ID ACYP2_MELGA Reviewed; 103 AA.
AC P00821;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-FEB-2023, entry version 106.
DE RecName: Full=Acylphosphatase-2;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphatase isozyme TU1;
DE AltName: Full=Acylphosphatase, muscle type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 2;
GN Name=ACYP2;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP PROTEIN SEQUENCE OF 2-103, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND GLUTATHIONYLATION AT CYS-26.
RC TISSUE=Skeletal muscle;
RX PubMed=6317387; DOI=10.1111/j.1432-1033.1983.tb07825.x;
RA Camici G., Manao G., Cappugi G., Berti A., Stefani M., Liguri G.,
RA Ramponi G.;
RT "The primary structure of turkey muscle acylphosphatase.";
RL Eur. J. Biochem. 137:269-277(1983).
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 -!- SUBUNIT: Monomer (TU1) or homodimer (TU3) in absence of reducing
CC factors; disulfide linked.
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR PIR; A01018; QPTK.
DR AlphaFoldDB; P00821; -.
DR SMR; P00821; -.
DR iPTMnet; P00821; -.
DR InParanoid; P00821; -.
DR Proteomes; UP000001645; Unplaced.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
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; Disulfide bond; Glutathionylation;
KW Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Acylphosphatase-2"
FT /id="PRO_0000158549"
FT DOMAIN 13..103
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6317387"
FT MOD_RES 26
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:6317387"
FT DISULFID 26
FT /note="Interchain; alternate"
SQ SEQUENCE 103 AA; 11448 MW; 23D12EB987EC37C8 CRC64;
MSALTKASGA LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTRQG TVTGQVQGPE
DKVNAMKSWL SKVGSPSSRI DRTNFSNEKE ISKLDFSGFS TRY
//
