Reviewed, UniProtKB/Swiss-Prot Q9VWR5 (CP306_DROME)

Names and origin

Protein names

Recommended name:
    Cytochrome P450 306a1
      Short name=CYPCCCVIA1
    EC=1.14.-.-
Alternative name(s):
    Protein phantom
      Short name=Dmphm

Gene names

Name:	phm
Synonyms:	Cyp306a1
ORF Names:	CG6578

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	574 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the metabolism of insect hormones; responsible for ecdysteroid C25-hydroxylase activity. May be involved in the breakdown of synthetic insecticides. Ref.1
Catalytic activity	RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.
Cofactor	Heme group By similarity.
Pathway	Steroid biosynthesis; ecdysteroid biosynthesis. Ref.1
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Ref.1
Tissue specificity	First seen at the early (syncytial) blastoderm stage 4. During cellularization of the blastoderm (stage 5), stripes of expression appear and remain through to stage 10. Expression becomes undetectable during germ band retraction (stages 11-14). By stage 15, some expression resumes in the primordium of the ring gland, so that by stage 17 strong expression is seen, but only in the ring gland. This specific localization continues throughout the larval instars (at protein level). Expressed in the prothoracic gland cells of the larval ring gland (RG). Levels decline just after the molt to the third instar then increase later during the wandering stage. Low levels of expression are seen in the larval brain and fat body. In the adult, majority of expression is restricted to the ovaries, with low levels in the head and carcass of both sexes. Ref.1
Developmental stage	Expressed both maternally and zygotically. Ref.1
Miscellaneous	Member of the Halloween gene group.
Sequence similarities	Belongs to the cytochrome P450 family.
Caution	It is uncertain whether Met-1 or Met-14 is the initiator.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ecdysone biosynthetic process Ref.1 Inferred from direct assay. Source: FlyBase embryonic development via the syncytial blastoderm Inferred from mutant phenotype. Source: FlyBase oogenesis Inferred from mutant phenotype. Source: FlyBase oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ecdysteroid 25-hydroxylase activity Ref.1 Inferred from direct assay. Source: FlyBase electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 574	574	Cytochrome P450 306a1		PRO_0000052315
Sites
	Metal binding	505	1	Iron (heme axial ligand) By similarity
Natural variations
	Natural variant	399	1	L → F in strain: CN13X. Ref.2
	Natural variant	560	1	A → T in strain: CN11X. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9VWR5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9A8A3E1747101700	FASTA	574	65,177
	10 20 30 40 50 60 MSADIVDIGH TGWMPSVQSL SILLVPGALV LVILYLCERQ CNDLMGAPPP GPWGLPFLGY 70 80 90 100 110 120 LPFLDARAPH KSLQKLAKRY GGIFELKMGR VPTVVLSDAA LVRDFFRRDV MTGRAPLYLT 130 140 150 160 170 180 HGIMGGFGII CAQEDIWRHA RRETIDWLKA LGMTRRPGEL RARLERRIAR GVDECVRLFD 190 200 210 220 230 240 TEAKKSCASE VNPLPALHHS LGNIINDLVF GITYKRDDPD WLYLQRLQEE GVKLIGVSGV 250 260 270 280 290 300 VNFLPWLRHL PANVRNIRFL LEGKAKTHAI YDRIVEACGQ RLKEKQKVFK ELQEQKRLQR 310 320 330 340 350 360 QLEKEQLRQS KEADPSQEQS EADEDDEESD EEDTYEPECI LEHFLAVRDT DSQLYCDDQL 370 380 390 400 410 420 RHLLADLFGA GVDTSLATLR WFLLYLAREQ RCQRRLHELL LPLGPSPTLE ELEPLAYLRA 430 440 450 460 470 480 CISETMRIRS VVPLGIPHGC KENFVVGDYF IKGGSMIVCS EWAIHMDPVA FPEPEEFRPE 490 500 510 520 530 540 RFLTADGAYQ APPQFIPFSS GYRMCPGEEM ARMILTLFTG RILRRFHLEL PSGTEVDMAG 550 560 570 ESGITLTPTP HMLRFTKLPA VEMRHAPDGA VVQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phantom encodes the 25-hydroxylase of Drosophila melanogaster and Bombyx mori: a P450 enzyme critical in ecdysone biosynthesis." Warren J.T., Petryk A., Marques G., Parvy J.P., Shinoda T., Itoyama K., Kobayashi J., Jarcho M., Li Y., O'Connor M.B., Dauphin-Villemant C., Gilbert L.I. Insect Biochem. Mol. Biol. 34:991-1010(2004) [PubMed: 15350618] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryo.
[2]	"Genome scans of variation and adaptive change: extended analysis of a candidate locus close to the phantom gene region in Drosophila melanogaster." Orengo D.J., Aguade M. Mol. Biol. Evol. 24:1122-1129(2007) [PubMed: 17322555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-399 AND THR-560. Strain: CN10X, CN11X, CN13X, CN15X, CN16X, CN17X, CN19X, CN21X, CN22BX, CN3X and CN7X.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF484413 mRNA. Translation: AAQ05971.1. AM411848 Genomic DNA. Translation: CAL69929.1. AM411849 Genomic DNA. Translation: CAL69931.1. AM411850 Genomic DNA. Translation: CAL69933.1. AM411851 Genomic DNA. Translation: CAL69935.1. AM411852 Genomic DNA. Translation: CAL69937.1. AM411853 Genomic DNA. Translation: CAL69939.1. AM411854 Genomic DNA. Translation: CAL69941.1. AM411855 Genomic DNA. Translation: CAL69943.1. AM411856 Genomic DNA. Translation: CAL69945.1. AM411857 Genomic DNA. Translation: CAL69947.1. AM411858 Genomic DNA. Translation: CAL69949.1. AM411859 Genomic DNA. Translation: CAL69951.1. AM411860 Genomic DNA. Translation: CAL69953.1. AE014298 Genomic DNA. Translation: AAF48873.1. AY070930 mRNA. Translation: AAL48552.1.
RefSeq	NP_573319.1.
UniGene	Dm.5302
3D structure databases
HSSP	HSSP built from PDB template 1DT6 based on UniProtKB P00179.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:21151N.
IntAct	Q9VWR5. 3 interactions.
Proteomic databases
PRIDE	Q9VWR5.
Genome annotation databases
Ensembl	FBgn0004959. Drosophila melanogaster. [Contig view]
GeneID	32857.
KEGG	dme:Dmel_CG6578.
NMPDR	fig|7227.3.peg.18527.
Organism-specific databases
FlyBase	FBgn0004959. phm.
Phylogenomic databases
HOGENOM	Q9VWR5.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-002506-MON.
Gene expression databases
ArrayExpress	Q9VWR5.
GermOnline	CG6578. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	780740.

Entry information

Entry name

CP306_DROME

Accession

Primary (citable) accession number: Q9VWR5
Secondary accession number(s): A5AC85, A5AC97, A5AC99

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project