ACYP1_BOVIN
ID ACYP1_BOVIN Reviewed; 101 AA.
AC P41500; Q1RMH2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Acylphosphatase-1;
DE EC=3.6.1.7 {ECO:0000305|PubMed:8142002};
DE AltName: Full=Acylphosphatase, erythrocyte/testis isozyme;
DE AltName: Full=Acylphosphatase, organ-common type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 1;
GN Name=ACYP1; Synonyms=ACYPE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ACY2).
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-101 (ISOFORM ACY2), AND ACETYLATION AT SER-2.
RC TISSUE=Erythrocyte;
RX PubMed=8262761;
RA Pazzagli L., Ikram U.K., Liguri G., Taddei N., Gentilini A., Cecchi C.,
RA Manao G., Cappugi G.;
RT "Purification, kinetic properties and primary structure of bovine
RT erythrocyte acylphosphatase.";
RL Ital. J. Biochem. 42:233-245(1993).
RN [3]
RP PROTEIN SEQUENCE OF 2-101, PROTEIN SEQUENCE OF 4-101 (ISOFORM ACY1),
RP ACETYLATION AT SER-2, ACETYLATION AT ALA-2 (ISOFORM ACY1), AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Testis;
RX PubMed=8142002; DOI=10.1007/bf01025124;
RA Pazzagli L., Cappugi G., Camici G., Manao G., Ramponi G.;
RT "Bovine testis acylphosphatase: purification and amino acid sequence.";
RL J. Protein Chem. 12:593-601(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-101 (ISOFORM ACY1).
RC TISSUE=Testis;
RX PubMed=9016712; DOI=10.1016/s0969-2126(97)00167-6;
RA Thunnissen M.M.G.M., Taddei N., Liguri G., Ramponi G., Nordlund P.;
RT "Crystal structure of common type acylphosphatase from bovine testis.";
RL Structure 5:69-79(1997).
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 Evidence={ECO:0000305|PubMed:8142002};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=It is uncertain whether isoform ACY1 is produced by
CC alternative initiation or another biological event.;
CC Name=ACY2;
CC IsoId=P41500-1; Sequence=Displayed;
CC Name=ACY1;
CC IsoId=P41500-2; Sequence=VSP_026023;
CC -!- TISSUE SPECIFICITY: Organ-common type isozyme is found in many
CC different tissues.
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; BC114901; AAI14902.1; -; mRNA.
DR PIR; A61449; A61449.
DR RefSeq; NP_001039447.1; NM_001045982.2. [P41500-1]
DR RefSeq; XP_005212005.1; XM_005211948.3. [P41500-1]
DR PDB; 2ACY; X-ray; 1.80 A; A=4-101.
DR PDBsum; 2ACY; -.
DR AlphaFoldDB; P41500; -.
DR SMR; P41500; -.
DR STRING; 9913.ENSBTAP00000018595; -.
DR iPTMnet; P41500; -.
DR PaxDb; P41500; -.
DR PRIDE; P41500; -.
DR Ensembl; ENSBTAT00000018595; ENSBTAP00000018595; ENSBTAG00000013992. [P41500-1]
DR GeneID; 507844; -.
DR KEGG; bta:507844; -.
DR CTD; 97; -.
DR VEuPathDB; HostDB:ENSBTAG00000013992; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00390000011103; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; P41500; -.
DR OMA; FRKYTQG; -.
DR OrthoDB; 1502266at2759; -.
DR TreeFam; TF300288; -.
DR SABIO-RK; P41500; -.
DR EvolutionaryTrace; P41500; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000013992; Expressed in semen and 106 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 3D-structure; Acetylation; Alternative initiation;
KW Direct protein sequencing; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8262761"
FT CHAIN 2..101
FT /note="Acylphosphatase-1"
FT /id="PRO_0000158534"
FT DOMAIN 11..101
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:8262761"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform ACY1)"
FT /evidence="ECO:0000305"
FT /id="VSP_026023"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:2ACY"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2ACY"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:2ACY"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2ACY"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2ACY"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2ACY"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:2ACY"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2ACY"
FT INIT_MET P41500-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8142002"
FT MOD_RES P41500-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8142002"
SQ SEQUENCE 101 AA; 11432 MW; 92DC05E7BF0D86B7 CRC64;
MSMAEGDTLI SVDYEIFGKV QGVFFRKYTQ AEGKKLGLVG WVQNTDQGTV QGQLQGPASK
VRHMQEWLET KGSPKSHIDR ASFHNEKVIV KLDYTDFQIV K
