Protein: Cytochrome P450 4F2 (EC 1.14.14.1) (20-hydroxyeicosatetraenoic acid synthase) (20-HETE synthase) (Arachidonic acid omega-hydroxylase) (CYPIVF2) (Cytochrome P450-LTB-omega) (Docosahexaenoic acid omega-hydroxylase) (EC 1.14.14.79) (Leukotriene-B(4) 20-monooxygenase 1) (Leukotriene-B(4) omega-hydroxylase 1) (EC 1.14.14.94) (Phylloquinone omega-hydroxylase CYP4F2) (EC 1.14.14.78) (P78329)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids 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 predominantly the oxidation of the terminal carbon (omega-oxidation) of long- and very long-chain fatty acids. Displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs). Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Plays a role in the oxidative inactivation of eicosanoids, including both pro-inflammatory and anti-inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs. Catalyzes omega-hydroxylation of 3-hydroxy fatty acids. Converts monoepoxides of linoleic acid leukotoxin and isoleukotoxin to omega-hydroxylated metabolites. Contributes to the degradation of very long-chain fatty acids (VLCFAs) by catalyzing successive omega-oxidations and chain shortening. Plays an important role in vitamin metabolism by chain shortening. Catalyzes omega-hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma-tocopherols over alpha-tocopherols, thus promoting retention of alpha-tocopherols in tissues. Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:19297519, ECO:0000269|PubMed:24138531, ECO:0000269|PubMed:8026587}; Peripheral membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20861217}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 4F3
- Cytochrome P450 2C9
- Vitamin K epoxide reductase complex subunit 1
- Cytochrome P450 2C19
- Cytochrome P450 2C8
- Cytochrome P450 2J2))
- Cytochrome P450 2B6
- Cytochrome P450 2E1
- Prostaglandin G/H synthase 2
- Cytochrome P450 2U1
Sequence:
MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS