CYP1A1
Cytochrome P450 1A1
Also known as: CP11, CP1A1_HUMAN, CYP1, P1-450, P450-C, P450DX
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P04798
- Gene
- CYP1A1
- Ensembl
- ENSG00000140465
- Chromosome
- 15
- Canonical length
- 512 aa
- Protein class
- Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
OverviewNCBI Gene
This gene, CYP1A1, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. The gene has been associated with lung cancer risk. A related family member, CYP1A2, is located approximately 25 kb away from CYP1A1 on chromosome 15. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jan 2016]
Canonical amino-acid sequenceUniProt
512 residues, UniProt reviewed canonical sequence.
>P04798|CYP1A1
1 MLFPISMSAT EFLLASVIFC LVFWVIRASR PQVPKGLKNP PGPWGWPLIG HMLTLGKNPH
61 LALSRMSQQY GDVLQIRIGS TPVVVLSGLD TIRQALVRQG DDFKGRPDLY TFTLISNGQS
121 MSFSPDSGPV WAARRRLAQN GLKSFSIASD PASSTSCYLE EHVSKEAEVL ISTLQELMAG
181 PGHFNPYRYV VVSVTNVICA ICFGRRYDHN HQELLSLVNL NNNFGEVVGS GNPADFIPIL
241 RYLPNPSLNA FKDLNEKFYS FMQKMVKEHY KTFEKGHIRD ITDSLIEHCQ EKQLDENANV
301 QLSDEKIINI VLDLFGAGFD TVTTAISWSL MYLVMNPRVQ RKIQEELDTV IGRSRRPRLS
361 DRSHLPYMEA FILETFRHSS FVPFTIPHST TRDTSLKGFY IPKGRCVFVN QWQINHDQKL
421 WVNPSEFLPE RFLTPDGAID KVLSEKVIIF GMGKRKCIGE TIARWEVFLF LAILLQRVEF
481 SVPLGVKVDM TPIYGLTMKH ACCEHFQMQL RSLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CYP1A1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.24
- Highest tissue expression
- 62 nTPM
Expression across tissuesHPA
Tissue
- liver: 62 nTPM
- urinary bladder: 60 nTPM
- small intestine: 19 nTPM
- adipose tissue: 18 nTPM
- breast: 14 nTPM
- skin: 13 nTPM
Single-cell type
- epididymal clear cells: 51 nCPM
- urothelial cells: 42 nCPM
- hepatocytes: 14 nCPM
- vascular endothelial cells: 14 nCPM
- endometrial glandular cells: 10 nCPM
- endometrial secretory cells: 8.8 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- hypothalamus: 1 nTPM
- midbrain: 0.9 nTPM
- pons: 0.8 nTPM
- medulla oblongata: 0.6 nTPM
- cerebral cortex: 0.5 nTPM
- hippocampal formation: 0.5 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.78
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.36
- DepMap mean gene effect
- -0.02
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- 9-cis-retinoic acid biosynthetic process
- amine metabolic process
- camera-type eye development
- cellular response to copper ion
- coumarin metabolic process
- digestive tract development
- epoxygenase P450 pathway
- estrogen metabolic process
- fatty acid metabolic process
- flavonoid metabolic process
- hepatocyte differentiation
- hydrogen peroxide biosynthetic process
- lipid hydroxylation
- long-chain fatty acid biosynthetic process
- long-chain fatty acid metabolic process
- maternal process involved in parturition
- nitric oxide metabolic process
- omega-hydroxylase P450 pathway
- phenol-containing compound metabolic process
- porphyrin-containing compound metabolic process
- positive regulation of G1/S transition of mitotic cell cycle
- response to 2,3,7,8-tetrachlorodibenzodioxine
- response to 3-methylcholanthrene
- response to Aroclor 1254
- response to arsenic-containing substance
- response to food
- response to genistein
- 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 vitamin A
- retinol metabolic process
- steroid biosynthetic process
- steroid catabolic process
- steroid metabolic process
- tissue remodeling
- toxin metabolic process
- vitamin D metabolic process
- xenobiotic catabolic process
- xenobiotic metabolic process
- dibenzo-p-dioxin catabolic process
- ethylene metabolic process
- insecticide metabolic process
- response to diphenyl ether
Molecular functions
- arachidonate monooxygenase activity
- demethylase activity
- enzyme binding
- estrogen 16-alpha-hydroxylase activity
- estrogen 2-hydroxylase activity
- heme binding
- Hsp70 protein binding
- Hsp90 protein binding
- hydroperoxy icosatetraenoate dehydratase activity
- iron ion binding
- long-chain fatty acid omega-1 hydroxylase activity
- long-chain fatty acid omega-hydroxylase activity
- monooxygenase activity
- oxidoreductase activity
- 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
- oxygen binding
- steroid hydroxylase activity
- vitamin D 24-hydroxylase activity
- flavonoid 3'-monooxygenase activity
- oxidoreductase activity, acting on diphenols and related substances as donors
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of CYP1A1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
- HSP90
- PGRMC1
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads CYP1A1 as an antibody target. Whether an autoantibody or antibody against CYP1A1 could matter depends on whether native CYP1A1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CYP1A1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label CYP1A1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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