CP1A1_RAT
ID CP1A1_RAT Reviewed; 524 AA.
AC P00185;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cytochrome P450 1A1;
DE Short=CYP1A1;
DE EC=1.14.14.1 {ECO:0000250|UniProtKB:P04798};
DE AltName: Full=CYPIA1;
DE AltName: Full=Cytochrome P450 form 6;
DE AltName: Full=Cytochrome P450-C;
DE AltName: Full=Cytochrome P450-P1;
DE AltName: Full=Cytochrome P450MT2;
DE AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE EC=4.2.1.152 {ECO:0000250|UniProtKB:P04798};
DE Contains:
DE RecName: Full=Cytochrome P450MT2A;
DE Contains:
DE RecName: Full=Cytochrome P450MT2B;
GN Name=Cyp1a1 {ECO:0000303|PubMed:19401463, ECO:0000312|RGD:2458};
GN Synonyms=Cyp1a-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6089174; DOI=10.1073/pnas.81.16.5066;
RA Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.;
RT "Distinct organization of methylcholanthrene- and phenobarbital-inducible
RT cytochrome P-450 genes in the rat.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6324135; DOI=10.1093/nar/12.6.2929;
RA Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.;
RT "Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-
RT induced rat liver cytochrome P-450MC.";
RL Nucleic Acids Res. 12:2929-2938(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3838427; DOI=10.1016/0003-9861(85)90300-5;
RA Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L., Renli A.M.,
RA Bresnick E.;
RT "Gene structure and nucleotide sequence for rat cytochrome P-450c.";
RL Arch. Biochem. Biophys. 237:465-476(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=3718958; DOI=10.1021/bi00357a015;
RA Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V.,
RA Friedman F.K.;
RT "Amino-terminal sequence and structure of monoclonal antibody
RT immunopurified cytochromes P-450.";
RL Biochemistry 25:2397-2402(1986).
RN [5]
RP PROTEIN SEQUENCE OF 2-22.
RX PubMed=3041969; DOI=10.1016/0006-2952(88)90634-x;
RA Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.;
RT "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat
RT liver.";
RL Biochem. Pharmacol. 37:3245-3249(1988).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8651689; DOI=10.1006/abbi.1996.0236;
RA Cvrk T., Hodek P., Strobel H.W.;
RT "Identification and characterization of cytochrome P4501A1 amino acid
RT residues interacting with a radiolabeled photoaffinity diazido-
RT benzphetamine analogue.";
RL Arch. Biochem. Biophys. 330:142-152(1996).
RN [7]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF 32-VAL-THR-33, AND TOPOLOGY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9348277; DOI=10.1083/jcb.139.3.589;
RA Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J.,
RA Avadhani N.G.;
RT "Targeting of NH2-terminal-processed microsomal protein to mitochondria: a
RT novel pathway for the biogenesis of hepatic mitochondrial P450MT2.";
RL J. Cell Biol. 139:589-599(1997).
RN [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH HSP70, INTERACTION WITH HSP90,
RP INTERACTION WITH TOMM40, AND TOPOLOGY.
RX PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT mechanism.";
RL J. Biol. Chem. 284:17352-17363(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20972997; DOI=10.1002/rcm.4760;
RA Mesaros C., Lee S.H., Blair I.A.;
RT "Analysis of epoxyeicosatrienoic acids by chiral liquid
RT chromatography/electron capture atmospheric pressure chemical ionization
RT mass spectrometry using [13C]-analog internal standards.";
RL Rapid Commun. Mass Spectrom. 24:3237-3247(2010).
RN [10]
RP GLYCOSYLATION AT SER-71.
RX PubMed=24098488; DOI=10.1371/journal.pone.0076399;
RA Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
RT "Discovery and confirmation of O-GlcNAcylated proteins in rat liver
RT mitochondria by combination of mass spectrometry and immunological
RT methods.";
RL PLoS ONE 8:E76399-E76399(2013).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC various endogenous substrates, including fatty acids, steroid hormones
CC and vitamins. Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the
CC hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic
CC activity for the formation of hydroxyestrogens from estrone (E1) and
CC 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring
CC hydroxylated E1 and E2 at the C15alpha and C16alpha positions (By
CC similarity). Displays different regioselectivities for polyunsaturated
CC fatty acids (PUFA) hydroxylation (By similarity). Catalyzes the
CC epoxidation of double bonds of certain PUFA (PubMed:20972997). Converts
CC arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers,
CC 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the
CC vascular system. Displays an absolute stereoselectivity in the
CC epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S)
CC enantiomer (By similarity). May play an important role in all-trans
CC retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two
CC successive oxidative transformation of all-trans retinol to all-trans
CC retinal and then to the active form all-trans retinoic acid (By
CC similarity). May also participate in eicosanoids metabolism by
CC converting hydroperoxide species into oxo metabolites (lipoxygenase-
CC like reaction, NADPH-independent) (By similarity).
