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P14620 (ACYP2_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acylphosphatase-2

EC=3.6.1.7
Alternative name(s):
Acylphosphatase, muscle type isozyme
Acylphosphate phosphohydrolase 2
Gene names
Name:ACYP2
OrganismAnas platyrhynchos (Domestic duck) (Anas boschas)
Taxonomic identifier8839 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeAnseriformesAnatidaeAnas

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Its physiological role is not yet clear.

Catalytic activity

An acylphosphate + H2O = a carboxylate + phosphate.

Sequence similarities

Belongs to the acylphosphatase family.

Contains 1 acylphosphatase-like domain.

Ontologies

Keywords
   Molecular functionHydrolase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular functionacylphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 103102Acylphosphatase-2
PRO_0000158547

Regions

Domain13 – 10391Acylphosphatase-like

Sites

Active site281 Potential
Active site461 Potential

Amino acid modifications

Modified residue21N-acetylserine

Sequences

Sequence LengthMass (Da)Tools
P14620 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 683D9EC280F40EB4

FASTA10311,389
        10         20         30         40         50         60 
MSTLGKAPGA LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTSQG TVTGQVQGPE 

        70         80         90        100 
DKVNAMKSWL TKVGSPSSRI DRTNFSNEKE ISKLDFSGFS TRY 

« Hide

References

[1]"Duck skeletal muscle acylphosphatase: primary structure."
Stefani M., Modesti A., Camici G., Manao G., Cappugi G., Berti A., Ramponi G.
J. Protein Chem. 5:307-321(1986)
Cited for: PROTEIN SEQUENCE OF 2-103.
Tissue: Skeletal muscle.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA45675.

3D structure databases

ProteinModelPortalP14620.
SMRP14620. Positions 11-103.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG050454.

Family and domain databases

InterProIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like.
IPR017968. Acylphosphatase_CS.
[Graphical view]
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...

Entry information

Entry nameACYP2_ANAPL
AccessionPrimary (citable) accession number: P14620
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 31, 2011
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families