CP4FB_HUMAN
ID CP4FB_HUMAN Reviewed; 524 AA.
AC Q9HBI6; A0A024R7G0; A8K059; O75254; Q96AQ5;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cytochrome P450 4F11 {ECO:0000303|PubMed:15364545};
DE Short=CYPIVF11;
DE EC=1.14.14.1 {ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:18065749, ECO:0000269|PubMed:24138531};
DE AltName: Full=3-hydroxy fatty acids omega-hydroxylase CYP4F11 {ECO:0000305|PubMed:18065749};
DE AltName: Full=Docosahexaenoic acid omega-hydroxylase {ECO:0000305|PubMed:19932081};
DE EC=1.14.14.79 {ECO:0000269|PubMed:19932081};
DE AltName: Full=Long-chain fatty acid omega-monooxygenase {ECO:0000305|PubMed:19932081};
DE EC=1.14.14.80 {ECO:0000269|PubMed:19932081};
DE AltName: Full=Phylloquinone omega-hydroxylase CYP4F11 {ECO:0000305|PubMed:24138531};
DE EC=1.14.14.78 {ECO:0000269|PubMed:24138531};
GN Name=CYP4F11 {ECO:0000303|PubMed:10964514, ECO:0000312|HGNC:HGNC:13265};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS ARG-276 AND
RP ASN-446.
RC TISSUE=Brain, and Liver;
RX PubMed=10964514; DOI=10.1006/geno.2000.6276;
RA Cui X., Nelson D.R., Strobel H.W.;
RT "A novel human cytochrome P450 4F isoform (CYP4F11): cDNA cloning,
RT expression, and genomic structural characterization.";
RL Genomics 68:161-166(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-276 AND ASN-446.
RC TISSUE=Mammary gland {ECO:0000312|EMBL:BAF82113.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-276.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-276 AND ASN-446.
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=15364545; DOI=10.1016/j.taap.2003.12.033;
RA Kalsotra A., Turman C.M., Kikuta Y., Strobel H.W.;
RT "Expression and characterization of human cytochrome P450 4F11: Putative
RT role in the metabolism of therapeutic drugs and eicosanoids.";
RL Toxicol. Appl. Pharmacol. 199:295-304(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=18065749; DOI=10.1194/jlr.m700450-jlr200;
RA Dhar M., Sepkovic D.W., Hirani V., Magnusson R.P., Lasker J.M.;
RT "Omega oxidation of 3-hydroxy fatty acids by the human CYP4F gene subfamily
RT enzyme CYP4F11.";
RL J. Lipid Res. 49:612-624(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=19932081; DOI=10.1016/j.abb.2009.11.017;
RA Tang Z., Salamanca-Pinzon S.G., Wu Z.L., Xiao Y., Guengerich F.P.;
RT "Human cytochrome P450 4F11: heterologous expression in bacteria,
RT purification, and characterization of catalytic function.";
RL Arch. Biochem. Biophys. 494:86-93(2010).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PATHWAY, AND
RP CHARACTERIZATION OF VARIANT ASN-446.
