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Protein

Ecdysone 20-monooxygenase

Gene

shd

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

Functioni

Required for CNS development; midline glial cells. Involved in the metabolism of insect hormones; responsible for all ecdysone 20-monooxygenase activity during embryonic, larval and adult stages. May be involved in the breakdown of synthetic insecticides.2 Publications

Catalytic activityi

Ecdysone + AH2 + O2 = 20-hydroxyecdysone + A + H2O.1 Publication

Cofactori

Pathwayi: ecdysteroid biosynthesis

This protein is involved in the pathway ecdysteroid biosynthesis, which is part of Steroid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ecdysteroid biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi488 – 4881Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • central nervous system development Source: FlyBase
  • dorsal closure Source: FlyBase
  • ecdysteroid biosynthetic process Source: FlyBase
  • growth of a germarium-derived egg chamber Source: FlyBase
  • head involution Source: FlyBase
  • midgut development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7726.
BRENDAi1.14.99.22. 1994.
UniPathwayiUPA00765.

Names & Taxonomyi

Protein namesi
Recommended name:
Ecdysone 20-monooxygenase (EC:1.14.99.22)
Short name:
E20MO
Alternative name(s):
CYPCCCXIVA1
Cytochrome P450 314a1, mitochondrial
Protein shade
Gene namesi
Name:shd
Synonyms:CYP314A1
ORF Names:CG13478
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003388. shd.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: FlyBase
  • mitochondrial membrane Source: UniProtKB-SubCell
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi225 – 2251E → K in allele shd-Z383; failure of head involution. Defects in dorsal closure and aberrant gut looping. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 540Ecdysone 20-monooxygenasePRO_0000003630
Transit peptidei1 – ?Mitochondrion

Proteomic databases

PaxDbiQ9VUF8.
PRIDEiQ9VUF8.

Expressioni

Tissue specificityi

Strong expression by embryonic stage 10 in epidermis, decreases significantly in older embryos. Third instar larvae show expression in the midgut copper cells, Malpighian tubules and fat body. In the adult ovaries, expression is seen in both nurse cells and centripetally migrating follicle cells.1 Publication

Gene expression databases

BgeeiQ9VUF8.
ExpressionAtlasiQ9VUF8. differential.
GenevisibleiQ9VUF8. DM.

Interactioni

Protein-protein interaction databases

BioGridi64922. 2 interactions.
IntActiQ9VUF8. 1 interaction.
STRINGi7227.FBpp0089324.

Structurei

3D structure databases

ProteinModelPortaliQ9VUF8.
SMRiQ9VUF8. Positions 61-533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
InParanoidiQ9VUF8.
KOiK10723.
OMAiRFVEMEV.
OrthoDBiEOG7Z95N9.
PhylomeDBiQ9VUF8.

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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: Q9VUF8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAVILLLALA LVLGCYCALH RHKLADIYLR PLLKNTLLED FYHAELIQPE
60 70 80 90 100
APKRRRRGIW DIPGPKRIPF LGTKWIFLLF FRRYKMTKLH EVYADLNRQY
110 120 130 140 150
GDIVLEVMPS NVPIVHLYNR DDLEKVLKYP SKYPFRPPTE IIVMYRQSRP
160 170 180 190 200
DRYASVGIVN EQGPMWQRLR SSLTSSITSP RVLQNFLPAL NAVCDDFIEL
210 220 230 240 250
LRARRDPDTL VVPNFEELAN LMGLEAVCTL MLGRRMGFLA IDTKQPQKIS
260 270 280 290 300
QLAAAVKQLF ISQRDSYYGL GLWKYFPTKT YRDFARAEDL IYDVISEIID
310 320 330 340 350
HELEELKKSA ACEDDEAAGL RSIFLNILEL KDLDIRDKKS AIIDFIAAGI
360 370 380 390 400
ETLANTLLFV LSSVTGDPGA MPRILSEFCE YRDTNILQDA LTNATYTKAC
410 420 430 440 450
IQESYRLRPT AFCLARILEE DMELSGYSLN AGTVVLCQNM IACHKDSNFQ
460 470 480 490 500
GAKQFTPERW IDPATENFTV NVDNASIVVP FGVGRRSCPG KRFVEMEVVL
510 520 530 540
LLAKMVLAFD VSFVKPLETE FEFLLAPKTP LSLRLSDRVF
Length:540
Mass (Da):61,690
Last modified:January 16, 2004 - v3
Checksum:iE6B007B6A6D99E58
GO
Isoform C (identifier: Q9VUF8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: Missing.

