ID   C36A1_CAEEL             Reviewed;         493 AA.
AC   P90771; O02645;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Probable cytochrome P450 CYP36A1;
DE            EC=1.14.-.-;
GN   Name=cyp-36A1; Synonyms=cyp36a1; ORFNames=C34B7.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       They oxidize a variety of structurally unrelated compounds, including
CC       steroids, fatty acids, and xenobiotics.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Z83220; CAB05702.1; -; Genomic_DNA.
DR   PIR; T19695; T19695.
DR   RefSeq; NP_492267.1; NM_059866.7.
DR   AlphaFoldDB; P90771; -.
DR   SMR; P90771; -.
DR   BioGRID; 48024; 1.
DR   DIP; DIP-25137N; -.
DR   FunCoup; P90771; 9.
DR   IntAct; P90771; 1.
DR   STRING; 6239.C34B7.3.1; -.
DR   PaxDb; 6239-C34B7.3.1; -.
DR   EnsemblMetazoa; C34B7.3.1; C34B7.3.1; WBGene00007913.
DR   GeneID; 183193; -.
DR   KEGG; cel:CELE_C34B7.3; -.
DR   UCSC; C34B7.3; c. elegans.
DR   AGR; WB:WBGene00007913; -.
DR   CTD; 183193; -.
DR   WormBase; C34B7.3; CE08567; WBGene00007913; cyp-36A1.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; P90771; -.
DR   OMA; RFTTHIF; -.
DR   OrthoDB; 5836879at2759; -.
DR   PhylomeDB; P90771; -.
DR   Reactome; R-CEL-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-CEL-211916; Vitamins.
DR   Reactome; R-CEL-211935; Fatty acids.
DR   Reactome; R-CEL-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-CEL-211958; Miscellaneous substrates.
DR   Reactome; R-CEL-211981; Xenobiotics.
DR   Reactome; R-CEL-211999; CYP2E1 reactions.
DR   Reactome; R-CEL-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   Reactome; R-CEL-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR   Reactome; R-CEL-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-CEL-9027307; Biosynthesis of maresin-like SPMs.
DR   Reactome; R-CEL-9749641; Aspirin ADME.
DR   Reactome; R-CEL-9753281; Paracetamol ADME.
DR   PRO; PR:P90771; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00007913; Expressed in larva and 1 other cell type or tissue.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20617; CYP1_2-like; 1.
DR   FunFam; 1.10.630.10:FF:000125; Probable cytochrome P450 CYP36A1; 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   InterPro; IPR050182; Cytochrome_P450_fam2.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF338; CYTOCHROME P450 CYP36A1-RELATED; 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   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..493
FT                   /note="Probable cytochrome P450 CYP36A1"
FT                   /id="PRO_0000052270"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         440
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   493 AA;  56982 MW;  2A959C010284C33A CRC64;
     MLFAQLVILV IIVMLFLCRF ANKLRGLPPG PTPWPFIGNT FQVPEDRIDL IINEFKKKYG
     GIFTLWLPFP TIVICDYDML KRNIVKNGES FSGRPDTFIM DMLVQGNYGL FFMENNWWKA
     QRRFTTHIFR SLGVGQAGTQ DTIASLASGL VEKIDGQKDK PIELRPLLVH VVGNVIHKHL
     FGFTREWNET EILDFHVAIN DVLEHFTSPK TQLLDAWPWL AYLDKPLSLG IPRTTRANDA
     IIQNLEQALA KHKTGINYDE EPSSYMDAFL KEMKIRAAEN ALEDGFTEKQ LIVAIYDLYS
     AGMETIIIVL RFAFLYLVNN PETQKRIHEE LDRNVGRERQ VVMDDQKHLP YTCAFLQEVY
     RLGYVLPVNF LRCTLTDVED CEGYRLNAGT RVIAQFQSVH VDKKHFPDPE HFNPDRFLNS
     RGEYIRDDRV NPFSMGKRSC LGENLARMEV FLYFCTLMQN FEWHTDGPYA PPIDVITSSL
     RAPKPFTVRA SRR
//