CP306_DROME
ID CP306_DROME Reviewed; 574 AA.
AC Q9VWR5; A5AC85; A5AC97; A5AC99;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytochrome P450 306a1;
DE Short=CYPCCCVIA1;
DE EC=1.14.-.-;
DE AltName: Full=Protein phantom;
DE Short=Dmphm;
GN Name=phm; Synonyms=Cyp306a1; ORFNames=CG6578;
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, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=15350618; DOI=10.1016/j.ibmb.2004.06.009;
RA Warren J.T., Petryk A., Marques G., Parvy J.P., Shinoda T., Itoyama K.,
RA Kobayashi J., Jarcho M., Li Y., O'Connor M.B., Dauphin-Villemant C.,
RA Gilbert L.I.;
RT "Phantom encodes the 25-hydroxylase of Drosophila melanogaster and Bombyx
RT mori: a P450 enzyme critical in ecdysone biosynthesis.";
RL Insect Biochem. Mol. Biol. 34:991-1010(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-399 AND THR-560.
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 [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Involved in the metabolism of insect hormones; responsible
CC for ecdysteroid C25-hydroxylase activity. May be involved in the
CC breakdown of synthetic insecticides. {ECO:0000269|PubMed:15350618}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Steroid biosynthesis; ecdysteroid biosynthesis.
CC {ECO:0000269|PubMed:15350618}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15350618}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15350618}. Microsome membrane
CC {ECO:0000269|PubMed:15350618}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15350618}.
CC -!- TISSUE SPECIFICITY: First seen at the early (syncytial) blastoderm
CC stage 4. During cellularization of the blastoderm (stage 5), stripes of
CC expression appear and remain through to stage 10. Expression becomes
CC undetectable during germ band retraction (stages 11-14). By stage 15,
CC some expression resumes in the primordium of the ring gland, so that by
CC stage 17 strong expression is seen, but only in the ring gland. This
CC specific localization continues throughout the larval instars (at
CC protein level). Expressed in the prothoracic gland cells of the larval
CC ring gland (RG). Levels decline just after the molt to the third instar
CC then increase later during the wandering stage. Low levels of
CC expression are seen in the larval brain and fat body. In the adult,
CC majority of expression is restricted to the ovaries, with low levels in
CC the head and carcass of both sexes. {ECO:0000269|PubMed:15350618}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15350618}.
CC -!- MISCELLANEOUS: Member of the Halloween gene group.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF484413; AAQ05971.1; -; mRNA.
DR EMBL; AM411848; CAL69929.1; -; Genomic_DNA.
DR EMBL; AM411849; CAL69931.1; -; Genomic_DNA.
DR EMBL; AM411850; CAL69933.1; -; Genomic_DNA.
DR EMBL; AM411851; CAL69935.1; -; Genomic_DNA.
DR EMBL; AM411852; CAL69937.1; -; Genomic_DNA.
DR EMBL; AM411853; CAL69939.1; -; Genomic_DNA.
DR EMBL; AM411854; CAL69941.1; -; Genomic_DNA.
DR EMBL; AM411855; CAL69943.1; -; Genomic_DNA.
DR EMBL; AM411856; CAL69945.1; -; Genomic_DNA.
DR EMBL; AM411857; CAL69947.1; -; Genomic_DNA.
DR EMBL; AM411858; CAL69949.1; -; Genomic_DNA.
DR EMBL; AM411859; CAL69951.1; -; Genomic_DNA.
DR EMBL; AM411860; CAL69953.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48873.1; -; Genomic_DNA.
DR EMBL; AY070930; AAL48552.1; -; mRNA.
DR RefSeq; NP_001285414.1; NM_001298485.1.
DR RefSeq; NP_573319.1; NM_133091.3.
DR AlphaFoldDB; Q9VWR5; -.
DR SMR; Q9VWR5; -.
DR BioGRID; 59169; 3.
DR DIP; DIP-21151N; -.
DR IntAct; Q9VWR5; 1.
DR STRING; 7227.FBpp0074374; -.
DR PaxDb; Q9VWR5; -.
DR DNASU; 32857; -.
DR EnsemblMetazoa; FBtr0074603; FBpp0074374; FBgn0004959.
DR EnsemblMetazoa; FBtr0342846; FBpp0309669; FBgn0004959.
DR GeneID; 32857; -.
DR KEGG; dme:Dmel_CG6578; -.
DR UCSC; CG6578-RA; d. melanogaster.
DR CTD; 32857; -.
DR FlyBase; FBgn0004959; phm.
DR VEuPathDB; VectorBase:FBgn0004959; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q9VWR5; -.
DR OMA; IMGGYGI; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9VWR5; -.
DR BioCyc; MetaCyc:MON-18105; -.
DR Reactome; R-DME-211958; Miscellaneous substrates.
DR Reactome; R-DME-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR UniPathway; UPA00765; -.
DR ChiTaRS; phm; fly.
DR GenomeRNAi; 32857; -.
DR PRO; PR:Q9VWR5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004959; Expressed in endocrine gland and 34 other tissues.
DR ExpressionAtlas; Q9VWR5; baseline and differential.
DR Genevisible; Q9VWR5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0035302; F:ecdysteroid 25-hydroxylase activity; IDA:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0006697; P:ecdysone biosynthetic process; IDA:FlyBase.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..574
FT /note="Cytochrome P450 306a1"
FT /id="PRO_0000052315"
FT REGION 303..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
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 399
FT /note="L -> F (in strain: CN13X)"
FT /evidence="ECO:0000269|PubMed:17322555"
FT VARIANT 560
FT /note="A -> T (in strain: CN11X)"
FT /evidence="ECO:0000269|PubMed:17322555"
SQ SEQUENCE 574 AA; 65177 MW; 9A8A3E1747101700 CRC64;
MSADIVDIGH TGWMPSVQSL SILLVPGALV LVILYLCERQ CNDLMGAPPP GPWGLPFLGY
LPFLDARAPH KSLQKLAKRY GGIFELKMGR VPTVVLSDAA LVRDFFRRDV MTGRAPLYLT
HGIMGGFGII CAQEDIWRHA RRETIDWLKA LGMTRRPGEL RARLERRIAR GVDECVRLFD
TEAKKSCASE VNPLPALHHS LGNIINDLVF GITYKRDDPD WLYLQRLQEE GVKLIGVSGV
VNFLPWLRHL PANVRNIRFL LEGKAKTHAI YDRIVEACGQ RLKEKQKVFK ELQEQKRLQR
QLEKEQLRQS KEADPSQEQS EADEDDEESD EEDTYEPECI LEHFLAVRDT DSQLYCDDQL
RHLLADLFGA GVDTSLATLR WFLLYLAREQ RCQRRLHELL LPLGPSPTLE ELEPLAYLRA
CISETMRIRS VVPLGIPHGC KENFVVGDYF IKGGSMIVCS EWAIHMDPVA FPEPEEFRPE
RFLTADGAYQ APPQFIPFSS GYRMCPGEEM ARMILTLFTG RILRRFHLEL PSGTEVDMAG
ESGITLTPTP HMLRFTKLPA VEMRHAPDGA VVQD
