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Protein

Cytochrome P450 307a1

Gene

spo

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for correct development of the embryonic midline glial cells which are necessary for the formation of distinct segmental commissures.1 Publication

Catalytic activityi

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactori

hemeBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi485 – 4851Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

  • central nervous system development Source: FlyBase
  • cuticle development Source: FlyBase
  • dorsal closure Source: FlyBase
  • ecdysone biosynthetic process Source: FlyBase
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • embryonic digestive tract development Source: FlyBase
  • head involution Source: FlyBase
  • midgut development Source: FlyBase
  • oogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-156581. Methylation.
R-DME-211957. Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2.
R-DME-211976. Endogenous sterols.
R-DME-211981. Xenobiotics.
R-DME-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
R-DME-2142816. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
R-DME-5423646. Aflatoxin activation and detoxification.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 307a1 (EC:1.14.-.-)
Alternative name(s):
CYPCCCVIIA1
Protein spook
Gene namesi
Name:spo
Synonyms:Cyp307a1
ORF Names:CG10594
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003486. spo.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 543543Cytochrome P450 307a1PRO_0000052316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei219 – 2191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VRM7.

PTM databases

iPTMnetiQ9VRM7.

Expressioni

Gene expression databases

BgeeiQ9VRM7.
GenevisibleiQ9VRM7. DM.

Interactioni

Protein-protein interaction databases

BioGridi64094. 3 interactions.
DIPiDIP-17643N.
IntActiQ9VRM7. 4 interactions.
MINTiMINT-280396.
STRINGi7227.FBpp0076836.

Structurei

3D structure databases

ProteinModelPortaliQ9VRM7.
SMRiQ9VRM7. Positions 56-520.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000118992.
InParanoidiQ9VRM7.
KOiK14939.
OMAiLKRNIPH.
OrthoDBiEOG70087V.
PhylomeDBiQ9VRM7.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VRM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAALIYTIL AILLSVLATS YICIIYGVKR RVLQPVKTKN STEINHNAYQ
60 70 80 90 100
KYTQAPGPRP WPIIGNLHLL DRYRDSPFAG FTALAQQYGD IYSLTFGHTR
110 120 130 140 150
CLVVNNLELI REVLNQNGKV MSGRPDFIRY HKLFGGERSN SLALCDWSQL
160 170 180 190 200
QQKRRNLARR HCSPREFSCF YMKMSQIGCE EMEHWNRELG NQLVPGEPIN
210 220 230 240 250
IKPLILKACA NMFSQYMCSL RFDYDDVDFQ QIVQYFDEIF WEINQGHPLD
260 270 280 290 300
FLPWLYPFYQ RHLNKIINWS STIRGFIMER IIRHRELSVD LDEPDRDFTD
310 320 330 340 350
ALLKSLLEDK DVSRNTIIFM LEDFIGGHSA VGNLVMLVLA YIAKNVDIGR
360 370 380 390 400
RIQEEIDAII EEENRSINLL DMNAMPYTMA TIFEVLRYSS SPIVPHVATE
410 420 430 440 450
DTVISGYGVT KGTIVFINNY VLNTSEKFWV NPKEFNPLRF LEPSKEQSPK
460 470 480 490 500
NSKGSDSGIE SDNEKLQLKR NIPHFLPFSI GKRTCIGQNL VRGFGFLVVV
510 520 530 540
NVMQRYNISS HNPSTIKISP ESLALPADCF PLVLTPREKI GPL
Length:543
Mass (Da):62,448
Last modified:August 15, 2003 - v3
Checksum:iF61DE137A0F5C219
GO

Sequence cautioni

The sequence AAL48675.1 differs from that shown. Reason: Frameshift at position 505. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF484415 mRNA. Translation: AAQ05973.1.
AE014296 Genomic DNA. Translation: AAF50766.3.
AY071053 mRNA. Translation: AAL48675.1. Frameshift.
RefSeqiNP_001286943.1. NM_001300014.1.
NP_647975.2. NM_139718.3.
UniGeneiDm.31174.

Genome annotation databases

EnsemblMetazoaiFBtr0077130; FBpp0076836; FBgn0003486.
FBtr0346640; FBpp0312220; FBgn0003486.
GeneIDi38631.
KEGGidme:Dmel_CG10594.
UCSCiCG10594-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF484415 mRNA. Translation: AAQ05973.1.
AE014296 Genomic DNA. Translation: AAF50766.3.
AY071053 mRNA. Translation: AAL48675.1. Frameshift.
RefSeqiNP_001286943.1. NM_001300014.1.
NP_647975.2. NM_139718.3.
UniGeneiDm.31174.

3D structure databases

ProteinModelPortaliQ9VRM7.
SMRiQ9VRM7. Positions 56-520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64094. 3 interactions.
DIPiDIP-17643N.
IntActiQ9VRM7. 4 interactions.
MINTiMINT-280396.
STRINGi7227.FBpp0076836.

PTM databases

iPTMnetiQ9VRM7.

Proteomic databases

PaxDbiQ9VRM7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077130; FBpp0076836; FBgn0003486.
FBtr0346640; FBpp0312220; FBgn0003486.
GeneIDi38631.
KEGGidme:Dmel_CG10594.
UCSCiCG10594-RA. d. melanogaster.

Organism-specific databases

CTDi38631.
FlyBaseiFBgn0003486. spo.

Phylogenomic databases

eggNOGiKOG0156. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000118992.
InParanoidiQ9VRM7.
KOiK14939.
OMAiLKRNIPH.
OrthoDBiEOG70087V.
PhylomeDBiQ9VRM7.

Enzyme and pathway databases

ReactomeiR-DME-156581. Methylation.
R-DME-211957. Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2.
R-DME-211976. Endogenous sterols.
R-DME-211981. Xenobiotics.
R-DME-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
R-DME-2142816. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
R-DME-5423646. Aflatoxin activation and detoxification.

Miscellaneous databases

GenomeRNAii38631.
PROiQ9VRM7.

Gene expression databases

BgeeiQ9VRM7.
GenevisibleiQ9VRM7. DM.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of Halloween group mutants."
    Petryk A., Jarcho M., O'Connor M.B.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Commissure formation in the embryonic CNS of Drosophila."
    Hummel T., Schimmelpfeng K., Klambt C.
    Dev. Biol. 209:381-398(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCP307_DROME
AccessioniPrimary (citable) accession number: Q9VRM7
Secondary accession number(s): Q8SZ84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 15, 2003
Last modified: June 8, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Member of the Halloween gene group.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.