ACYP2_RABIT
ID ACYP2_RABIT Reviewed; 99 AA.
AC P00820;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 117.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 2-99.
RC TISSUE=Skeletal muscle;
RX PubMed=2993260; DOI=10.1093/oxfordjournals.jbchem.a135160;
RA Kizaki T., Takasawa T., Mizuno Y., Shiokawa H.;
RT "Amino acid sequence of acylphosphatase from rabbit skeletal muscle.";
RL J. Biochem. 97:1155-1161(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-99, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND GLUTATHIONYLATION AT CYS-22.
RC TISSUE=Skeletal muscle;
RX PubMed=2994566; DOI=10.1016/0003-9861(85)90565-x;
RA Manao G., Camici G., Cappugi G., Stefani M., Liguri G., Berti A.,
RA Ramponi G.;
RT "Rabbit skeletal muscle acylphosphatase: the amino acid sequence of form
RT Ra1.";
RL Arch. Biochem. Biophys. 241:418-423(1985).
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 -!- SUBUNIT: Monomer (RA1) and homodimer (RA3); disulfide linked.
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; A91988; QPRB.
DR AlphaFoldDB; P00820; -.
DR SMR; P00820; -.
DR STRING; 9986.ENSOCUP00000013234; -.
DR iPTMnet; P00820; -.
DR eggNOG; KOG3360; Eukaryota.
DR InParanoid; P00820; -.
DR TreeFam; TF300288; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
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; Disulfide bond; Glutathionylation;
KW Hydrolase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P14621"
FT CHAIN 2..99
FT /note="Acylphosphatase-2"
FT /id="PRO_0000158545"
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:0000269|PubMed:2993260,
FT ECO:0000269|PubMed:2994566"
FT MOD_RES 22
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:2994566"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35745"
FT DISULFID 22
FT /note="Interchain; alternate"
SQ SEQUENCE 99 AA; 10992 MW; 1EB9AA7CF8F13620 CRC64;
MSTAGPLKSV DYEVFGRVQG VCFRMYTEGE AKKIGVVGWV KNTSKGTVTG QVQGPEDKVN
SMKSWLSKVG SPSSRIDRTN FSNEKTISKL EYSNFSIRY
