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ACYP2_DROME
ID   ACYP2_DROME             Reviewed;         102 AA.
AC   Q9VF36; Q29QI6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Acylphosphatase-2;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
DE            Short=AcPDro2;
GN   Name=Acyp2 {ECO:0000312|EMBL:AAF55224.1}; ORFNames=CG18505;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAF55224.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAF55224.1}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   CATALYTIC ACTIVITY, MASS SPECTROMETRY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12560098; DOI=10.1016/s0014-5793(02)03901-7;
RA   Degl'Innocenti D., Ramazzotti M., Marzocchini R., Chiti F., Raugei G.,
RA   Ramponi G.;
RT   "Characterization of a novel Drosophila melanogaster acylphosphatase.";
RL   FEBS Lett. 535:171-174(2003).
RN   [5] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=15159593; DOI=10.1107/s0907444904006808;
RA   Zuccotti S., Rosano C., Ramazzotti M., Degl'Innocenti D., Stefani M.,
RA   Manao G., Bolognesi M.;
RT   "Three-dimensional structural characterization of a novel Drosophila
RT   melanogaster acylphosphatase.";
RL   Acta Crystallogr. D 60:1177-1179(2004).
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:0000269|PubMed:12560098};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.80 mM for benzoylphosphate {ECO:0000269|PubMed:12560098};
CC       pH dependence:
CC         Optimum pH is 4.8-5.8. {ECO:0000269|PubMed:12560098};
CC   -!- MASS SPECTROMETRY: Mass=11778; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12560098};
CC   -!- SIMILARITY: Belongs to the acylphosphatase family.
CC       {ECO:0000269|PubMed:12560098, ECO:0000269|PubMed:15159593}.
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DR   EMBL; AE014297; AAF55224.1; -; Genomic_DNA.
DR   EMBL; BT024404; ABC86466.1; -; mRNA.
DR   RefSeq; NP_001262612.1; NM_001275683.1.
DR   RefSeq; NP_650491.1; NM_142234.2.
DR   PDB; 1URR; X-ray; 1.50 A; A=1-102.
DR   PDBsum; 1URR; -.
DR   AlphaFoldDB; Q9VF36; -.
DR   SMR; Q9VF36; -.
DR   STRING; 7227.FBpp0082628; -.
DR   PaxDb; Q9VF36; -.
DR   PRIDE; Q9VF36; -.
DR   DNASU; 41910; -.
DR   EnsemblMetazoa; FBtr0083174; FBpp0082628; FBgn0038363.
DR   EnsemblMetazoa; FBtr0334591; FBpp0306658; FBgn0038363.
DR   GeneID; 41910; -.
DR   KEGG; dme:Dmel_CG18505; -.
DR   CTD; 98; -.
DR   FlyBase; FBgn0038363; Acyp2.
DR   VEuPathDB; VectorBase:FBgn0038363; -.
DR   eggNOG; KOG3360; Eukaryota.
DR   GeneTree; ENSGT00940000166472; -.
DR   HOGENOM; CLU_141932_0_1_1; -.
DR   InParanoid; Q9VF36; -.
DR   OMA; TNGIMAG; -.
DR   OrthoDB; 1502266at2759; -.
DR   PhylomeDB; Q9VF36; -.
DR   SABIO-RK; Q9VF36; -.
DR   BioGRID-ORCS; 41910; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Acyp2; fly.
DR   EvolutionaryTrace; Q9VF36; -.
DR   GenomeRNAi; 41910; -.
DR   PRO; PR:Q9VF36; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0038363; Expressed in testis and 26 other tissues.
DR   ExpressionAtlas; Q9VF36; baseline and differential.
DR   Genevisible; Q9VF36; DM.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0003998; F:acylphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
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; PS51160; ACYLPHOSPHATASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..102
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158551"
FT   DOMAIN          12..102
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        27
FT                   /evidence="ECO:0000303|PubMed:12560098"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000303|PubMed:12560098"
FT   STRAND          10..20
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   HELIX           26..37
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          40..45
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   HELIX           59..71
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:1URR"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1URR"
SQ   SEQUENCE   102 AA;  11766 MW;  3CDC09E7FF96FBDE CRC64;
     MAGSGVAKQI FALDFEIFGR VQGVFFRKHT SHEAKRLGVR GWCMNTRDGT VKGQLEAPMM
     NLMEMKHWLE NNRIPNAKVS KAEFSQIQEI EDYTFTSFDI KH
 
 
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