CC {ECO:0000250|UniProtKB:P04798, ECO:0000269|PubMed:20972997}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17151;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-
CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-
CC hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC 6alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47308, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:87605; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47309;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC 15alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47312, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:87618; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47313;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] =
CC 16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:47204, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47205;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47284, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:62847;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47285;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47288, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:87598;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47289;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC = 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:47276, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16469, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:87593;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47277;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132024;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49972, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132019; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49973;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49968, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:132016; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49969;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39811, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:63590; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76636; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131975; Evidence={ECO:0000269|PubMed:20972997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC Evidence={ECO:0000305|PubMed:20972997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49880, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131970; Evidence={ECO:0000269|PubMed:20972997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC Evidence={ECO:0000305|PubMed:20972997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49876, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131969; Evidence={ECO:0000269|PubMed:20972997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49877;
CC Evidence={ECO:0000305|PubMed:20972997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:131965; Evidence={ECO:0000269|PubMed:20972997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC Evidence={ECO:0000305|PubMed:20972997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52124, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:136411; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52125;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-
CC (6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P04798}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:20972997}.
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P04798}.
CC -!- SUBUNIT: Both Cytochrome P450MT2A and Cytochrome P450MT2B interact with
CC cytosolic chaperones HSP70 and HSP90; this interaction is required for
CC initial targeting to mitochondria. P450MT2B interacts (via
CC mitochondrial targeting signal) with TOMM40 (via N-terminus); this
CC interaction is required for translocation across the mitochondrial
CC outer membrane. {ECO:0000269|PubMed:19401463}.
CC -!- SUBCELLULAR LOCATION: [Cytochrome P450 1A1]: Cytoplasm
CC {ECO:0000269|PubMed:9348277}.
CC -!- SUBCELLULAR LOCATION: [Cytochrome P450MT2A]: Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:9348277}; Peripheral
CC membrane protein {ECO:0000305|PubMed:19401463,
CC ECO:0000305|PubMed:9348277}. Microsome membrane
CC {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC -!- SUBCELLULAR LOCATION: [Cytochrome P450MT2B]: Endoplasmic reticulum
CC membrane; Peripheral membrane protein. Mitochondrion inner membrane
CC {ECO:0000305|PubMed:19401463}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}. Microsome
CC membrane {ECO:0000269|PubMed:9348277}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19401463, ECO:0000305|PubMed:9348277}.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- INDUCTION: By 3-methylcholanthrene (3MC) and beta-naphthoflavone (BNF).
CC -!- DOMAIN: Contains a chimeric signal that facilitates targeting of the
CC protein to both the endoplasmic reticulum and mitochondria. A 12 amino
CC acid sequence between 33 and 44 functions as a putative mitochondrial-
CC targeting signal. The removal of the first 4- or 32-amino acid residues
CC from the intact protein positions the mitochondrial targeting signal
CC for efficient binding to the mitochondrial import receptors. The
CC membrane-free P4501A1 seems to be more sensitive to proteolysis.
CC -!- PTM: Two forms; MT2A (long form) and MT2B (short form); are produced by
CC NH2-terminal proteolytic cleavage. This cleavage activates a cryptic
CC mitochondrial targeting signal.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; K02246; AAA41027.1; -; Genomic_DNA.
DR EMBL; X00469; CAA25153.1; -; mRNA.
DR EMBL; M26129; AAA41025.1; -; Genomic_DNA.
DR PIR; A00185; O4RTMC.
DR RefSeq; NP_036672.2; NM_012540.2.
DR RefSeq; XP_006243212.1; XM_006243150.2.
DR AlphaFoldDB; P00185; -.
DR SMR; P00185; -.
