C13AA_CAEEL
ID C13AA_CAEEL Reviewed; 519 AA.
AC Q09653;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Putative cytochrome P450 CYP13A10;
DE EC=1.14.-.-;
GN Name=cyp-13A10; Synonyms=cyp13a10; ORFNames=ZK1320.4;
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}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; Z46934; CAA87042.3; -; Genomic_DNA.
DR PIR; T27750; T27750.
DR RefSeq; NP_496085.3; NM_063684.4.
DR AlphaFoldDB; Q09653; -.
DR SMR; Q09653; -.
DR STRING; 6239.ZK1320.4; -.
DR PaxDb; Q09653; -.
DR EnsemblMetazoa; ZK1320.4.1; ZK1320.4.1; WBGene00014254.
DR GeneID; 174522; -.
DR KEGG; cel:CELE_ZK1320.4; -.
DR UCSC; ZK1320.4; c. elegans.
DR CTD; 174522; -.
DR WormBase; ZK1320.4; CE37736; WBGene00014254; cyp-13A10.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00970000196408; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q09653; -.
DR OMA; IWTYWRR; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q09653; -.
DR PRO; PR:Q09653; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00014254; Expressed in embryo and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..519
FT /note="Putative cytochrome P450 CYP13A10"
FT /id="PRO_0000052269"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 465
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 519 AA; 60017 MW; AFC961B7E214B12A CRC64;
MSVILLAIPT LFIGFISYYL WIWTYWRRRG IPGPLGYPLV GSFPKTLKSE YPQYLQIRDW
TKLYGPIYGY TEGTIKTLIV SDIDIVRQIF VEQYDNFYGR KLNPIQGDPE KDERTNLFSA
QGFRWKRLRA ISSPTFSNNS LRKINVTVED SAMELLRHIE EQTSEGQQID MLQFYQEFTM
DTIGRIAMGQ TDSQMFKNPL LKFVRAIFGD NRKHIPLIGG VFPTLAQVFR FFMLKFPLLG
AANFIHVNKT VVTAVQNRID QRENDRKNGI EIGEPQDFID LFLEARADDV EHFQENNGDF
SKTSSYGNRQ LTTQEIVGQC LVFLIAGFDT TALSLSYTTF LLATHPEVQK KLQEEIEREC
IEPSISFDHL SKLKYMDCII KETLRLYPLG TMANSRRCMR ATKLGNVEVE VGTMVQVDTW
SLHTDTKIWG DDAKEFKPER WLDPNCDQVF QKGGYISFGL GPRQCVGMRL AYMEEKMLLA
HILRKYTFEV GTKTEIPLKL VGRATTQPET VWMHLKQRI