ID   ACYP2_HUMAN             Reviewed;          99 AA.
AC   P14621;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 198.
DE   RecName: Full=Acylphosphatase-2 {ECO:0000305};
DE            EC=3.6.1.7 {ECO:0000305|PubMed:8268218};
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=ACYP2 {ECO:0000312|HGNC:HGNC:180}; Synonyms=ACYP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8268218; DOI=10.1016/0167-4781(93)90003-v;
RA   Modesti A., Raugei G., Taddei N., Marzocchini R., Vecchi M., Camici G.,
RA   Manao G., Ramponi G.;
RT   "Chemical synthesis and expression of a gene coding for human muscle
RT   acylphosphatase.";
RL   Biochim. Biophys. Acta 1216:369-374(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-99.
RC   TISSUE=Muscle;
RX   PubMed=6100723;
RA   Manao G., Camici G., Modesti A., Liguri G., Berti A., Setfani M.,
RA   Cappugi G., Ramponi G.;
RT   "Human skeletal muscle acylphosphatase: the primary structure.";
RL   Mol. Biol. Med. 2:369-378(1984).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-99.
RC   TISSUE=Heart;
RX   PubMed=7796909; DOI=10.1016/0014-5793(95)00553-l;
RA   Fiaschi T., Raugei G., Marzocchini R., Chiarugi P., Cirri P., Ramponi G.;
RT   "Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of
RT   human acylphosphatase.";
RL   FEBS Lett. 367:145-148(1995).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: catalyzes the hydrolysis of acylphosphates compounds
CC       containing a carboxylphosphate bond. {ECO:0000269|PubMed:8268218}.
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:8268218};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14966;
CC         Evidence={ECO:0000305|PubMed:8268218};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.85 mM for benzoyl phosphate {ECO:0000269|PubMed:8268218};
CC       pH dependence:
CC         Optimum pH is 4.8-5.8. {ECO:0000269|PubMed:8268218};
CC   -!- INTERACTION:
CC       P14621; P14621: ACYP2; NbExp=3; IntAct=EBI-10198377, EBI-10198377;
CC       P14621; Q9NS37: CREBZF; NbExp=3; IntAct=EBI-10198377, EBI-632965;
CC       P14621; O00204: SULT2B1; NbExp=3; IntAct=EBI-10198377, EBI-749441;
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   EMBL; BC012290; AAH12290.1; -; mRNA.
DR   EMBL; X84195; CAA58988.1; -; mRNA.
DR   CCDS; CCDS1850.1; -.
DR   PIR; S59138; S52327.
DR   RefSeq; NP_612457.1; NM_138448.4.
DR   AlphaFoldDB; P14621; -.
DR   BMRB; P14621; -.
DR   SMR; P14621; -.
DR   BioGRID; 106613; 16.
DR   DIP; DIP-48449N; -.
DR   FunCoup; P14621; 98.
DR   IntAct; P14621; 7.
DR   STRING; 9606.ENSP00000475986; -.
DR   DrugBank; DB01942; Formic acid.
DR   GlyGen; P14621; 2 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; P14621; -.
DR   PhosphoSitePlus; P14621; -.
DR   BioMuta; ACYP2; -.
DR   jPOST; P14621; -.
DR   MassIVE; P14621; -.
DR   PaxDb; 9606-ENSP00000475986; -.
DR   PeptideAtlas; P14621; -.
DR   ProteomicsDB; 53066; -.
DR   Pumba; P14621; -.
DR   Antibodypedia; 30250; 122 antibodies from 23 providers.
DR   DNASU; 98; -.
DR   Ensembl; ENST00000394666.9; ENSP00000378161.3; ENSG00000170634.13.
DR   GeneID; 98; -.
DR   KEGG; hsa:98; -.
DR   MANE-Select; ENST00000394666.9; ENSP00000378161.3; NM_138448.4; NP_612457.1.
DR   UCSC; uc002rxq.5; human.
DR   AGR; HGNC:180; -.
DR   ClinPGx; PA24500; -.
DR   CTD; 98; -.
DR   DisGeNET; 98; -.
DR   GeneCards; ACYP2; -.
DR   HGNC; HGNC:180; ACYP2.
DR   HPA; ENSG00000170634; Tissue enhanced (brain, skeletal muscle, tongue).
DR   MalaCards; ACYP2; -.
DR   MIM; 102595; gene.
DR   OpenTargets; ENSG00000170634; -.
DR   VEuPathDB; HostDB:ENSG00000170634; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   GeneTree; ENSGT00390000011103; -.
DR   HOGENOM; CLU_141932_0_1_1; -.
DR   InParanoid; P14621; -.
DR   OMA; ADKMNNM; -.
DR   OrthoDB; 7961613at2759; -.
DR   PAN-GO; P14621; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; P14621; -.
DR   BRENDA; 3.6.1.7; 2681.
DR   PathwayCommons; P14621; -.
DR   SABIO-RK; P14621; -.
DR   SignaLink; P14621; -.
DR   Agora; ENSG00000170634; -.
DR   BioGRID-ORCS; 98; 14 hits in 1161 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; ACYP2; human.
DR   GeneWiki; ACYP2; -.
DR   GenomeRNAi; 98; -.
DR   Pharos; P14621; Tbio.
DR   PRO; PR:P14621; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P14621; protein.
DR   Bgee; ENSG00000170634; Expressed in pons and 200 other cell types or tissues.
DR   ExpressionAtlas; P14621; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0003998; F:acylphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
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   Proteomics identification; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6100723,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..99
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158542"
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:0007744|PubMed:22814378"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35745"
SQ   SEQUENCE   99 AA;  11140 MW;  AEDE40E45B6207A0 CRC64;
     MSTAQSLKSV DYEVFGRVQG VCFRMYTEDE ARKIGVVGWV KNTSKGTVTG QVQGPEDKVN
     SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSIRY
//