RX PubMed=24138531; DOI=10.1021/bi401208m;
RA Edson K.Z., Prasad B., Unadkat J.D., Suhara Y., Okano T., Guengerich F.P.,
RA Rettie A.E.;
RT "Cytochrome P450-dependent catabolism of vitamin K: omega-hydroxylation
RT catalyzed by human CYP4F2 and CYP4F11.";
RL Biochemistry 52:8276-8285(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC various endogenous substrates, including fatty acids and their
CC oxygenated derivatives (oxylipins) (PubMed:24138531, PubMed:15364545,
CC PubMed:18065749). Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:15364545,
CC PubMed:18065749, PubMed:24138531). Catalyzes with high efficiency the
CC oxidation of the terminal carbon (omega-oxidation) of 3-hydroxy fatty
CC acids, such as 3-hydroxyhexadecanoic and 3-hydroxyoctadecanoic acids,
CC likely participating in the biosynthesis of long-chain 3-
CC hydroxydicarboxylic acids (PubMed:18065749, PubMed:19932081). Omega-
CC hydroxylates and inactivates phylloquinone (vitamin K1), and
CC menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in
CC blood coagulation (PubMed:24138531). Metabolizes with low efficiciency
CC fatty acids, including (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
CC (arachidonate) and its oxygenated metabolite 8-hydroxyeicosatetraenoic
CC acid (8-HETE) (PubMed:15364545, PubMed:19932081). Catalyzes N- and O-
CC demethylation of drugs such as erythromycin, benzphetamine,
CC ethylmorphine, chlorpromazine, imipramine and verapamil
CC (PubMed:15364545). {ECO:0000269|PubMed:15364545,
CC ECO:0000269|PubMed:18065749, ECO:0000269|PubMed:19932081,
CC ECO:0000269|PubMed:24138531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:15364545, ECO:0000269|PubMed:18065749,
CC ECO:0000269|PubMed:19932081, ECO:0000269|PubMed:24138531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:15364545, ECO:0000305|PubMed:18065749,
CC ECO:0000305|PubMed:24138531};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:19932081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749;
CC Evidence={ECO:0000305|PubMed:19932081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:18065749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948;
CC Evidence={ECO:0000305|PubMed:18065749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.80;
CC Evidence={ECO:0000269|PubMed:19932081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40200;
CC Evidence={ECO:0000305|PubMed:19932081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424;
CC EC=1.14.14.80; Evidence={ECO:0000269|PubMed:19932081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41729;
CC Evidence={ECO:0000305|PubMed:19932081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76624; Evidence={ECO:0000269|PubMed:15364545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000305|PubMed:15364545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 22-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40155, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77015,
CC ChEBI:CHEBI:77016; EC=1.14.14.79;
CC Evidence={ECO:0000269|PubMed:19932081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40156;
CC Evidence={ECO:0000305|PubMed:19932081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 8,20-dihydroxy-(5Z,9E,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:48660, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:90716,
CC ChEBI:CHEBI:90717; Evidence={ECO:0000269|PubMed:15364545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48661;
CC Evidence={ECO:0000305|PubMed:15364545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyhexadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3,16-dihydroxyhexadecanoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39731, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:63904, ChEBI:CHEBI:76613;
CC Evidence={ECO:0000269|PubMed:18065749, ECO:0000269|PubMed:19932081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39732;
CC Evidence={ECO:0000305|PubMed:18065749, ECO:0000305|PubMed:19932081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyoctadecanoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3,18-dihydroxyoctadecanoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39735, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:76614, ChEBI:CHEBI:76615;
CC Evidence={ECO:0000269|PubMed:18065749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39736;
CC Evidence={ECO:0000305|PubMed:18065749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + phylloquinone + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + omega-hydroxyphylloquinone + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:41516, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:18067, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:78276; EC=1.14.14.78;
CC Evidence={ECO:0000269|PubMed:24138531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41517;
CC Evidence={ECO:0000305|PubMed:24138531};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=menaquinone-4 + O2 + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + omega-hydroxymenaquinone-4 + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:41520, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:78277, ChEBI:CHEBI:78278; EC=1.14.14.78;
CC Evidence={ECO:0000269|PubMed:24138531};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41521;
CC Evidence={ECO:0000305|PubMed:24138531};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q02928};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for hexadecanoic acid {ECO:0000269|PubMed:19932081};
CC KM=85 uM for (9Z)-octadecenoic acid (oleate)
CC {ECO:0000269|PubMed:19932081};
CC KM=80 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
CC {ECO:0000269|PubMed:19932081};
CC KM=48 uM for (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoic acid
CC {ECO:0000269|PubMed:19932081};
CC KM=74 uM for 3-hydroxyhexadecanoic acid
CC {ECO:0000269|PubMed:19932081};
CC KM=105.8 uM for 3-hydroxyhexadecanoic acid
CC {ECO:0000269|PubMed:18065749};
CC KM=53.5 uM for 3-hydroxyoctadecanoic acid
CC {ECO:0000269|PubMed:18065749};
CC KM=2.4 uM for menaquinone-4 (MK-4) {ECO:0000269|PubMed:24138531};
CC KM=125 uM for erythromycin {ECO:0000269|PubMed:15364545};
CC Vmax=830 pmol/min/ng enzyme with erythromycin as substrate
CC {ECO:0000269|PubMed:15364545};
CC Note=kcat is 0.088 min(-1) with menaquinone-4 (MK-4) as substrate
CC (PubMed:24138531). kcat is 1.8 min(-1) with hexadecanoic acid as
CC substrate. kcat is 1.0 min(-1) with (9Z)-octadecenoic acid as
CC substrate. kcat is 0.54 min(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoic
CC acid (arachidonate) as substrate. kcat is 0.35 min(-1) with
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoic acid as substrate. kcat is
CC 27.5 min(-1) with 3-hydroxyhexadecanoic acid as substrate
CC (PubMed:19932081). {ECO:0000269|PubMed:19932081,
CC ECO:0000269|PubMed:24138531};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000269|PubMed:15364545}.
