glaucoma.
Orphanet; 708; Peters anomaly.
Orphanet; 353225; Primary adult open-angle glaucoma.
PharmGKB; PA27094; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140831; -.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; Q16678; -.
KO; K07410; -.
OMA; AVCFGCR; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; Q16678; -.
TreeFam; TF105095; -.
BioCyc; MetaCyc:HS06443-MONOMER; -.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
Reactome; R-HSA-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
SABIO-RK; Q16678; -.
SIGNOR; Q16678; -.
ChiTaRS; CYP1B1; human.
EvolutionaryTrace; Q16678; -.
GeneWiki; CYP1B1; -.
GenomeRNAi; 1545; -.
PRO; PR:Q16678; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138061; -.
CleanEx; HS_CYP1B1; -.
ExpressionAtlas; Q16678; baseline and differential.
Genevisible; Q16678; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISS: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; IDA: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:0019825; F:oxygen binding; TAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
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; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
GO; GO:0071603; P:endothelial cell-cell adhesion; IEA:Ensembl.
GO; GO:0019373; P:epoxygenase P450 pathway; TAS:Reactome.
GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:UniProtKB.
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:0097267; P:omega-hydroxylase P450 pathway; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
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:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0061304; P:retinal blood vessel morphogenesis; ISS: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; IDA:UniProtKB.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
GO; GO:0009404; P:toxin metabolic process; IEA:Ensembl.
GO; GO:0002930; P:trabecular meshwork development; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; TAS:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; IDA: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;
3D-structure; Complete proteome; Disease mutation;
Endoplasmic reticulum; Glaucoma; Heme; Iron; Membrane; Metal-binding;
Microsome; Mitochondrion; Monooxygenase; Oxidoreductase;
Peters anomaly; Polymorphism; Reference proteome.
CHAIN 1 543 Cytochrome P450 1B1.
/FTId=PRO_0000051660.
METAL 470 470 Iron (heme axial ligand).
{ECO:0000244|PDB:3PM0,
ECO:0000269|PubMed:21147782}.
SITE 395 395 Major determinant of CYP1B1 17beta-
estradiol hydroxylation regiospecificity.
VARIANT 28 28 S -> W (in POAG; dbSNP:rs780002791).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054227.
VARIANT 48 48 R -> G (in allele CYP1B1*2, allele
CYP1B1*5, allele CYP1B1*6 and allele
CYP1B1*7; dbSNP:rs10012).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:11527932,
ECO:0000269|PubMed:11854439,
ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:12525557,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16688110,
ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
/FTId=VAR_011752.
VARIANT 52 52 P -> L (in dbSNP:rs201824781).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054228.
VARIANT 57 57 W -> C (in POAG; juvenile onset; allele
CYP1B1*11; dbSNP:rs72549387).
{ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_008350.
VARIANT 61 61 G -> E (in GLC3A and POAG; allele
CYP1B1*12; reduces enzymatic activity;
dbSNP:rs28936700).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:16490498,
ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:16862072,
ECO:0000269|PubMed:18470941,
ECO:0000269|PubMed:9463332,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_001244.
VARIANT 68 68 Q -> R (in dbSNP:rs9282670).
/FTId=VAR_028735.
VARIANT 77 77 L -> P (in GLC3A).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:15475877}.
/FTId=VAR_054229.
VARIANT 81 81 Y -> N (in POAG; adult-onset; hypomorphic
allele; reduces the abundance of the
enzyme; dbSNP:rs9282671).
{ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:16862072,
ECO:0000269|PubMed:18470941}.
/FTId=VAR_028736.
VARIANT 115 115 A -> P (in GLC3A; dbSNP:rs764338357).
{ECO:0000269|PubMed:15475877}.
/FTId=VAR_054230.
VARIANT 119 119 A -> S (in allele CYP1B1*2, allele
CYP1B1*6 and allele CYP1B1*7;
significantly associated with breast or
lung cancer; no significant change in
17beta-estradiol 2- and 4-hydroxylation
activities and 17beta-estradiol affinity;
1.5-fold reduction in testosterone
affinity but nearly no change in
testosterone 6beta-hydroxylation
activity; 2-fold increase in progesterone
6beta- and 16alpha-hydroxylation
activities and 5-fold reduction in
progesterone affinity; dbSNP:rs1056827).
{ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:10739169,
ECO:0000269|PubMed:11527932,
ECO:0000269|PubMed:11854439,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:12525557,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16688110,
ECO:0000269|Ref.5}.
/FTId=VAR_011753.
VARIANT 132 132 M -> R (in GLC3A).
{ECO:0000269|PubMed:15475877}.
/FTId=VAR_054231.
VARIANT 144 144 Q -> H. {ECO:0000269|PubMed:16862072}.
/FTId=VAR_054232.
VARIANT 144 144 Q -> P (in GLC3A).
{ECO:0000269|PubMed:15475877}.
/FTId=VAR_054233.
VARIANT 144 144 Q -> R (in GLC3A; dbSNP:rs753847648).
{ECO:0000269|PubMed:14640114}.
/FTId=VAR_054234.
VARIANT 145 145 R -> W (in POAG).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054235.
VARIANT 184 184 G -> S. {ECO:0000269|PubMed:11980847}.
/FTId=VAR_054236.
VARIANT 189 189 A -> P (associated with ocular
hypertension susceptibility).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054237.
VARIANT 192 192 D -> V (in GLC3A).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054238.
VARIANT 193 193 P -> L (in GLC3A; dbSNP:rs529769268).
{ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:15475877}.
/FTId=VAR_054239.
VARIANT 198 198 V -> I (in GLC3A; dbSNP:rs59472972).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054240.
VARIANT 203 203 N -> S (in GLC3A; reduces enzymatic
activity). {ECO:0000269|PubMed:18470941}.
/FTId=VAR_054241.
VARIANT 206 206 S -> N (in dbSNP:rs9341248).
{ECO:0000269|Ref.5}.
/FTId=VAR_018869.
VARIANT 215 215 S -> I (in GLC3A; dbSNP:rs72549384).
{ECO:0000269|PubMed:12525557}.
/FTId=VAR_054242.
VARIANT 229 229 E -> K (in GLC3A and POAG; juvenile-
onset; hypomorphic allele; reduces the
abundance of the enzyme;
dbSNP:rs57865060).
{ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:16862072,
ECO:0000269|PubMed:18470941}.
/FTId=VAR_054243.
VARIANT 232 232 G -> R (in GLC3A and POAG; adult-onset;
dbSNP:rs104893628).
{ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693}.
/FTId=VAR_054244.
VARIANT 239 239 S -> R (in GLC3A).
{ECO:0000269|PubMed:15475877}.
/FTId=VAR_054245.
VARIANT 266 266 R -> L (in dbSNP:rs9341250).
{ECO:0000269|Ref.5}.
/FTId=VAR_018870.
VARIANT 269 271 Missing (in GLC3A and POAG).
{ECO:0000269|PubMed:10655546}.
/FTId=VAR_054246.
VARIANT 320 320 V -> L (in GLC3A; dbSNP:rs72549382).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054247.
VARIANT 330 330 A -> F (in GLC3A; requires 2 nucleotide
substitutions; unknown pathological
significance).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054248.
VARIANT 330 330 A -> S (associated with ocular
hypertension susceptibility).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054249.
VARIANT 343 343 Missing (in GLC3A; reduces enzymatic
activity and also the abundance of the
enzyme). {ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:18470941}.
/FTId=VAR_054250.
VARIANT 345 345 L -> F (in POAG; dbSNP:rs66583685).
{ECO:0000269|PubMed:11774072}.
/FTId=VAR_054251.
VARIANT 355 358 Missing (in GLC3A).
{ECO:0000269|PubMed:12525557}.
/FTId=VAR_054252.
VARIANT 364 364 V -> M (in GLC3A; dbSNP:rs72549379).
{ECO:0000269|PubMed:11184479,
ECO:0000269|PubMed:11527932,
ECO:0000269|PubMed:12525557}.
/FTId=VAR_054253.
VARIANT 365 365 G -> W (in GLC3A; allele CYP1B1*18;
dbSNP:rs55771538).
{ECO:0000269|PubMed:9497261}.
/FTId=VAR_001245.
VARIANT 368 368 R -> H (in GLC3A and GLC1A; acts as GLC1A
disease modifier in patients also
carrying Val-399 mutation in MYOC;
dbSNP:rs79204362).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16490498,
ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:16735994}.
/FTId=VAR_016034.
VARIANT 374 374 D -> N (in GLC3A; dbSNP:rs28936413).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:9463332}.
/FTId=VAR_001246.
VARIANT 379 379 P -> L (in allele CYP1B1*19;
dbSNP:rs56305281).
{ECO:0000269|PubMed:9497261}.
/FTId=VAR_008351.
VARIANT 387 387 E -> K (in GLC3A and POAG; allele
CYP1B1*20; dbSNP:rs55989760).
