ID CP4X1_RAT Reviewed; 507 AA.
AC Q8K4D6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 128.
DE RecName: Full=Cytochrome P450 4X1 {ECO:0000303|PubMed:12176035};
DE EC=1.14.14.- {ECO:0000250|UniProtKB:Q8N118};
DE AltName: Full=CYPIVX1;
GN Name=Cyp4x1 {ECO:0000303|PubMed:12176035, ECO:0000312|RGD:628719};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12176035; DOI=10.1016/s0006-291x(02)00918-x;
RA Bylund J., Zhang C., Harder D.R.;
RT "Identification of a novel cytochrome P450, CYP4X1, with unique
RT localization specific to the brain.";
RL Biochem. Biophys. Res. Commun. 296:677-684(2002).
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:0000250|UniProtKB:Q6A152}; Single-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q6A152};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, mainly in
CC neurons in different regions, including brain stem, hippocampus, cortex
CC and cerebellum. Also expressed in cerebral vasculature. Not detected in
CC kidney, nor liver. {ECO:0000269|PubMed:12176035}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF439343; AAM73782.1; -; mRNA.
DR PIR; JC7883; JC7883.
DR RefSeq; NP_663708.1; NM_145675.1.
DR AlphaFoldDB; Q8K4D6; -.
DR SMR; Q8K4D6; -.
DR STRING; 10116.ENSRNOP00000011985; -.
DR PhosphoSitePlus; Q8K4D6; -.
DR PaxDb; 10116-ENSRNOP00000011985; -.
DR Ensembl; ENSRNOT00000011985.3; ENSRNOP00000011985.1; ENSRNOG00000043513.2.
DR Ensembl; ENSRNOT00055054312; ENSRNOP00055044901; ENSRNOG00055031360.
DR Ensembl; ENSRNOT00060051160; ENSRNOP00060042568; ENSRNOG00060029479.
DR Ensembl; ENSRNOT00065025865; ENSRNOP00065020351; ENSRNOG00065015575.
DR GeneID; 246767; -.
DR KEGG; rno:246767; -.
DR UCSC; RGD:628719; rat.
DR AGR; RGD:628719; -.
DR CTD; 260293; -.
DR RGD; 628719; Cyp4x1.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000160927; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q8K4D6; -.
DR OMA; VLHQYTE; -.
DR OrthoDB; 1611592at2759; -.
DR PhylomeDB; Q8K4D6; -.
DR TreeFam; TF105088; -.
DR PRO; PR:Q8K4D6; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000043513; Expressed in frontal cortex and 5 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0062189; F:anandamide 14,15 epoxidase activity; ISS:UniProtKB.
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 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.
PE 2: Evidence at transcript 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_0000051863"
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"
SQ SEQUENCE 507 AA; 58574 MW; E19D76B9811B8223 CRC64;
MEASWLENRW ARPLHLALVF CLALVLMQAV KLYLRRQRLL RDLRPFPGPT AHWLLGHQKF
LQEDNMEKLD EIVKEYPCAF PCWVGPFQAF FYIYDPDYAK IFLSRTDPKT QYLHQLMTPF
LGRGLLNLDG PRWFQHRCLL TPAFHQDILK PCVDMMAHSV NMMLDKWEKT WTTQETTIEV
FEHINLMTLD IIMKCAFGQE TNCQINGTYE SYVKATFELG EIISSRLYNF WHHHDIIFKL
SPKGHCFQEL GKVIHQCTEK IIQDRKKTLK DQVNQDDTQT SQNFLDIVLS AQAGDEKAFS
DADLRSEVNT FMWAGHDASA ASISWLLYCL ALNPEHQDRC RTEIRSILGD GSSITWEQLD
EIPYTTMCIK ETLRLIPPIP SISRELSKPL TLPDGHSLPA GMTVVLSIWG LHHNPAVWKD
PKVFDPLRFT KENSEQRHPC AFLPFSSGPR NCIGQQFAML ELKVAIALTL LRFRVAADLT
RPPAFSSHTV LRPKHGIYLH LKKLPEC
//
