ID   ACYP2_HORSE             Reviewed;          99 AA.
AC   P00818;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Acylphosphatase-2;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=ACYP2; Synonyms=ACYP;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-99, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   SER-2, AND GLUTATHIONYLATION AT CYS-22.
RC   TISSUE=Muscle;
RX   PubMed=6248536; DOI=10.1016/s0021-9258(18)43654-x;
RA   Cappugi G., Manao G., Camici G., Ramponi G.;
RT   "The complete amino acid sequence of horse muscle acylphosphatase.";
RL   J. Biol. Chem. 255:6868-6874(1980).
RN   [2]
RP   STRUCTURE BY NMR OF ALPHA HELICES.
RX   PubMed=2538623; DOI=10.1016/0022-2836(89)90377-x;
RA   Saudek V., Atkinson R.A., Williams R.J.P., Ramponi G.;
RT   "Identification and description of alpha-helical regions in horse muscle
RT   acylphosphatase by 1H nuclear magnetic resonance spectroscopy.";
RL   J. Mol. Biol. 205:229-239(1989).
RN   [3]
RP   STRUCTURE BY NMR OF BETA-STRUCTURES.
RX   PubMed=2547076; DOI=10.1016/0022-2836(89)90263-5;
RA   Saudek V., Wormald M.R., Williams R.J.P., Boyd J., Stefani M., Ramponi G.;
RT   "Identification and description of beta-structure in horse muscle
RT   acylphosphatase by nuclear magnetic resonance spectroscopy.";
RL   J. Mol. Biol. 207:405-415(1989).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=1313885; DOI=10.1016/0022-2836(92)91005-a;
RA   Pastore A., Saudek V., Ramponi G., Williams R.J.P.;
RT   "Three-dimensional structure of acylphosphatase. Refinement and structure
RT   analysis.";
RL   J. Mol. Biol. 224:427-440(1992).
CC   -!- FUNCTION: Its physiological role is not yet clear.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
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   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   PIR; A01015; QPHO.
DR   PDB; 1APS; NMR; -; A=2-99.
DR   PDBsum; 1APS; -.
DR   AlphaFoldDB; P00818; -.
DR   BMRB; P00818; -.
DR   SMR; P00818; -.
DR   STRING; 9796.ENSECAP00000049256; -.
DR   iPTMnet; P00818; -.
DR   PaxDb; P00818; -.
DR   PeptideAtlas; P00818; -.
DR   HOGENOM; CLU_141932_0_1_1; -.
DR   InParanoid; P00818; -.
DR   OMA; HAIMAEN; -.
DR   TreeFam; TF300288; -.
DR   EvolutionaryTrace; P00818; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
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; PTHR10029; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; SSF54975; 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   3D-structure; Acetylation; Direct protein sequencing; Glutathionylation;
KW   Hydrolase; Phosphoprotein; 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_0000158541"
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:6248536"
FT   MOD_RES         22
FT                   /note="S-glutathionyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:6248536"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35745"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   HELIX           26..34
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          47..55
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   HELIX           56..64
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          79..89
FT                   /evidence="ECO:0007829|PDB:1APS"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:1APS"
SQ   SEQUENCE   99 AA;  11148 MW;  911DAF1820A53790 CRC64;
     MSTARPLKSV DYEVFGRVQG VCFRMYAEDE ARKIGVVGWV KNTSKGTVTG QVQGPEEKVN
     SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSVRY