Skip Header

 
Contribute Send feedback

Unreviewed, UniProtKB/TrEMBL Q8ST50 (Q8ST50_DROME)

Last modified September 23, 2008. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Acyl coenzyme A:diacylglycerol acyltransferase EMBL AAL78365.1
Gene names
Name: mdy FlyBase FBgn0004797
ORF Names: CG31991 FlyBase FBgn0004797
OrganismDrosophila melanogaster (Fruit fly) EMBL AAL78365.1
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Ontologies

Keywords

   Cellular componentMembrane
   DomainTransmembrane Spearmint SPM004299
   Molecular functionAcyltransferase
Transferase

Gene Ontology (GO)

   Biological processregulation of nurse cell apoptosis Ref.1

Inferred from mutant phenotype. Source: FlyBase

   Molecular functiondiacylglycerol O-acyltransferase activity Ref.1

Inferred from direct assay. Source: FlyBase

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q8ST50-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E1895AF6A3846E04

FASTA56564,929
        10         20         30         40         50         60 
MTTNKDPQDK EPGKAEQPTK NSGSSGVGIM KRLRRSASAT EHNLSSLRNR KSTQNLFDQH 

        70         80         90        100        110        120 
GNPIDLRQYR KVLDKDENGN GTNGSEKKLR YRRTQSVTRA EEISNKEEKQ RRAQPGRPIH 

       130        140        150        160        170        180 
RPRDSLFSWS SGFTNFSGLV NWGFLLLCIG GLRLGLENLL KYGIRINPLD WFFFISGHNE 

       190        200        210        220        230        240 
GEGHNALILS IYSLVHISLC LAVEKGLAME IIAEGLGLFI QIVNIVVLVC LPVVTIHLKG 

       250        260        270        280        290        300 
HAFSLMGAST VCFFYSVLFL KLWSYVQTNM WCRQTYYQKN PRERRPSITL AELKKGVLNG 

       310        320        330        340        350        360 
GEEDEDVSKL VQYPDNLTYN DLLYFLCAPT LCYELNFPRT SRVRKRFLLK RLLEVVIGVN 

       370        380        390        400        410        420 
VVMALFQQWI IPSVRNSLIP FSNMDVALAT ERLLKLALPN HLCWLCFFYL MFHSFLNAVG 

       430        440        450        460        470        480 
ELLNFADRNF YCDWWNANNI DTFWRTWNMP VHRWCVRHLY IPVVQMGYSS RQASTIVFLF 

       490        500        510        520        530        540 
SAVFHEYLVS VPLQIYKIWA FMGMMGQIPL SAISKSIEKK LGPRMGNIIV WASIILGQPL 

       550        560 
CIMAYYHDYV VQHFKNSLNG TDYSS 

« Hide

References

[1]"Mutations in the midway gene disrupt a Drosophila acyl coenzyme A: diacylglycerol acyltransferase."
Buszczak M., Lu X., Segraves W.A., Chang T.Y., Cooley L.
Genetics 160:1511-1518(2002) [PubMed: 11973306] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

AF468649 mRNA. Translation: AAL78365.1.
AF468650 mRNA. Translation: AAL78366.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblCG31991. Drosophila melanogaster. [Contig view]

Organism-specific databases

FlyBaseFBgn0004797. mdy.

Gene expression databases

ArrayExpressQ8ST50.

Family and domain databases

InterProIPR004299. MBOAT_fam.
[Graphical view]
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
ProDomQ8ST50.
[Graphical view] [Entries sharing at least one domain]

Entry information

Entry nameQ8ST50_DROME
AccessionPrimary (citable) accession number: Q8ST50
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: September 23, 2008
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information