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ACYP2_PIG
ID   ACYP2_PIG               Reviewed;          99 AA.
AC   P00819;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 102.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-99, AND ACETYLATION AT SER-2.
RC   TISSUE=Skeletal muscle;
RX   PubMed=2993259; DOI=10.1093/oxfordjournals.jbchem.a135158;
RA   Mizuno Y., Yamazaki M., Takasawa T., Kizaki T., Shiokawa H.;
RT   "Amino acid sequence of acylphosphatase from porcine skeletal muscle.";
RL   J. Biochem. 97:1135-1142(1985).
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; A01016; QPPG.
DR   AlphaFoldDB; P00819; -.
DR   SMR; P00819; -.
DR   STRING; 9823.ENSSSCP00000021583; -.
DR   iPTMnet; P00819; -.
DR   PeptideAtlas; P00819; -.
DR   PRIDE; P00819; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   InParanoid; P00819; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   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_0000158544"
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:2993259"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35745"
SQ   SEQUENCE   99 AA;  11206 MW;  0A9CBC9831A42961 CRC64;
     MSTARPLKSV DYEVFGRVQG VCFRMYTEDE ARKIGVVGWV KNTSKGTVTG QVQGPEEKVN
     SMKSWLSKIG SPSSRIDRTN FSNEKTISKL EYSNFSIRY
 
 
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