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Q9VGX3 (FAU_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein anoxia up-regulated
Gene names
Name:fau
ORF Names:CG6544
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the regulation of tissue responsiveness to oxygen deprivation.

Tissue specificity

Concentrated in lamina neurons, first optic lobe neurons and cortical neurons of central brain.

Induction

By anoxia.

Ontologies

Keywords
   Biological processStress response
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to anoxia

Inferred from mutant phenotype Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform E (identifier: Q9VGX3-5)

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.
Note: No experimental confirmation available.
Isoform B (identifier: Q9VGX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-163: YPSVEKVTRV...PLRITPSPVR → RTKRTPIDWE...SGAMVTKYSY
     164-619: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: Q9VGX3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     26-131: YPSVEKVTRV...TYIPTSYTTY → TPRLDLCTDR...TKYRHFSYHV
     132-619: Missing.
Isoform D (identifier: Q9VGX3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     36-98: YKSSYPIYSS...TTRVISSPER → SIWFSSLSPT...HIIVLFRLKH
     99-619: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Protein anoxia up-regulated
PRO_0000087203

Regions

Compositional bias88 – 14356Thr-rich
Compositional bias305 – 619315Ala/Glu-rich

Amino acid modifications

Modified residue791Phosphoserine Ref.5
Modified residue811Phosphoserine Ref.5

Natural variations

Alternative sequence26 – 163138YPSVE…PSPVR → RTKRTPIDWEKVPFVPRPSL ISDPVTAFGVRRPDLERRQR SILDPINRASIKPDYKLAYE PIEPYVSTRDKNRTRILGMV RQHIDTVEAGGNTAGRTFRD SLDAQLPRLHRAVSESLPVR RETYRNERSGAMVTKYSY in isoform B.
VSP_004048
Alternative sequence26 – 131106YPSVE…SYTTY → TPRLDLCTDRPGSHRSRASS DYSYTSKSSVEKSSYDSSNP HSYRPERSTYTSTVEKTSRS GPGGSYNYSTERTSTTGAGP GGYSYSSTTSGNLPGGTKYR HFSYHV in isoform C.
VSP_004046
Alternative sequence36 – 9863YKSSY…SSPER → SIWFSSLSPTSLVIIHLSMD YYYSFLLTYITHCSITSITS SSLEKQIRLVISPHIIVLFR LKH in isoform D.
VSP_004050
Alternative sequence99 – 619521Missing in isoform D.
VSP_004051
Alternative sequence132 – 619488Missing in isoform C.
VSP_004047
Alternative sequence164 – 619456Missing in isoform B.
VSP_004049

Sequences

Sequence LengthMass (Da)Tools
Isoform E [UniParc].

Last modified July 19, 2004. Version 3.
Checksum: 7DDCB26AD1AB9CEE

FASTA61968,642
        10         20         30         40         50         60 
MVYESGFTTR RTYSSRPVTT SYAVTYPSVE KVTRVYKSSY PIYSSYSVPR RVYGATRVVT 

        70         80         90        100        110        120 
SPIRVVTSPA RVVSRVIHSP SPVRVVRTTT RVISSPERTT YSYTTPSTYY SPSYLPSTYT 

       130        140        150        160        170        180 
STYIPTSYTT YTPSYAYSPT TVTRVYAPRS SLSPLRITPS PVRVITSPVR SVPSYLKRLP 

       190        200        210        220        230        240 
PGYGARALTN YLNTEPFTTF SEETSRIRNR AQSLIRDLHT PVVRRARSCT PFPVTGYTYE 

       250        260        270        280        290        300 
PASQLALDAY VARVTNPVRH IAKEVHNISH YPRPAVKYVD AELDPNRPSR KFSAPRPLED 

       310        320        330        340        350        360 
PLDVEAKEKQ RLRQERLLTV NEEALDEVDL EKKRAQKADE AKRREERALK EERDRLTAEA 

       370        380        390        400        410        420 
EKQAAAKAKK AAEEAAKIAA EEALLAEAAA QKAAEEAKAL KAAEDAAQKA AEEARLAEEA 

       430        440        450        460        470        480 
AAQKVAEEAA QKAAEEARLA EEAAAQKAAE EAAQKAAEEA ALKAAEEARL AEEAAQKAAE 

       490        500        510        520        530        540 
EAALKAVEEA RAAEEAAQKA AEEARVAEEA RLEEEQRVRE QELERLAEIE KESEGELARQ 

       550        560        570        580        590        600 
AAELAEIARQ ESELAAQELQ AIQKNENETS EPVVEEPVTP VEEQEPIIEL GSNVTPTGGN 

       610 
SYEEDLDAEE EEDEEEEEE 

« Hide

Isoform B [UniParc].

Checksum: 5871581843CB6030
Show »

FASTA16318,836
Isoform C [UniParc].

Checksum: 58EF580B0F90570D
Show »

FASTA13114,371
Isoform D [UniParc].

Checksum: 0DBFBEFF66AE6398
Show »

FASTA9811,304

References

« Hide 'large scale' references
[1]"Gene regulation by O2 deprivation: an anoxia-regulated novel gene in Drosophila melanogaster."
Ma E., Xu T., Haddad G.G.
Brain Res. Mol. Brain Res. 63:217-224(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
Strain: Canton-S.
Tissue: Head.
[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. expand/collapse author list , 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]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
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] (ISOFORMS C AND E).
Strain: Berkeley.
Tissue: Head.
[5]"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-79 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF154418 mRNA. Translation: AAD38397.1.
AE014297 Genomic DNA. Translation: AAF54549.3.
AE014297 Genomic DNA. Translation: AAF54550.1.
AE014297 Genomic DNA. Translation: AAF54551.1.
AE014297 Genomic DNA. Translation: AAF54552.1.
AY060997 mRNA. Translation: AAL28545.1.
AY119569 mRNA. Translation: AAM50223.1.
RefSeqNP_650015.3. NM_141758.5. [Q9VGX3-5]
NP_731504.1. NM_169360.3. [Q9VGX3-4]
NP_731505.1. NM_169361.3. [Q9VGX3-3]
NP_731506.1. NM_169362.4. [Q9VGX3-2]
UniGeneDm.19238.

3D structure databases

ProteinModelPortalQ9VGX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66435. 17 interactions.
DIPDIP-18797N.
IntActQ9VGX3. 3 interactions.

Proteomic databases

PaxDbQ9VGX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082307; FBpp0081783; FBgn0020439. [Q9VGX3-5]
GeneID41291.
KEGGdme:Dmel_CG6544.
UCSCCG6544-RA. d. melanogaster. [Q9VGX3-5]

Organism-specific databases

CTD2197.
FlyBaseFBgn0020439. fau.

Phylogenomic databases

eggNOGNOG242396.
InParanoidQ9VGX3.
OMARILSMVR.
OrthoDBEOG7F24SQ.
PhylomeDBQ9VGX3.

Gene expression databases

BgeeQ9VGX3.

Family and domain databases

ProtoNetSearch...

Other

ChiTaRSFAU. drosophila.
GenomeRNAi41291.
NextBio823138.

Entry information

Entry nameFAU_DROME
AccessionPrimary (citable) accession number: Q9VGX3
Secondary accession number(s): Q95S18 expand/collapse secondary AC list , Q9VGX1, Q9VGX2, Q9Y0F9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase