CP18A_DROME
ID CP18A_DROME Reviewed; 538 AA.
AC Q95078; A5AC86; A5AC96; Q0KHQ8; Q27767; Q9VWR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cytochrome P450 18a1;
DE EC=1.14.-.-;
DE AltName: Full=CYPXVIIIA1;
GN Name=Cyp18a1; Synonyms=CYP18, Eig17-1; ORFNames=CG6816;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Larva;
RX PubMed=9256362; DOI=10.1016/s0303-7207(97)00093-2;
RA Bassett M.H., McCarthy J.L., Waterman M.R., Sliter T.J.;
RT "Sequence and developmental expression of Cyp18, a member of a new
RT cytochrome P450 family from Drosophila.";
RL Mol. Cell. Endocrinol. 131:39-49(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-530.
RC STRAIN=CN10X, CN11X, CN13X, CN15X, CN16X, CN17X, CN19X, CN21X, CN22BX,
RC CN3X, and CN7X;
RX PubMed=17322555; DOI=10.1093/molbev/msm032;
RA Orengo D.J., Aguade M.;
RT "Genome scans of variation and adaptive change: extended analysis of a
RT candidate locus close to the phantom gene region in Drosophila
RT melanogaster.";
RL Mol. Biol. Evol. 24:1122-1129(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 459-479.
RC STRAIN=Canton-S;
RX PubMed=8413299; DOI=10.1128/mcb.13.11.7101-7111.1993;
RA Hurban P., Thummel C.S.;
RT "Isolation and characterization of fifteen ecdysone-inducible Drosophila
RT genes reveal unexpected complexities in ecdysone regulation.";
RL Mol. Cell. Biol. 13:7101-7111(1993).
CC -!- FUNCTION: Probably involved in steroid hormones biosynthesis.
CC {ECO:0000269|PubMed:9256362}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall (epidermal and muscle cells)
CC and mid- and hind-gut. {ECO:0000269|PubMed:9256362}.
CC -!- DEVELOPMENTAL STAGE: Low levels throughout postembryonic development.
CC -!- INDUCTION: By 20-hydroxyecdysone during the three larval stages, at
CC pupariation and in pupae. {ECO:0000269|PubMed:9256362}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44753; AAB69750.1; -; mRNA.
DR EMBL; AM411848; CAL69930.1; -; Genomic_DNA.
DR EMBL; AM411849; CAL69932.1; -; Genomic_DNA.
DR EMBL; AM411850; CAL69934.1; -; Genomic_DNA.
DR EMBL; AM411851; CAL69936.1; -; Genomic_DNA.
DR EMBL; AM411852; CAL69938.1; -; Genomic_DNA.
DR EMBL; AM411853; CAL69940.1; -; Genomic_DNA.
DR EMBL; AM411854; CAL69942.1; -; Genomic_DNA.
DR EMBL; AM411855; CAL69944.1; -; Genomic_DNA.
DR EMBL; AM411856; CAL69946.1; -; Genomic_DNA.
DR EMBL; AM411857; CAL69948.1; -; Genomic_DNA.
DR EMBL; AM411858; CAL69950.1; -; Genomic_DNA.
DR EMBL; AM411859; CAL69952.1; -; Genomic_DNA.
DR EMBL; AM411860; CAL69954.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09473.1; -; Genomic_DNA.
DR EMBL; S66112; AAB28524.1; -; mRNA.
DR RefSeq; NP_523403.2; NM_078679.3.
DR RefSeq; NP_728191.1; NM_167628.2.
DR AlphaFoldDB; Q95078; -.
DR SMR; Q95078; -.
DR BioGRID; 59170; 2.
DR STRING; 7227.FBpp0074381; -.
DR PaxDb; Q95078; -.
DR EnsemblMetazoa; FBtr0074609; FBpp0074380; FBgn0010383.
DR EnsemblMetazoa; FBtr0074610; FBpp0074381; FBgn0010383.
DR GeneID; 32858; -.
DR KEGG; dme:Dmel_CG6816; -.
DR CTD; 32858; -.
DR FlyBase; FBgn0010383; Cyp18a1.
DR VEuPathDB; VectorBase:FBgn0010383; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000167749; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q95078; -.
DR OMA; FDGKNHE; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q95078; -.
DR BioCyc; MetaCyc:MON-18164; -.
DR Reactome; R-DME-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-DME-211916; Vitamins.
DR Reactome; R-DME-211958; Miscellaneous substrates.
DR Reactome; R-DME-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR BioGRID-ORCS; 32858; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32858; -.
DR PRO; PR:Q95078; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010383; Expressed in capitellum (Drosophila) and 45 other tissues.
DR Genevisible; Q95078; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0008395; F:steroid hydroxylase activity; IDA:FlyBase.
DR GO; GO:0007304; P:chorion-containing eggshell formation; IMP:FlyBase.
DR GO; GO:0046344; P:ecdysteroid catabolic process; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0035210; P:prepupal development; IMP:FlyBase.
DR GO; GO:0035074; P:pupation; IMP:FlyBase.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Developmental protein; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Cytochrome P450 18a1"
FT /id="PRO_0000051949"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 466
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 530
FT /note="H -> Y (in strain: CN15X)"
FT /evidence="ECO:0000269|PubMed:17322555"
FT CONFLICT 19
FT /note="Q -> E (in Ref. 1; AAB69750)"
FT /evidence="ECO:0000305"
FT CONFLICT 478..479
FT /note="LF -> PV (in Ref. 5; AAB28524)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="R -> S (in Ref. 1; AAB69750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 61949 MW; A1C95E74505C28CE CRC64;
MLADSYLIKF VLRQLQVQQD GDAQHLLMVF LGLLALVTLL QWLVRNYREL RKLPPGPWGL
PVIGYLLFMG SEKHTRFMEL AKQYGSLFST RLGSQLTVVM SDYKMIRECF RREEFTGRPD
TPFMQTLNGY GIINSTGKLW KDQRRFLHDK LRQFGMTYMG NGKQQMQKRI MTEVHEFIGH
LHASDGQPVD MSPVISVAVS NVICSLMMST RFSIDDPKFR RFNFLIEEGM RLFGEIHTVD
YIPTMQCFPS ISTAKNKIAQ NRAEMQRFYQ DVIDDHKRSF DPNNIRDLVD FYLCEIEKAK
AEGTDAELFD GKNHEEQLVQ VIIDLFSAGM ETIKTTLLWI NVFMLRNPKE MRRVQDELDQ
VVGRHRLPTI EDLQYLPITE STILESMRRS SIVPLATTHS PTRDVELNGY TIPAGSHVIP
LINSVHMDPN LWEKPEEFRP SRFIDTEGKV RKPEYFIPFG VGRRMCLGDV LARMELFLFF
ASFMHCFDIA LPEGQPLPSL KGNVGATITP ESFKVCLKRR PLGPTAADPH HMRNVGAN