ID   ACYP2_CAVPO             Reviewed;          99 AA.
AC   P35744;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 105.
DE   RecName: Full=Acylphosphatase-2 {ECO:0000250|UniProtKB:P14621};
DE            EC=3.6.1.7 {ECO:0000250|UniProtKB:P14621};
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=ACYP2 {ECO:0000250|UniProtKB:P14621}; Synonyms=ACYP;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-99, AND ACETYLATION AT SER-2.
RC   TISSUE=Skeletal muscle;
RX   PubMed=2855598; DOI=10.1007/bf01024889;
RA   Manao G., Cappugi G., Modesti A., Stefani M., Marzocchini R.,
RA   Degl'Innocenti D., Camici G.;
RT   "Guinea pig acylphosphatase: the amino acid sequence.";
RL   J. Protein Chem. 7:417-426(1988).
CC   -!- FUNCTION: catalyzes the hydrolysis of acylphosphates compounds
CC       containing a carboxylphosphate bond. {ECO:0000250|UniProtKB:P14621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + phosphate + H(+);
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000250|UniProtKB:P14621};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14966;
CC         Evidence={ECO:0000250|UniProtKB:P14621};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   PIR; A60893; QPGP.
DR   AlphaFoldDB; P35744; -.
DR   SMR; P35744; -.
DR   FunCoup; P35744; 572.
DR   STRING; 10141.ENSCPOP00000007930; -.
DR   iPTMnet; P35744; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   InParanoid; P35744; -.
DR   OMA; ADKMNNM; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0003998; F:acylphosphatase activity; ISS:UniProtKB.
DR   FunFam; 3.30.70.100:FF:000011; Acylphosphatase; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR10029; ACYLPHOSPHATASE; 1.
DR   PANTHER; PTHR10029:SF20; ACYLPHOSPHATASE-2; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrolase; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P14621"
FT   CHAIN           2..99
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158540"
FT   DOMAIN          9..99
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2855598"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35745"
SQ   SEQUENCE   99 AA;  11007 MW;  1DF22894292E5137 CRC64;
     MSAAAQLKSV DYEVFGRVQG VCFRMYTEGE AKKIGVVGWV KNTSKGTVTG QVQGPEEKVN
     SMKSWLSKVG SPSSRIDRTN FSNEKSISKL EYSNFSIRY
//