Q86W10 · CP4Z1_HUMAN
- ProteinCytochrome P450 4Z1
- GeneCYP4Z1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids505 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A cytochrome P450 monooxygenase that catalyzes the in-chain oxidation of fatty acids (PubMed:19090726, PubMed:29018033).
Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively (PubMed:19090726, PubMed:29018033).
Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Displays an absolute stereoselectivity in the epoxidation of arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid (EET) enantiomer (PubMed:29018033).
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) (PubMed:19090726, PubMed:29018033).
Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively (PubMed:19090726, PubMed:29018033).
Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Displays an absolute stereoselectivity in the epoxidation of arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid (EET) enantiomer (PubMed:29018033).
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) (PubMed:19090726, PubMed:29018033).
Catalytic activity
- an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 8-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 9-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 10-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 9-hydroxytetradecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 10-hydroxytetradecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 11-hydroxytetradecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 12-hydroxytetradecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]This reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | arachidonic acid 14,15-epoxygenase activity | |
Molecular Function | aromatase activity | |
Molecular Function | fatty acid in-chain hydroxylase activity | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | lauric acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome P450 4Z1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86W10
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Microsome membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MEPSWLQEL | ||||||
Transmembrane | 10-30 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: MAHPFLLLILLCMSLLLFQVI | ||||||
Topological domain | 31-505 | Lumenal | ||||
Sequence: RLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048461 | 393 | in dbSNP:rs28463559 | |||
Sequence: P → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 585 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051864 | 1-505 | Cytochrome P450 4Z1 | |||
Sequence: MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC |
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)59,086
- Last updated2003-06-01 v1
- ChecksumCF23D96739402E86
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY262056 EMBL· GenBank· DDBJ | AAO89257.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358631 EMBL· GenBank· DDBJ | AAQ88994.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292175 EMBL· GenBank· DDBJ | BAF84864.1 EMBL· GenBank· DDBJ | mRNA | ||
AL450996 EMBL· GenBank· DDBJ | CAH71036.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL135960 EMBL· GenBank· DDBJ | CAH71036.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL135960 EMBL· GenBank· DDBJ | CAI19734.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL450996 EMBL· GenBank· DDBJ | CAI19734.1 EMBL· GenBank· DDBJ | Genomic DNA |