ID   ACYP2_RAT               Reviewed;          97 AA.
AC   P35745;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=Acylphosphatase-2 {ECO:0000305};
DE            EC=3.6.1.7 {ECO:0000305|PubMed:1647162};
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=Acyp2 {ECO:0000312|RGD:1595836}; Synonyms=Acyp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-97, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT ALA-2.
RC   TISSUE=Skeletal muscle;
RX   PubMed=1647162; DOI=10.1007/bf01024659;
RA   Berti A., Tremori E., Pazzagli L., Degl'Innocenti D., Camici G.,
RA   Cappugi G., Manoa G., Ramponi G.;
RT   "Rat muscle acylphosphatase: purification, amino sequence, and
RT   immunological characterization.";
RL   J. Protein Chem. 10:91-102(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 44-56, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: catalyzes the hydrolysis of acylphosphates compounds
CC       containing a carboxylphosphate bond. {ECO:0000269|PubMed:1647162}.
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:0000305|PubMed:1647162};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14966;
CC         Evidence={ECO:0000305|PubMed:1647162};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 mM for benzoyl phosphate {ECO:0000269|PubMed:1647162};
CC       pH dependence:
CC         Optimum pH is 5.3. {ECO:0000269|PubMed:1647162};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   PIR; A61427; A61427.
DR   AlphaFoldDB; P35745; -.
DR   SMR; P35745; -.
DR   FunCoup; P35745; 807.
DR   STRING; 10116.ENSRNOP00000061028; -.
DR   iPTMnet; P35745; -.
DR   PhosphoSitePlus; P35745; -.
DR   PaxDb; 10116-ENSRNOP00000061028; -.
DR   AGR; RGD:1595836; -.
DR   RGD; 1595836; Acyp2.
DR   eggNOG; KOG3360; Eukaryota.
DR   InParanoid; P35745; -.
DR   PhylomeDB; P35745; -.
DR   PRO; PR:P35745; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0003998; F:acylphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1647162"
FT   CHAIN           2..97
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158546"
FT   DOMAIN          7..97
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1647162"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   97 AA;  10863 MW;  12947520EF12F4BB CRC64;
     MAEPLKSVDY EVFGTVQGVC FRMYTEGEAK KRGLVGWVKN TSKGTVTGQV QGPEEKVNSM
     KSWLSKVGSP SSRIDRADFS NEKTISKLEY SNFSIRY
//