DR BioGRID; 246477; 2.
DR STRING; 10116.ENSRNOP00000026473; -.
DR BindingDB; P00185; -.
DR ChEMBL; CHEMBL2922; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB01645; Genistein.
DR SwissLipids; SLP:000001590; -.
DR GlyGen; P00185; 1 site.
DR iPTMnet; P00185; -.
DR PhosphoSitePlus; P00185; -.
DR PaxDb; P00185; -.
DR PRIDE; P00185; -.
DR Ensembl; ENSRNOT00000026473; ENSRNOP00000026473; ENSRNOG00000019500.
DR GeneID; 24296; -.
DR KEGG; rno:24296; -.
DR UCSC; RGD:2458; rat.
DR CTD; 1543; -.
DR RGD; 2458; Cyp1a1.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00950000183037; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P00185; -.
DR OMA; NYGFRIE; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P00185; -.
DR TreeFam; TF105095; -.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR Reactome; R-RNO-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR Reactome; R-RNO-9018681; Biosynthesis of protectins.
DR SABIO-RK; P00185; -.
DR UniPathway; UPA00199; -.
DR UniPathway; UPA00912; -.
DR PRO; PR:P00185; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000019500; Expressed in duodenum and 10 other tissues.
DR Genevisible; P00185; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; ISO:RGD.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003824; F:catalytic activity; IDA:RGD.
DR GO; GO:0032451; F:demethylase activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:UniProtKB.
DR GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:RGD.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; ISO:RGD.
DR GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:RGD.
DR GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA:RGD.
DR 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; ISO:RGD.
DR GO; GO:0008395; F:steroid hydroxylase activity; IDA:RGD.
DR GO; GO:0070576; F:vitamin D 24-hydroxylase activity; ISO:RGD.
DR GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009308; P:amine metabolic process; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; IEP:RGD.
DR GO; GO:0008283; P:cell population proliferation; IEP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0009804; P:coumarin metabolic process; IDA:RGD.
DR GO; GO:0032502; P:developmental process; IEP:RGD.
DR GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IDA:RGD.
DR GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IDA:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0006306; P:DNA methylation; IEP:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0009812; P:flavonoid metabolic process; IDA:RGD.
DR GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:RGD.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISO:RGD.
DR GO; GO:0017143; P:insecticide metabolic process; IDA:RGD.
DR GO; GO:0002933; P:lipid hydroxylation; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:RGD.
DR GO; GO:0060137; P:maternal process involved in parturition; IEP:RGD.
DR GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009624; P:response to nematode; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0009615; P:response to virus; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01683; EP450ICYP1A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Heme; Iron; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Metal-binding; Microsome; Mitochondrion; Mitochondrion inner membrane;
KW Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..524
FT /note="Cytochrome P450 1A1"
FT /id="PRO_0000003564"
FT CHAIN 5..524
FT /note="Cytochrome P450MT2A"
FT /id="PRO_0000003565"
FT CHAIN 33..524
FT /note="Cytochrome P450MT2B"
FT /id="PRO_0000003566"
FT REGION 33..44
FT /note="Mitochondrial targeting signal"
FT /evidence="ECO:0000269|PubMed:19401463,
FT ECO:0000269|PubMed:9348277"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CARBOHYD 71
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:24098488"
FT MUTAGEN 32..33
FT /note="VT->AI: No proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:9348277"
FT CONFLICT 21..22
FT /note="TT -> VV (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="I -> M (in Ref. 2; CAA25153)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="M -> S (in Ref. 3; AAA41025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 59393 MW; C766DF8044D598C5 CRC64;
MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL PFIGHVLTLG
KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VKQGDDFKGR PDLYSFTLIA
NGQSMTFNPD SGPLWAARRR LAQNALKSFS IASDPTLASS CYLEEHVSKE AEYLISKFQK
LMAEVGHFDP FKYLVVSVAN VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF
IPILRYLPNS SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE
NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE LDTVIGRDRQ
PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL NGFYIPKGHC VFVNQWQVNH
DQELWGDPNE FRPERFLTSS GTLDKHLSEK VILFGLGKRK CIGETIGRLE VFLFLAILLQ
QMEFNVSPGE KVDMTPAYGL TLKHARCEHF QVQMRSSGPQ HLQA
