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