ID   ACYP1_PIG               Reviewed;         101 AA.
AC   P24540;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Acylphosphatase-1;
DE            EC=3.6.1.7 {ECO:0000305|PubMed:1664426};
DE   AltName: Full=Acylphosphatase, organ-common type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 1;
GN   Name=ACYP1; Synonyms=ACYPE;
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 2-101, PROTEIN SEQUENCE OF 4-101 (ISOFORM ACYA),
RP   ACETYLATION AT SER-2, ACETYLATION AT ALA-2 (ISOFORM ACYA), AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Brain, and Testis;
RX   PubMed=1664426; DOI=10.1093/oxfordjournals.jbchem.a123661;
RA   Mizuno Y., Kanesaka Y., Fujita H., Minowa O., Shiokawa H.;
RT   "The primary structure of two molecular species of porcine organ-common
RT   type acylphosphatase.";
RL   J. Biochem. 110:790-794(1991).
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         Evidence={ECO:0000305|PubMed:1664426};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC         Comment=It is uncertain whether isoform ACYA is produced by
CC         alternative initiation or another biological event.;
CC       Name=ACYB;
CC         IsoId=P24540-1; Sequence=Displayed;
CC       Name=ACYA;
CC         IsoId=P24540-2; Sequence=VSP_026024;
CC   -!- TISSUE SPECIFICITY: Organ-common type isozyme is found in many
CC       different tissues.
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   RefSeq; NP_001177128.1; NM_001190199.1. [P24540-1]
DR   RefSeq; XP_005656433.1; XM_005656376.2. [P24540-1]
DR   AlphaFoldDB; P24540; -.
DR   SMR; P24540; -.
DR   STRING; 9823.ENSSSCP00000002579; -.
DR   iPTMnet; P24540; -.
DR   PaxDb; P24540; -.
DR   PeptideAtlas; P24540; -.
DR   PRIDE; P24540; -.
DR   GeneID; 100155997; -.
DR   KEGG; ssc:100155997; -.
DR   CTD; 97; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   HOGENOM; CLU_1781825_0_0_1; -.
DR   InParanoid; P24540; -.
DR   OrthoDB; 735423at2759; -.
DR   SABIO-RK; P24540; -.
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; Alternative initiation; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1664426"
FT   CHAIN           2..101
FT                   /note="Acylphosphatase-1"
FT                   /id="PRO_0000158537"
FT   DOMAIN          11..101
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1664426"
FT   VAR_SEQ         1..2
FT                   /note="Missing (in isoform ACYA)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_026024"
FT   INIT_MET        P24540-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1664426"
FT   MOD_RES         P24540-2:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1664426"
SQ   SEQUENCE   101 AA;  11427 MW;  F707C03DEE1BF18A CRC64;
     MSMAEGDTLI SVDYEVFGKV QGVFFRKYTQ AEGKKLGLVG WVQNTDQGTV QGQLQGPTSK
     VRHMQEWLET RGSPKSHIDR ASFNNEKVIS KLDYSDFQIV K