ACYP2_CHICK
ID ACYP2_CHICK Reviewed; 103 AA.
AC P07031;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acylphosphatase-2;
DE EC=3.6.1.7;
DE AltName: Full=Acylphosphatase isozyme CH1;
DE AltName: Full=Acylphosphatase, muscle type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 2;
GN Name=ACYP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP PROTEIN SEQUENCE OF 2-103, AND ACETYLATION AT SER-2.
RC TISSUE=Muscle;
RX PubMed=2830253; DOI=10.1093/oxfordjournals.jbchem.a122160;
RA Minowa O., Ohba Y., Mizuno Y., Shiokawa H.;
RT "The primary structure of chicken muscle acylphosphatase isozyme Ch1.";
RL J. Biochem. 102:1213-1220(1987).
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 -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR PIR; A41512; QPCH.
DR RefSeq; NP_001161234.1; NM_001167762.1.
DR AlphaFoldDB; P07031; -.
DR SMR; P07031; -.
DR STRING; 9031.ENSGALP00000041720; -.
DR iPTMnet; P07031; -.
DR PaxDb; P07031; -.
DR Ensembl; ENSGALT00000045290; ENSGALP00000041720; ENSGALG00000027632.
DR GeneID; 421217; -.
DR KEGG; gga:421217; -.
DR CTD; 98; -.
DR VEuPathDB; HostDB:geneid_421217; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00390000011103; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; P07031; -.
DR OMA; HAIMAEN; -.
DR OrthoDB; 1502266at2759; -.
DR PhylomeDB; P07031; -.
DR SABIO-RK; P07031; -.
DR PRO; PR:P07031; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000027632; Expressed in muscle tissue and 14 other tissues.
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; Direct protein sequencing; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..103
FT /note="Acylphosphatase-2"
FT /id="PRO_0000158548"
FT DOMAIN 13..103
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2830253"
SQ SEQUENCE 103 AA; 11409 MW; A54F5640514F05DA CRC64;
MSALTKASGS LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTSQG TVTGQVQGPE
DKVNAMKSWL SKVGSPSSRI DRTKFSNEKE ISKLDFSGFS TRY
