Q86W10 · CP4Z1_HUMAN

  • Protein
    Cytochrome P450 4Z1
  • Gene
    CYP4Z1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

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.
    EC:1.14.14.1 (UniProtKB | ENZYME | Rhea)
  • dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 7-hydroxydodecanoate + H+ + H2O + oxidized [NADPH--hemoprotein reductase]
    This reaction proceeds in the forward direction.
    EC:1.14.14.130 (UniProtKB | ENZYME | Rhea)
  • 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

heme (UniProtKB | Rhea| CHEBI:30413 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site452Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionarachidonic acid 14,15-epoxygenase activity
Molecular Functionaromatase activity
Molecular Functionfatty acid in-chain hydroxylase activity
Molecular Functionheme binding
Molecular Functioniron ion binding
Biological Processarachidonic acid metabolic process
Biological Processlauric acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome P450 4Z1
  • EC number
  • Alternative names
    • CYPIVZ1
    • Laurate 7-monooxygenase
      (EC:1.14.14.130
      ) . EC:1.14.14.130 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      CYP4Z1
    • ORF names
      UNQ3060/PRO9882

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q86W10
  • Secondary accessions
    • Q5VVE4

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type II membrane protein
Microsome membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Cytoplasmic
Transmembrane10-30Helical; Signal-anchor for type II membrane protein
Topological domain31-505Lumenal

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_048461393in dbSNP:rs28463559

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000518641-505Cytochrome P450 4Z1

Proteomic databases

PTM databases

Expression

Tissue specificity

Preferentially detected in breast carcinoma tissue and mammary gland, whereas only marginal expression is found in all other tested tissues.

Gene expression databases

    • ENSG00000186160Expressed in male germ line stem cell (sensu Vertebrata) in testis and 93 other cell types or tissues

Organism-specific databases

Interaction

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    505
  • Mass (Da)
    59,086
  • Last updated
    2003-06-01 v1
  • Checksum
    CF23D96739402E86
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp