ACYP2_HUMAN
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 03-AUG-2022, entry version 179.
DE RecName: Full=Acylphosphatase-2;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphatase, muscle type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 2;
GN Name=ACYP2; 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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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: 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 -!- 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_138448.3.
DR AlphaFoldDB; P14621; -.
DR BMRB; P14621; -.
DR SMR; P14621; -.
DR BioGRID; 106613; 12.
DR DIP; DIP-48449N; -.
DR IntAct; P14621; 3.
DR STRING; 9606.ENSP00000378161; -.
DR DrugBank; DB01942; Formic acid.
DR iPTMnet; P14621; -.
DR PhosphoSitePlus; P14621; -.
DR BioMuta; ACYP2; -.
DR EPD; P14621; -.
DR jPOST; P14621; -.
DR MassIVE; P14621; -.
DR MaxQB; P14621; -.
DR PaxDb; P14621; -.
DR PeptideAtlas; P14621; -.
DR PRIDE; P14621; -.
DR ProteomicsDB; 53066; -.
DR Antibodypedia; 30250; 115 antibodies from 23 providers.
DR DNASU; 98; -.
DR Ensembl; ENST00000394666.7; ENSP00000378161.3; ENSG00000170634.13.
DR GeneID; 98; -.
DR KEGG; hsa:98; -.
DR UCSC; uc002rxq.5; human.
DR CTD; 98; -.
DR DisGeNET; 98; -.
DR GeneCards; ACYP2; -.
DR HGNC; HGNC:180; ACYP2.
DR HPA; ENSG00000170634; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 102595; gene.
DR neXtProt; NX_P14621; -.
DR OpenTargets; ENSG00000170634; -.
DR PharmGKB; PA24500; -.
DR VEuPathDB; HostDB:ENSG00000170634; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00390000011103; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; P14621; -.
DR OMA; HAIMAEN; -.
DR OrthoDB; 1502266at2759; -.
DR PhylomeDB; P14621; -.
DR TreeFam; TF300288; -.
DR BRENDA; 3.6.1.7; 2681.
DR PathwayCommons; P14621; -.
DR SABIO-RK; P14621; -.
DR SignaLink; P14621; -.
DR BioGRID-ORCS; 98; 14 hits in 1080 CRISPR screens.
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 198 other tissues.
DR ExpressionAtlas; P14621; baseline and differential.
DR Genevisible; P14621; HS.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
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; Direct protein sequencing; Hydrolase; Phosphoprotein;
KW 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