Note: No experimental confirmation available.
Show »
Length:433
Mass (Da):49,017
Checksum:i21A4C62F0940D147
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141G → V in AAQ05972 (PubMed:14610274).Curated
Sequence conflicti198 – 1981I → T in AAQ05972 (PubMed:14610274).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 107107Missing in isoform C. 1 PublicationVSP_009267Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF484414 mRNA. Translation: AAQ05972.1.
AE014296 Genomic DNA. Translation: AAS65010.1.
AY089309 mRNA. Translation: AAL90047.1.
RefSeqiNP_001261843.1. NM_001274914.1. [Q9VUF8-1]
NP_648709.2. NM_140452.2. [Q9VUF8-2]
NP_996074.1. NM_206352.2. [Q9VUF8-1]
UniGeneiDm.5109.

Genome annotation databases

EnsemblMetazoaiFBtr0075676; FBpp0089324; FBgn0003388. [Q9VUF8-1]
FBtr0333031; FBpp0305245; FBgn0003388. [Q9VUF8-1]
GeneIDi39592.
KEGGidme:Dmel_CG13478.
UCSCiCG13478-RA. d. melanogaster. [Q9VUF8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF484414 mRNA. Translation: AAQ05972.1.
AE014296 Genomic DNA. Translation: AAS65010.1.
AY089309 mRNA. Translation: AAL90047.1.
RefSeqiNP_001261843.1. NM_001274914.1. [Q9VUF8-1]
NP_648709.2. NM_140452.2. [Q9VUF8-2]
NP_996074.1. NM_206352.2. [Q9VUF8-1]
UniGeneiDm.5109.

3D structure databases

ProteinModelPortaliQ9VUF8.
SMRiQ9VUF8. Positions 61-533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64922. 2 interactions.
IntActiQ9VUF8. 1 interaction.
STRINGi7227.FBpp0089324.

Proteomic databases

PaxDbiQ9VUF8.
PRIDEiQ9VUF8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075676; FBpp0089324; FBgn0003388. [Q9VUF8-1]
FBtr0333031; FBpp0305245; FBgn0003388. [Q9VUF8-1]
GeneIDi39592.
KEGGidme:Dmel_CG13478.
UCSCiCG13478-RA. d. melanogaster. [Q9VUF8-1]

Organism-specific databases

CTDi56961.
FlyBaseiFBgn0003388. shd.

Phylogenomic databases

eggNOGiKOG0159. Eukaryota.
COG2124. LUCA.
GeneTreeiENSGT00760000119243.
InParanoidiQ9VUF8.
KOiK10723.
OMAiRFVEMEV.
OrthoDBiEOG7Z95N9.
PhylomeDBiQ9VUF8.

Enzyme and pathway databases

UniPathwayiUPA00765.
BioCyciMetaCyc:MONOMER-7726.
BRENDAi1.14.99.22. 1994.

Miscellaneous databases

GenomeRNAii39592.
PROiQ9VUF8.

Gene expression databases

BgeeiQ9VUF8.
ExpressionAtlasiQ9VUF8. differential.
GenevisibleiQ9VUF8. 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. "Shade is the Drosophila P450 enzyme that mediates the hydroxylation of ecdysone to the steroid insect molting hormone 20-hydroxyecdysone."
    Petryk A., Warren J.T., Marques G., Jarcho M.P., Gilbert L.I., Kahler J., Parvy J.-P., Li Y., Dauphin-Villemant C., O'Connor M.B.
    Proc. Natl. Acad. Sci. U.S.A. 100:13773-13778(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, ENZYME ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-225.
  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, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley.
    Tissue: Testis.
  5. "Regulation of glial cell number and differentiation by ecdysone and Fos signaling."
    Giesen K., Lammel U., Langehans D., Krukkert K., Bunse I., Klambt C.
    Mech. Dev. 120:401-413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCP314_DROME
AccessioniPrimary (citable) accession number: Q9VUF8
Secondary accession number(s): Q8T483
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 16, 2004
Last modified: July 6, 2016
This is version 133 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.