{ECO:0000269|PubMed:10227395,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_008352.
VARIANT 388 388 A -> T (in GLC3A).
{ECO:0000269|PubMed:16490498}.
/FTId=VAR_054254.
VARIANT 390 390 R -> C (in GLC3A; dbSNP:rs148542782).
{ECO:0000269|PubMed:15255109,
ECO:0000269|PubMed:15475877}.
/FTId=VAR_054255.
VARIANT 390 390 R -> H (in GLC3A; allele CYP1B1*21;
dbSNP:rs56010818).
{ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_008353.
VARIANT 390 390 R -> S (in GLC3A; dbSNP:rs148542782).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:14635112}.
/FTId=VAR_054256.
VARIANT 399 399 I -> S (in GLC3A; dbSNP:rs72549378).
{ECO:0000269|PubMed:14635112}.
/FTId=VAR_054257.
VARIANT 409 409 V -> F (in POAG).
{ECO:0000269|PubMed:16862072}.
/FTId=VAR_054258.
VARIANT 422 422 V -> G. {ECO:0000269|PubMed:16490498}.
/FTId=VAR_054259.
VARIANT 423 423 N -> Y (in GLC3A and POAG; juvenile-
onset; dbSNP:rs104893629).
{ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693}.
/FTId=VAR_054260.
VARIANT 432 432 L -> V (in allele CYP1B1*3, allele
CYP1B1*5, allele CYP1B1*6 and allele
CYP1B1*7; 1.6-fold increase in 17beta-
estradiol 4-hydroxylation activity but no
change in 17beta-estradiol 2-
hydroxylation activity; 2-fold reduction
in testosterone 6beta-hydroxylation
activity and 3-fold reduction in
testosterone affinity; 6-fold and 4-fold
increase in progesterone 6beta- and
16alpha-hydroxylation activity,
respectively and 7-fold reduction in
progesterone affinity; dbSNP:rs1056836).
{ECO:0000269|PubMed:10426814,
ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:10739169,
ECO:0000269|PubMed:11527932,
ECO:0000269|PubMed:11774072,
ECO:0000269|PubMed:11854439,
ECO:0000269|PubMed:11980847,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:12525557,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:9497261,
ECO:0000269|PubMed:9823305,
ECO:0000269|Ref.5}.
/FTId=VAR_001248.
VARIANT 437 437 P -> L (in GLC3A; allele CYP1B1*23;
dbSNP:rs56175199).
{ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_008354.
VARIANT 441 441 D -> H (in dbSNP:rs4986887).
/FTId=VAR_028737.
VARIANT 443 443 A -> G (in GLC3A and POAG; allele
CYP1B1*7; unknown pathological
significance; dbSNP:rs4986888).
{ECO:0000269|PubMed:11854439,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:16862072}.
/FTId=VAR_018774.
VARIANT 444 444 R -> Q (in GLC3A; dbSNP:rs72549376).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054261.
VARIANT 445 445 F -> C (in GLC3A).
{ECO:0000269|PubMed:14640114}.
/FTId=VAR_054262.
VARIANT 449 449 D -> E (in dbSNP:rs1056837).
/FTId=VAR_028738.
VARIANT 453 453 N -> S (in allele CYP1B1*4;
dbSNP:rs1800440).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:11854439,
ECO:0000269|PubMed:12036985,
ECO:0000269|PubMed:12525557,
ECO:0000269|PubMed:14635112,
ECO:0000269|PubMed:15342693,
ECO:0000269|PubMed:15475877,
ECO:0000269|PubMed:16688110,
ECO:0000269|PubMed:9823305,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_008355.
VARIANT 466 466 G -> D (in GLC3A; dbSNP:rs868208502).
{ECO:0000269|PubMed:15475877}.
/FTId=VAR_054263.
VARIANT 469 469 R -> W (in GLC3A; allele CYP1B1*25;
dbSNP:rs28936701).
{ECO:0000269|PubMed:10655546,
ECO:0000269|PubMed:16735994,
ECO:0000269|PubMed:9463332,
ECO:0000269|PubMed:9497261}.
/FTId=VAR_001247.
VARIANT 499 499 E -> G (in GLC3A; dbSNP:rs72549372).
{ECO:0000269|PubMed:11527932}.
/FTId=VAR_054264.
VARIANT 515 515 S -> L (in POAG; unknown pathological
significance).
{ECO:0000269|PubMed:16688110}.
/FTId=VAR_054265.
VARIANT 518 518 V -> A. {ECO:0000269|PubMed:16688110}.
