ID CP4Z1_HUMAN Reviewed; 505 AA. AC Q86W10; Q5VVE4; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 165. DE RecName: Full=Cytochrome P450 4Z1 {ECO:0000303|PubMed:29018033}; DE EC=1.14.14.1 {ECO:0000269|PubMed:19090726, ECO:0000269|PubMed:29018033}; DE AltName: Full=CYPIVZ1; DE AltName: Full=Laurate 7-monooxygenase {ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; DE EC=1.14.14.130 {ECO:0000269|PubMed:19090726, ECO:0000269|PubMed:29018033}; GN Name=CYP4Z1 {ECO:0000303|PubMed:19090726, GN ECO:0000312|HGNC:HGNC:20583}; ORFNames=UNQ3060/PRO9882; 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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15059886; DOI=10.1158/0008-5472.can-03-0849; RA Rieger M.A., Ebner R., Bell D.R., Kiessling A., Rohayem J., Schmitz M., RA Temme A., Rieber E.P., Weigle B.; RT "Identification of a novel mammary-restricted cytochrome P450, CYP4Z1, with RT overexpression in breast carcinoma."; RL Cancer Res. 64:2357-2364(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19090726; DOI=10.1515/bc.2009.030; RA Zoellner A., Dragan C.A., Pistorius D., Mueller R., Bode H.B., Peters F.T., RA Maurer H.H., Bureik M.; RT "Human CYP4Z1 catalyzes the in-chain hydroxylation of lauric acid and RT myristic acid."; RL Biol. Chem. 390:313-317(2009). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29018033; DOI=10.1124/dmd.117.078188; RA McDonald M.G., Ray S., Amorosi C.J., Sitko K.A., Kowalski J.P., Paco L., RA Nath A., Gallis B., Totah R.A., Dunham M.J., Fowler D.M., Rettie A.E.; RT "Expression and Functional Characterization of Breast Cancer-Associated RT Cytochrome P450 4Z1 in Saccharomyces cerevisiae."; RL Drug Metab. Dispos. 45:1364-1371(2017). CC -!- FUNCTION: A cytochrome P450 monooxygenase that catalyzes the in-chain CC oxidation of fatty acids (PubMed:19090726, PubMed:29018033). Catalyzes CC the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and CC myristic acids predominantly at the omega-4 and omega-2 positions, CC respectively (PubMed:19090726, PubMed:29018033). Catalyzes the CC epoxidation of double bonds of polyunsaturated fatty acids (PUFA). CC Displays an absolute stereoselectivity in the epoxidation of CC arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid CC (EET) enantiomer (PubMed:29018033). Mechanistically, uses molecular CC oxygen inserting one oxygen atom into a substrate, and reducing the CC second into a water molecule, with two electrons provided by NADPH via CC cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) CC (PubMed:19090726, PubMed:29018033). {ECO:0000269|PubMed:19090726, CC ECO:0000269|PubMed:29018033}. 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:19090726, ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; CC Evidence={ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 7- CC hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:45084, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:84921; EC=1.14.14.130; CC Evidence={ECO:0000269|PubMed:19090726, ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45085; CC Evidence={ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 8- CC hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66888, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167541; Evidence={ECO:0000269|PubMed:19090726, CC ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66889; CC Evidence={ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 9- CC hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66872, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167543; Evidence={ECO:0000269|PubMed:19090726, CC ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66873; CC Evidence={ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = CC 10-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66892, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167542; Evidence={ECO:0000269|PubMed:19090726, CC ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66893; CC Evidence={ECO:0000305|PubMed:19090726, ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = CC 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:76628; Evidence={ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; CC Evidence={ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = CC 9-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66916, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167544; Evidence={ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66917; CC Evidence={ECO:0000305|PubMed:29018033}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = CC 10-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66880, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167545; Evidence={ECO:0000269|PubMed:19090726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66881; CC Evidence={ECO:0000305|PubMed:19090726}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = CC 11-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66884, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167547; Evidence={ECO:0000269|PubMed:19090726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66885; CC Evidence={ECO:0000305|PubMed:19090726}; CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = CC 12-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:66876, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:167546; Evidence={ECO:0000269|PubMed:19090726}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66877; CC Evidence={ECO:0000305|PubMed:19090726}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced CC [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)- CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein CC reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA- CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:131964; Evidence={ECO:0000269|PubMed:29018033}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857; CC Evidence={ECO:0000305|PubMed:29018033}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:Q02928}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:15059886}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:15059886}. Microsome membrane CC {ECO:0000269|PubMed:15059886}; Single-pass type II membrane protein CC {ECO:0000269|PubMed:15059886}. CC -!- TISSUE SPECIFICITY: Preferentially detected in breast carcinoma tissue CC and mammary gland, whereas only marginal expression is found in all CC other tested tissues. {ECO:0000269|PubMed:15059886}. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY262056; AAO89257.1; -; mRNA. DR EMBL; AY358631; AAQ88994.1; -; mRNA. DR EMBL; AK292175; BAF84864.1; -; mRNA. DR EMBL; AL450996; CAH71036.1; -; Genomic_DNA. DR EMBL; AL135960; CAH71036.1; JOINED; Genomic_DNA. DR EMBL; AL135960; CAI19734.1; -; Genomic_DNA. DR EMBL; AL450996; CAI19734.1; JOINED; Genomic_DNA. DR CCDS; CCDS545.1; -. DR RefSeq; NP_835235.1; NM_178134.2. DR AlphaFoldDB; Q86W10; -. DR SMR; Q86W10; -. DR STRING; 9606.ENSP00000334246; -. DR BindingDB; Q86W10; -. DR ChEMBL; CHEMBL4523375; -. DR GuidetoPHARMACOLOGY; 1352; -. DR iPTMnet; Q86W10; -. DR PhosphoSitePlus; Q86W10; -. DR BioMuta; CYP4Z1; -. DR DMDM; 48428052; -. DR EPD; Q86W10; -. DR jPOST; Q86W10; -. DR MassIVE; Q86W10; -. DR PaxDb; 9606-ENSP00000334246; -. DR PeptideAtlas; Q86W10; -. DR ProteomicsDB; 70100; -. DR Antibodypedia; 32850; 168 antibodies from 26 providers. DR DNASU; 199974; -. DR Ensembl; ENST00000334194.4; ENSP00000334246.3; ENSG00000186160.5. DR GeneID; 199974; -. DR KEGG; hsa:199974; -. DR MANE-Select; ENST00000334194.4; ENSP00000334246.3; NM_178134.3; NP_835235.1. DR UCSC; uc001cqu.2; human. DR AGR; HGNC:20583; -. DR CTD; 199974; -. DR DisGeNET; 199974; -. DR GeneCards; CYP4Z1; -. DR HGNC; HGNC:20583; CYP4Z1. DR HPA; ENSG00000186160; Tissue enhanced (breast). DR MIM; 618953; gene. DR neXtProt; NX_Q86W10; -. DR OpenTargets; ENSG00000186160; -. DR PharmGKB; PA134941057; -. DR VEuPathDB; HostDB:ENSG00000186160; -. DR eggNOG; KOG0157; Eukaryota. DR GeneTree; ENSGT00940000160927; -. DR HOGENOM; CLU_001570_5_1_1; -. DR InParanoid; Q86W10; -. DR OMA; LHHNDLV; -. DR OrthoDB; 1611592at2759; -. DR PhylomeDB; Q86W10; -. DR TreeFam; TF105088; -. DR PathwayCommons; Q86W10; -. DR BioGRID-ORCS; 199974; 18 hits in 1142 CRISPR screens. DR GeneWiki; CYP4Z1; -. DR GenomeRNAi; 199974; -. DR Pharos; Q86W10; Tchem. DR PRO; PR:Q86W10; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q86W10; Protein. DR Bgee; ENSG00000186160; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 93 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IDA:UniProtKB. DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC. DR GO; GO:0052722; F:fatty acid in-chain hydroxylase activity; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0048252; P:lauric acid metabolic process; IDA:UniProtKB. DR CDD; cd20678; CYP4B-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24291:SF63; CYTOCHROME P450 4X1-RELATED; 1. DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. DR Genevisible; Q86W10; HS. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Fatty acid metabolism; Heme; Iron; Lipid metabolism; KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..505 FT /note="Cytochrome P450 4Z1" FT /id="PRO_0000051864" FT TOPO_DOM 1..9 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 10..30 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 31..505 FT /note="Lumenal" FT /evidence="ECO:0000255" FT BINDING 452 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" FT VARIANT 393 FT /note="P -> L (in dbSNP:rs28463559)" FT /id="VAR_048461" SQ SEQUENCE 505 AA; 59086 MW; CF23D96739402E86 CRC64; MEPSWLQELM AHPFLLLILL CMSLLLFQVI RLYQRRRWMI RALHLFPAPP AHWFYGHKEF YPVKEFEVYH KLMEKYPCAV PLWVGPFTMF FSVHDPDYAK ILLKRQDPKS AVSHKILESW VGRGLVTLDG SKWKKHRQIV KPGFNISILK IFITMMSESV RMMLNKWEEH IAQNSRLELF QHVSLMTLDS IMKCAFSHQG SIQLDSTLDS YLKAVFNLSK ISNQRMNNFL HHNDLVFKFS SQGQIFSKFN QELHQFTEKV IQDRKESLKD KLKQDTTQKR RWDFLDILLS AKSENTKDFS EADLQAEVKT FMFAGHDTTS SAISWILYCL AKYPEHQQRC RDEIRELLGD GSSITWEHLS QMPYTTMCIK ECLRLYAPVV NISRLLDKPI TFPDGRSLPA GITVFINIWA LHHNPYFWED PQVFNPLRFS RENSEKIHPY AFIPFSAGLR NCIGQHFAII ECKVAVALTL LRFKLAPDHS RPPQPVRQVV LKSKNGIHVF AKKVC //