ID   ACYP2_CHICK             Reviewed;         103 AA.
AC   P07031;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=Acylphosphatase-2 {ECO:0000250|UniProtKB:P14621};
DE            EC=3.6.1.7 {ECO:0000250|UniProtKB:P14621};
DE   AltName: Full=Acylphosphatase isozyme CH1;
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=ACYP2 {ECO:0000250|UniProtKB:P14621};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-103, AND ACETYLATION AT SER-2.
RC   TISSUE=Muscle;
RX   PubMed=2830253; DOI=10.1093/oxfordjournals.jbchem.a122160;
RA   Minowa O., Ohba Y., Mizuno Y., Shiokawa H.;
RT   "The primary structure of chicken muscle acylphosphatase isozyme Ch1.";
RL   J. Biochem. 102:1213-1220(1987).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A41512; QPCH.
DR   RefSeq; NP_001161234.1; NM_001167762.1.
DR   AlphaFoldDB; P07031; -.
DR   SMR; P07031; -.
DR   FunCoup; P07031; 969.
DR   STRING; 9031.ENSGALP00000041720; -.
DR   iPTMnet; P07031; -.
DR   PaxDb; 9031-ENSGALP00000041720; -.
DR   GeneID; 421217; -.
DR   KEGG; gga:421217; -.
DR   CTD; 98; -.
DR   VEuPathDB; HostDB:geneid_421217; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   HOGENOM; CLU_141932_0_1_1; -.
DR   InParanoid; P07031; -.
DR   OMA; HAIMAEN; -.
DR   OrthoDB; 7961613at2759; -.
DR   PhylomeDB; P07031; -.
DR   SABIO-RK; P07031; -.
DR   PRO; PR:P07031; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000027632; Expressed in muscle tissue and 14 other cell types or tissues.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..103
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158548"
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:2830253"
SQ   SEQUENCE   103 AA;  11409 MW;  A54F5640514F05DA CRC64;
     MSALTKASGS LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTSQG TVTGQVQGPE
     DKVNAMKSWL SKVGSPSSRI DRTKFSNEKE ISKLDFSGFS TRY
//