CP4Z1_HUMAN
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 03-AUG-2022, entry version 157.
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, ECO:0000312|HGNC:HGNC:20583};
GN 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 [NADPH--
CC hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49856, 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: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}.
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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; Q86W10; -.
DR PeptideAtlas; Q86W10; -.
DR PRIDE; Q86W10; -.
DR ProteomicsDB; 70100; -.
DR Antibodypedia; 32850; 149 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 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; HIAQNSC; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q86W10; -.
DR TreeFam; TF105088; -.
DR PathwayCommons; Q86W10; -.
DR BioGRID-ORCS; 199974; 18 hits in 1064 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 calcaneal tendon and 91 other tissues.
DR Genevisible; Q86W10; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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
