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P56544 (ACYP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acylphosphatase-1
EC=3.6.1.7
Alternative name(s):
Acylphosphate phosphohydrolase 1
Short name=AcPDro
Gene names
Name:Acyp
Synonyms:AcP
ORF Names:CG16870
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An acylphosphate + H2O = a carboxylate + phosphate.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the acylphosphatase family.

Contains 1 acylphosphatase-like domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.3-6.3.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacylphosphatase activity

Inferred from direct assay Ref.1. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG7742Q9VMT41EBI-125011,EBI-172862

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 120119Acylphosphatase-1
PRO_0000158550

Regions

Domain8 – 9891Acylphosphatase-like

Sites

Active site231 Potential
Active site411 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
P56544 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B07C97175FEE77A1

FASTA12013,697
        10         20         30         40         50         60 
MATHNVHSCE FEVFGRVQGV NFRRHALRKA KTLGLRGWCM NSSRGTVKGY IEGRPAEMDV 

        70         80         90        100        110        120 
MKEWLRTTGS PLSSIEKVEF SSQRERDRYG YANFHIKPDP HENRPVHEGL GSSSSHHDSN

« Hide

References

« Hide 'large scale' references
[1]"Drosophila melanogaster acylphosphatase: a common ancestor for acylphosphatase isoenzymes of vertebrate species."
Pieri A., Magherini F., Liguri G., Raugei G., Taddei N., Bozzetti M.P., Cecchi C., Ramponi G.
FEBS Lett. 433:205-210(1998) [PubMed: 9744795] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed: 10471707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[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. 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: 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. 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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ243543 mRNA. Translation: CAB48386.1.
AE014134 Genomic DNA. Translation: AAF53355.1.
RefSeqNP_523563.1. NM_078839.2.

3D structure databases

ProteinModelPortalP56544.
SMRP56544. Positions 3-98.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-22487N.
IntActP56544. 1 interaction.
MINTMINT-877389.
STRINGP56544.

Proteomic databases

PRIDEP56544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080555; FBpp0080132; FBgn0025115.
GeneID34807.
KEGGdme:Dmel_CG16870.
NMPDRfig|7227.3.peg.2348.
UCSCCG16870-RA. d. melanogaster.

Organism-specific databases

CTD34807.
FlyBaseFBgn0025115. Acyp.

Phylogenomic databases

eggNOGmeNOG20691.
GeneTreeEMGT00050000016359.
InParanoidP56544.
OMAQNIVTIH.
OrthoDBEOG4NZS9T.
PhylomeDBP56544.

Gene expression databases

BgeeP56544.
GermOnlineCG16870. Drosophila melanogaster.

Family and domain databases

InterProIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like.
IPR017968. Acylphosphatase_CS.
[Graphical view]
KOK01512.
PfamPF00708. Acylphosphatase. 1 hit.
[Graphical view]
PRINTSPR00112. ACYLPHPHTASE.
SUPFAMSSF54975. Acylphosphatase. 1 hit.
PROSITEPS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio790318.

Entry information

Entry nameACYP1_DROME
AccessionPrimary (citable) accession number: P56544
Secondary accession number(s): Q9V3K1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 90 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents