Cytochrome P450 1A1

Details

Name
Cytochrome P450 1A1
Kind
protein
Synonyms
  • 1.14.14.1
  • Cyp1a-1
  • CYP1A1
  • CYPIA1
  • Cytochrome P450-C
  • Cytochrome P450MT2
Gene Name
Cyp1a1
UniProtKB Entry
P00185Swiss-Prot
Organism
Rat
NCBI Taxonomy ID
10116
Amino acid sequence
>lcl|BSEQ0051627|Cytochrome P450 1A1
MPSVYGFPAFTSATELLLAVTTFCLGFWVVRVTRTWVPKGLKSPPGPWGLPFIGHVLTLG
KNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLIA
NGQSMTFNPDSGPLWAARRRLAQNALKSFSIASDPTLASSCYLEEHVSKEAEYLISKFQK
LMAEVGHFDPFKYLVVSVANVICAICFGRRYDHDDQELLSIVNLSNEFGEVTGSGYPADF
IPILRYLPNSSLDAFKDLNKKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRRLDE
NANVQLSDDKVITIVFDLFGAGFDTITTAISWSLMYLVTNPRIQRKIQEELDTVIGRDRQ
PRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTIRDTSLNGFYIPKGHCVFVNQWQVNH
DQELWGDPNEFRPERFLTSSGTLDKHLSEKVILFGLGKRKCIGETIGRLEVFLFLAILLQ
QMEFNVSPGEKVDMTPAYGLTLKHARCEHFQVQMRSSGPQHLQA
Number of residues
524
Molecular Weight
59392.695
Theoretical pI
Not Available
GO Classification
Functions
aromatase activity / catalytic activity / demethylase activity / enzyme binding / estrogen 16-alpha-hydroxylase activity / flavonoid 3'-monooxygenase activity / heme binding / iron ion binding / monooxygenase activity / oxidoreductase activity / oxidoreductase activity, acting on diphenols and related substances as donors / 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 / steroid hydroxylase activity / vitamin D 24-hydroxylase activity
Processes
9-cis-retinoic acid biosynthetic process / aging / amine metabolic process / camera-type eye development / cell proliferation / cellular response to copper ion / cellular response to organic cyclic compound / coumarin metabolic process / developmental process / dibenzo-p-dioxin catabolic process / dibenzo-p-dioxin metabolic process / digestive tract development / drug metabolic process / flavonoid metabolic process / hepatocyte differentiation / heterocycle metabolic process / hydrogen peroxide biosynthetic process / insecticide metabolic process / lipid hydroxylation / liver development / maternal process involved in parturition / oxidation-reduction process / porphyrin-containing compound metabolic process / positive regulation of G1/S transition of mitotic cell cycle / response to antibiotic / response to arsenic-containing substance / response to drug / response to food / response to herbicide / response to hyperoxia / response to hypoxia / response to immobilization stress / response to iron(III) ion / response to lipopolysaccharide / response to nematode / response to organic cyclic compound / response to organic substance / response to toxic substance / response to virus / response to vitamin A / response to wounding / steroid metabolic process / toxin metabolic process
Components
cytoplasm / endoplasmic reticulum membrane / intracellular membrane-bounded organelle / mitochondrial membrane / mitochondrion
General Function
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions (By similarity). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (By similarity). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (By similarity). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (By similarity). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (By similarity).
Specific Function
arachidonic acid monooxygenase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051628|Cytochrome P450 1A1 (Cyp1a1)
ATGCCTTCTGTGTATGGATTCCCAGCCTTCACATCAGCCACAGAGCTGCTCTTGGCCGTC
ACCACATTCTGCCTTGGATTCTGGGTGGTTAGAGTCACAAGAACCTGGGTTCCCAAAGGT
CTGAAGAGTCCACCCGGACCCTGGGGCTTGCCCTTCATGGGGCACGTGCTGACCCTGGGG
AAGAACCCACACCTGTCACTGACAAAACTGAGTCAGCAGTATGGGGACGTGCTGCAGATC
CGTATTGGCTCCACACCCGTGGTGGTGCTGAGCGGCCTGAACACCATCAAGCAGGCCCTG
GTGAAACAGGGGGATGACTTCAAAGGCCGGCCAGACCTCTACAGCTTCACACTTATCGCT
AATGGCCAGAGCATGACTTTCAACCCAGACTCTGGACCGCTGTGGGCTGCCCGCCGGCGC
CTGGCCCAGAATGCGCTGAAGAGTTTCTCCATAGCCTCAGACCCAACACTGGCATCCTCT
TGCTACTTGGAAGAGCACGTGAGCAAAGAGGCTGAATACTTAATCAGCAAGTTCCAGAAG
CTGATGGCAGAGGTTGGCCACTTCGACCCTTTCAAGTATTTGGTGGTGTCAGTGGCCAAT
GTCATCTGTGCCATATGCTTTGGCAGACGTTATGACCACGATGACCAAGAGCTGCTCAGC
ATAGTCAATCTAAGCAATGAGTTTGGGGAGGTTACTGGTTCTGGATACCCAGCTGACTTC
ATTCCTATCCTCCGTTACCTCCCTAACTCTTCCCTGGATGCCTTCAAGGACTTGAATAAG
AAGTTCTACAGTTTCATGAAGAAGCTAATCAAAGAGCACTACAGGACATTTGAGAAGGGC
CACATCCGGGACATCACAGACAGCCTCATTGAGCATTGTCAGGACAGGAGGCTGGACGAG
AATGCCAATGTCCAGCTCTCAGATGATAAGGTCATTACGATTGTTTTTGACCTCTTTGGA
GCTGGGTTTGACACAATCACAACTGCTATCTCTTGGAGCCTCATGTACCTGGTAACCAAC
CCTAGGATACAGAGAAAGATCCAGGAGGAGTTAGACACAGTGATTGGCAGGGATCGGCAG
CCCCGGCTTTCTGACAGACCTCAGCTGCCCTATCTGGAGGCCTTCATCCTGGAGACCTTC
CGACATTCATCCTTTGTCCCATTCACCATCCCCCACAGCACCATAAGAGATACAAGTCTG
AATGGCTTCTATATCCCCAAGGGACACTGTGTCTTTGTGAACCAGTGGCAGGTTAACCAT
GACCAGGAACTATGGGGTGATCCAAACGAGTTCCGGCCTGAAAGGTTTCTTACCTCCAGT
GGCACTCTGGACAAACACCTGAGTGAGAAGGTCATTCTCTTTGGTTTGGGCAAGCGAAAG
TGCATTGGGGAGACCATTGGCCGACTGGAGGTCTTTCTCTTCCTGGCCATCCTGCTGCAG
CAAATGGAATTTAATGTGTCACCAGGCGAGAAGGTGGATATGACTCCTGCCTATGGGCTG
ACTTTAAAACATGCCCGCTGTGAGCACTTCCAAGTGCAGATGCGGTCTTCTGGTCCTCAG
CATCTCCAGGCTTAG
Chromosome Location
8
Locus
8q24
External Identifiers
ResourceLink
UniProtKB IDP00185
UniProtKB Entry NameCP1A1_RAT
KEGG IDrno:24296
NCBI Gene ID24296
General References
  1. Sogawa K, Gotoh O, Kawajiri K, Fujii-Kuriyama Y: Distinct organization of methylcholanthrene- and phenobarbital-inducible cytochrome P-450 genes in the rat. Proc Natl Acad Sci U S A. 1984 Aug;81(16):5066-70. [Article]
  2. Yabusaki Y, Shimizu M, Murakami H, Nakamura K, Oeda K, Ohkawa H: Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC. Nucleic Acids Res. 1984 Mar 26;12(6):2929-38. [Article]
  3. Hines RN, Levy JB, Conrad RD, Iversen PL, Shen ML, Renli AM, Bresnick E: Gene structure and nucleotide sequence for rat cytochrome P-450c. Arch Biochem Biophys. 1985 Mar;237(2):465-76. [Article]
  4. Cheng KC, Park SS, Krutzsch HC, Grantham PH, Gelboin HV, Friedman FK: Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450. Biochemistry. 1986 May 6;25(9):2397-402. [Article]
  5. Amelizad Z, Narbonne JF, Wolf CR, Robertson LW, Oesch F: Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver. Biochem Pharmacol. 1988 Sep 1;37(17):3245-9. [Article]
  6. Cvrk T, Hodek P, Strobel HW: Identification and characterization of cytochrome P4501A1 amino acid residues interacting with a radiolabeled photoaffinity diazido-benzphetamine analogue. Arch Biochem Biophys. 1996 Jun 1;330(1):142-52. doi: 10.1006/abbi.1996.0236. [Article]
  7. Addya S, Anandatheerthavarada HK, Biswas G, Bhagwat SV, Mullick J, Avadhani NG: Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2. J Cell Biol. 1997 Nov 3;139(3):589-99. [Article]
  8. Cao W, Cao J, Huang J, Yao J, Yan G, Xu H, Yang P: Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods. PLoS One. 2013 Oct 2;8(10):e76399. doi: 10.1371/journal.pone.0076399. eCollection 2013. [Article]

Associated Data

Drug Relations
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