CP4X1_MOUSE
ID CP4X1_MOUSE Reviewed; 507 AA.
AC Q6A152; Q2HJC6; Q8BYS0;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytochrome P450 4X1 {ECO:0000303|PubMed:16478468};
DE EC=1.14.14.- {ECO:0000250|UniProtKB:Q8N118};
DE AltName: Full=CYPIVX1;
GN Name=Cyp4x1 {ECO:0000303|PubMed:16478468, ECO:0000312|MGI:MGI:1932403};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=129; TISSUE=Brain;
RX PubMed=16478468; DOI=10.1111/j.1742-4658.2006.05119.x;
RA Al-Anizy M., Horley N.J., Kuo C.W., Gillett L.C., Laughton C.A.,
RA Kendall D., Barrett D.A., Parker T., Bell D.R.;
RT "Cytochrome P450 Cyp4x1 is a major P450 protein in mouse brain.";
RL FEBS J. 273:936-947(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-507.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-507.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: A cytochrome P450 monooxygenase that selectively catalyzes
CC the epoxidation of the last double bond of the arachidonoyl moiety of
CC anandamide, potentially modulating endocannabinoid signaling. Has no
CC hydroxylase activity toward various fatty acids, steroids and
CC prostaglandins. 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).
CC {ECO:0000250|UniProtKB:Q8N118}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced
CC [NADPH--hemoprotein reductase] = H(+) + H2O + N-(14,15-epoxy-
CC 5Z,8Z,11Z-eicosatrienoyl)-ethanolamine + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53148, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:136991; Evidence={ECO:0000250|UniProtKB:Q8N118};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53149;
CC Evidence={ECO:0000250|UniProtKB:Q8N118};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:16478468}; Single-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:16478468};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and aorta. In the brain,
CC expressed in the Purkinje cells of the cerebellum, pyramidal neurons in
CC the dentate gyrus of the hippocampus, cortical forebrain neurons and
CC those of brain stem nuclei (at protein level). In addition to neurons,
CC also expressed in cerebral vascular endothelial cells (at protein
CC level). Also expressed in epithelial cells of the choroid plexus (at
CC protein level). Hardly detectable in heart, lung, kidney and spleen.
CC {ECO:0000269|PubMed:16478468}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ786769; CAH10751.1; -; mRNA.
DR EMBL; AL645473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113125; AAI13126.1; -; mRNA.
DR EMBL; AK038526; BAC30028.1; -; mRNA.
DR CCDS; CCDS18488.1; -.
DR RefSeq; NP_001003947.1; NM_001003947.1.
DR AlphaFoldDB; Q6A152; -.
DR SMR; Q6A152; -.
DR STRING; 10090.ENSMUSP00000059545; -.
DR iPTMnet; Q6A152; -.
DR PhosphoSitePlus; Q6A152; -.
DR EPD; Q6A152; -.
DR jPOST; Q6A152; -.
DR MaxQB; Q6A152; -.
DR PaxDb; Q6A152; -.
DR PRIDE; Q6A152; -.
DR ProteomicsDB; 285283; -.
DR Antibodypedia; 32842; 217 antibodies from 25 providers.
DR DNASU; 81906; -.
DR Ensembl; ENSMUST00000051400; ENSMUSP00000059545; ENSMUSG00000047155.
DR GeneID; 81906; -.
DR KEGG; mmu:81906; -.
DR UCSC; uc008uep.1; mouse.
DR CTD; 260293; -.
DR MGI; MGI:1932403; Cyp4x1.
DR VEuPathDB; HostDB:ENSMUSG00000047155; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000160927; -.
DR InParanoid; Q6A152; -.
DR OMA; SDQRHPY; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q6A152; -.
DR TreeFam; TF105088; -.
DR BioGRID-ORCS; 81906; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q6A152; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6A152; protein.
DR Bgee; ENSMUSG00000047155; Expressed in facial nucleus and 88 other tissues.
DR ExpressionAtlas; Q6A152; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0062189; F:anandamide 14,15 epoxidase activity; ISS:UniProtKB.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; ISO:MGI.
DR GO; GO:0052722; F:fatty acid in-chain hydroxylase activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Cytochrome P450 4X1"
FT /id="PRO_0000421683"
FT TRANSMEM 14..34
FT /note="Helical"
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 CONFLICT 9
FT /note="R -> G (in Ref. 4; BAC30028)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="M -> T (in Ref. 3; AAI13126)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="T -> A (in Ref. 3; AAI13126)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="L -> P (in Ref. 3; AAI13126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 58557 MW; 11A2FAAA650F705A CRC64;
MEASWLETRW ARPLHLALVF CLALVLMQAM KLYLRRQRLL RDLSPFPGPP AHWLLGHQKF
LQEDNMETLD EIVKKHPCAF PCWVGPFQAF FYIYDPDYAK IFLSRTDPKM QYLHQLLTPC
IGRGLLNLDG PRWFQHRCLL TPAFHQDILK PCVDTMAHSV KVMLDKWEKM WTTQETTIEV
FEHINLMTLD IIMKCAFGQE TNCQINGTYE SYVKATFELG EIISSRLYNF WHHHDIIFKL
SPKGHCFQEL GKVIHQYTEK IIQDRKKILK NQVKQDDTQT SQIFLDIVLS AQAEDERAFS
DADLRAEVNT FMWAGHDASA ASISWLLYCL ALNPEHQDRC RTEIRSILGD GSSITWEQLD
EMSYTTMCIK ETLRLIPPVP SISRELSKPL TLPDGHSLPA GMTVVLSIWG LHHNPAVWND
PKVFDPLRFT KENSDQRHPC AFLPFSSGPR NCIGQQFAML ELKVAIALIL LHFQVAPDLT
RPPAFSSHTV LRPKHGIYLH LKKLLEC