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:15364545}.
CC -!- PATHWAY: Cofactor degradation; phylloquinone degradation.
CC {ECO:0000269|PubMed:24138531}.
CC -!- PATHWAY: Xenobiotic degradation. {ECO:0000269|PubMed:15364545}.
CC -!- INTERACTION:
CC Q9HBI6; Q14696: MESD; NbExp=3; IntAct=EBI-3924028, EBI-6165891;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18065749}; Single-pass membrane protein
CC {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:18065749};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in human liver, followed by
CC kidney, heart, and skeletal muscle. {ECO:0000269|PubMed:10964514,
CC ECO:0000269|PubMed:24138531}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF236085; AAG15889.1; -; mRNA.
DR EMBL; AK289424; BAF82113.1; -; mRNA.
DR EMBL; AC005336; AAC27731.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC020950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84512.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84513.1; -; Genomic_DNA.
DR EMBL; BC016853; AAH16853.1; -; mRNA.
DR CCDS; CCDS12337.1; -.
DR RefSeq; NP_001122404.1; NM_001128932.1.
DR RefSeq; NP_067010.3; NM_021187.3.
DR AlphaFoldDB; Q9HBI6; -.
DR SMR; Q9HBI6; -.
DR BioGRID; 121790; 13.
DR IntAct; Q9HBI6; 2.
DR STRING; 9606.ENSP00000384588; -.
DR ChEMBL; CHEMBL4295949; -.
DR SwissLipids; SLP:000000470; -.
DR iPTMnet; Q9HBI6; -.
DR PhosphoSitePlus; Q9HBI6; -.
DR BioMuta; CYP4F11; -.
DR DMDM; 296439388; -.
DR EPD; Q9HBI6; -.
DR jPOST; Q9HBI6; -.
DR MassIVE; Q9HBI6; -.
DR MaxQB; Q9HBI6; -.
DR PaxDb; Q9HBI6; -.
DR PeptideAtlas; Q9HBI6; -.
DR PRIDE; Q9HBI6; -.
DR ProteomicsDB; 81562; -.
DR Antibodypedia; 2634; 161 antibodies from 29 providers.
DR DNASU; 57834; -.
DR Ensembl; ENST00000248041.12; ENSP00000248041.6; ENSG00000171903.17.
DR Ensembl; ENST00000402119.9; ENSP00000384588.2; ENSG00000171903.17.
DR GeneID; 57834; -.
DR KEGG; hsa:57834; -.
DR MANE-Select; ENST00000402119.9; ENSP00000384588.2; NM_021187.4; NP_067010.3.
DR UCSC; uc002nbt.3; human.
DR CTD; 57834; -.
DR DisGeNET; 57834; -.
DR GeneCards; CYP4F11; -.
DR HGNC; HGNC:13265; CYP4F11.