/FTId=VAR_054266.
VARIANT 523 523 R -> T (in POAG; juvenile-onset).
{ECO:0000269|PubMed:16688110}.
/FTId=VAR_054267.
VARIANT 530 530 D -> G (in POAG).
{ECO:0000269|PubMed:16688110}.
/FTId=VAR_054268.
MUTAGEN 395 395 V->L: Invertes the 4OH E2:2OH E2
hydroxylation preference from 5.1 to
0.45. {ECO:0000269|PubMed:23821647}.
HELIX 70 81 {ECO:0000244|PDB:3PM0}.
STRAND 83 89 {ECO:0000244|PDB:3PM0}.
STRAND 92 97 {ECO:0000244|PDB:3PM0}.
HELIX 100 107 {ECO:0000244|PDB:3PM0}.
TURN 108 113 {ECO:0000244|PDB:3PM0}.
HELIX 121 125 {ECO:0000244|PDB:3PM0}.
HELIX 126 129 {ECO:0000244|PDB:3PM0}.
STRAND 132 135 {ECO:0000244|PDB:3PM0}.
HELIX 139 154 {ECO:0000244|PDB:3PM0}.
HELIX 162 183 {ECO:0000244|PDB:3PM0}.
HELIX 184 188 {ECO:0000244|PDB:3PM0}.
HELIX 194 209 {ECO:0000244|PDB:3PM0}.
HELIX 219 224 {ECO:0000244|PDB:3PM0}.
HELIX 228 235 {ECO:0000244|PDB:3PM0}.
TURN 241 243 {ECO:0000244|PDB:3PM0}.
HELIX 245 249 {ECO:0000244|PDB:3PM0}.
HELIX 253 282 {ECO:0000244|PDB:3PM0}.
HELIX 292 304 {ECO:0000244|PDB:3PM0}.
HELIX 317 319 {ECO:0000244|PDB:3PM0}.
HELIX 320 348 {ECO:0000244|PDB:3PM0}.
HELIX 350 363 {ECO:0000244|PDB:3PM0}.
HELIX 372 377 {ECO:0000244|PDB:3PM0}.
HELIX 379 392 {ECO:0000244|PDB:3PM0}.
STRAND 407 409 {ECO:0000244|PDB:3PM0}.
STRAND 412 414 {ECO:0000244|PDB:3PM0}.
STRAND 419 424 {ECO:0000244|PDB:3PM0}.
HELIX 425 428 {ECO:0000244|PDB:3PM0}.
TURN 431 433 {ECO:0000244|PDB:3PM0}.
STRAND 435 439 {ECO:0000244|PDB:3PM0}.
HELIX 442 445 {ECO:0000244|PDB:3PM0}.
HELIX 454 457 {ECO:0000244|PDB:3PM0}.
HELIX 473 490 {ECO:0000244|PDB:3PM0}.
STRAND 491 495 {ECO:0000244|PDB:3PM0}.
STRAND 505 513 {ECO:0000244|PDB:3PM0}.
STRAND 518 524 {ECO:0000244|PDB:3PM0}.
SEQUENCE 543 AA; 60846 MW; 46B6DA7368F63EA2 CRC64;
MGTSLSPNDP WPLNPLSIQQ TTLLLLLSVL ATVHVGQRLL RQRRRQLRSA PPGPFAWPLI
GNAAAVGQAA HLSFARLARR YGDVFQIRLG SCPIVVLNGE RAIHQALVQQ GSAFADRPAF
ASFRVVSGGR SMAFGHYSEH WKVQRRAAHS MMRNFFTRQP RSRQVLEGHV LSEARELVAL
LVRGSADGAF LDPRPLTVVA VANVMSAVCF GCRYSHDDPE FRELLSHNEE FGRTVGAGSL
VDVMPWLQYF PNPVRTVFRE FEQLNRNFSN FILDKFLRHC ESLRPGAAPR DMMDAFILSA
EKKAAGDSHG GGARLDLENV PATITDIFGA SQDTLSTALQ WLLLLFTRYP DVQTRVQAEL
DQVVGRDRLP CMGDQPNLPY VLAFLYEAMR FSSFVPVTIP HATTANTSVL GYHIPKDTVV
FVNQWSVNHD PLKWPNPENF DPARFLDKDG LINKDLTSRV MIFSVGKRRC IGEELSKMQL
FLFISILAHQ CDFRANPNEP AKMNFSYGLT IKPKSFKVNV TLRESMELLD SAVQNLQAKE
TCQ


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