DR HPA; ENSG00000171903; Tissue enhanced (intestine, liver).
DR MIM; 611517; gene.
DR neXtProt; NX_Q9HBI6; -.
DR OpenTargets; ENSG00000171903; -.
DR PharmGKB; PA27120; -.
DR VEuPathDB; HostDB:ENSG00000171903; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000164421; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q9HBI6; -.
DR OMA; ELYPMMW; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9HBI6; -.
DR TreeFam; TF105088; -.
DR PathwayCommons; Q9HBI6; -.
DR Reactome; R-HSA-211935; Fatty acids.
DR Reactome; R-HSA-211958; Miscellaneous substrates.
DR Reactome; R-HSA-211979; Eicosanoids.
DR Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR SignaLink; Q9HBI6; -.
DR UniPathway; UPA00382; -.
DR UniPathway; UPA00383; -.
DR UniPathway; UPA01054; -.
DR BioGRID-ORCS; 57834; 76 hits in 1069 CRISPR screens.
DR ChiTaRS; CYP4F11; human.
DR GeneWiki; CYP4F11; -.
DR GenomeRNAi; 57834; -.
DR Pharos; Q9HBI6; Tbio.
DR PRO; PR:Q9HBI6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HBI6; protein.
DR Bgee; ENSG00000171903; Expressed in right lobe of liver and 102 other tissues.
DR ExpressionAtlas; Q9HBI6; baseline and differential.
DR Genevisible; Q9HBI6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005504; F:fatty acid binding; IDA:BHF-UCL.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; TAS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0036101; P:leukotriene B4 catabolic process; IBA:GO_Central.
DR GO; GO:0042361; P:menaquinone catabolic process; IDA:UniProtKB.
DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; IDA:UniProtKB.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042376; P:phylloquinone catabolic process; IDA:UniProtKB.
DR GO; GO:0042377; P:vitamin K catabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid metabolism; Heme; Iron; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="Cytochrome P450 4F11"
FT /id="PRO_0000051856"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P24464"
FT BINDING 468
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P24464"
FT VARIANT 146
FT /note="R -> C (in dbSNP:rs57519667)"
FT /id="VAR_060265"
FT VARIANT 276
FT /note="C -> R (in dbSNP:rs8104361)"
FT /evidence="ECO:0000269|PubMed:10964514,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_060266"
FT VARIANT 446
FT /note="D -> N (does not affect enzyme activity;
FT dbSNP:rs1060463)"
FT /evidence="ECO:0000269|PubMed:10964514,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:24138531"
FT /id="VAR_071198"
FT CONFLICT 458
FT /note="F -> L (in Ref. 2; BAF82113)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="T -> I (in Ref. 1; AAG15889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 60146 MW; 8B0F14C52E657CB2 CRC64;
MPQLSLSWLG LGPVAASPWL LLLLVGGSWL LARVLAWTYT FYDNCRRLQC FPQPPKQNWF
WGHQGLVTPT EEGMKTLTQL VTTYPQGFKL WLGPTFPLLI LCHPDIIRPI TSASAAVAPK
DMIFYGFLKP WLGDGLLLSG GDKWSRHRRM LTPAFHFNIL KPYMKIFNKS VNIMHDKWQR
LASEGSARLD MFEHISLMTL DSLQKCVFSF ESNCQEKPSE YIAAILELSA FVEKRNQQIL
LHTDFLYYLT PDGQRFRRAC HLVHDFTDAV IQERRCTLPT QGIDDFLKNK AKSKTLDFID
VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWV LYHLAKHPEY QEQCRQEVQE
LLKDREPIEI EWDDLAQLPF LTMCIKESLR LHPPVPVISR CCTQDFVLPD GRVIPKGIVC
LINIIGIHYN PTVWPDPEVY DPFRFDQENI KERSPLAFIP FSAGPRNCIG QAFAMAEMKV
VLALTLLHFR ILPTHTEPRR KPELILRAEG GLWLRVEPLG ANSQ
