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Database: UniProt
Entry: O75608
LinkDB: O75608
Original site: O75608 
ID   LYPA1_HUMAN             Reviewed;         230 AA.
AC   O75608; O43202; Q9UQF9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   29-SEP-2021, entry version 185.
DE   RecName: Full=Acyl-protein thioesterase 1;
DE            Short=APT-1;
DE            Short=hAPT1;
DE            EC=3.1.2.-;
DE   AltName: Full=Lysophospholipase 1;
DE   AltName: Full=Lysophospholipase I;
DE            Short=LPL-I;
DE            Short=LysoPLA I;
GN   Name=LYPLA1; Synonyms=APT1, LPL1;
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 [MRNA] (ISOFORM 1).
RA   Hu G.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (1.5
RP   ANGSTROMS) OF 6-230, SUBUNIT, AND ACTIVE SITE.
RC   TISSUE=Testis;
RX   PubMed=11080636; DOI=10.1016/s0969-2126(00)00529-3;
RA   Devedjiev Y., Dauter Z., Kuznetsov S.R., Jones T.L.Z., Derewenda Z.S.;
RT   "Crystal structure of the human acyl protein thioesterase I from a single
RT   X-ray data set to 1.5 A.";
RL   Structure 8:1137-1146(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow, and Eye;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-230 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Yu W., Sarginson J., Gibbs R.A.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   SER-119.
RX   PubMed=19439193; DOI=10.1016/j.bbalip.2009.05.001;
RA   Hirano T., Kishi M., Sugimoto H., Taguchi R., Obinata H., Ohshima N.,
RA   Tatei K., Izumi T.;
RT   "Thioesterase activity and subcellular localization of acylprotein
RT   thioesterase 1/lysophospholipase 1.";
RL   Biochim. Biophys. Acta 1791:797-805(2009).
RN   [7]
RP   ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=20418879; DOI=10.1038/nchembio.362;
RA   Dekker F.J., Rocks O., Vartak N., Menninger S., Hedberg C., Balamurugan R.,
RA   Wetzel S., Renner S., Gerauer M., Scholermann B., Rusch M., Kramer J.W.,
RA   Rauh D., Coates G.W., Brunsveld L., Bastiaens P.I., Waldmann H.;
RT   "Small-molecule inhibition of APT1 affects Ras localization and
RT   signaling.";
RL   Nat. Chem. Biol. 6:449-456(2010).
RN   [8]
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   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=21393252; DOI=10.1194/jlr.m013326;
RA   Bolen A.L., Naren A.P., Yarlagadda S., Beranova-Giorgianni S., Chen L.,
RA   Norman D., Baker D.L., Rowland M.M., Best M.D., Sano T., Tsukahara T.,
RA   Liliom K., Igarashi Y., Tigyi G.;
RT   "The phospholipase A1 activity of lysophospholipase A-I links platelet
RT   activation to LPA production during blood coagulation.";
RL   J. Lipid Res. 52:958-970(2011).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22399288; DOI=10.1074/jbc.m111.335547;
RA   Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
RT   "Distinct acyl protein transferases and thioesterases control surface
RT   expression of calcium-activated potassium channels.";
RL   J. Biol. Chem. 287:14718-14725(2012).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   FUNCTION.
RX   PubMed=27481942; DOI=10.1074/jbc.m116.725762;
RA   Adachi N., Hess D.T., McLaughlin P., Stamler J.S.;
RT   "S-Palmitoylation of a Novel Site in the beta2-Adrenergic Receptor
RT   Associated with a Novel Intracellular Itinerary.";
RL   J. Biol. Chem. 291:20232-20246(2016).
CC   -!- FUNCTION: Acts as a acyl-protein thioesterase (PubMed:19439193,
CC       PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine
CC       residues in proteins such as trimeric G alpha proteins or HRAS
CC       (PubMed:20418879). Has depalmitoylating activity toward KCNMA1
CC       (PubMed:22399288). Could also depalmitoylate ADRB2 (PubMed:27481942).
CC       Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine
CC       (lyso-PC) (PubMed:19439193). Also hydrolyzes
CC       lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-
CC       PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much
CC       higher thioesterase activity than lysophospholipase activity
CC       (PubMed:19439193). Contributes to the production of lysophosphatidic
CC       acid (LPA) during blood coagulation by recognizing and cleaving plasma
CC       phospholipids to generate lysophospholipids which in turn act as
CC       substrates for ENPP2 to produce LPA (PubMed:21393252).
CC       {ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:19439193,
CC       ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:21393252,
CC       ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:27481942}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC         hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:74151; Evidence={ECO:0000269|PubMed:22399288};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:19439193};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:19439193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O
CC         = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:41720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57875, ChEBI:CHEBI:78421;
CC         Evidence={ECO:0000269|PubMed:21393252};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721;
CC         Evidence={ECO:0000305|PubMed:21393252};
CC   -!- ACTIVITY REGULATION: Inhibited by palmostatin-B, leading to impair
CC       depalmitoylating of Ras. {ECO:0000269|PubMed:20418879}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.3 uM for lysophosphatidylcholine for lysophospholipase activity
CC         {ECO:0000269|PubMed:19439193};
CC         KM=3.49 uM for thioesterase activity {ECO:0000269|PubMed:19439193};
CC         Vmax=1.62 umol/min/mg enzyme toward lysophosphatidylcholine for
CC         lysophospholipase activity {ECO:0000269|PubMed:19439193};
CC         Vmax=27.3 umol/min/mg enzyme for thioesterase activity
CC         {ECO:0000269|PubMed:19439193};
CC       pH dependence:
CC         Optimum pH is 7.4 for the thioesterase activity.
CC         {ECO:0000269|PubMed:19439193};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11080636}.
CC   -!- INTERACTION:
CC       O75608; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1052185, EBI-618309;
CC       O75608; Q5VUG0: SFMBT2; NbExp=3; IntAct=EBI-1052185, EBI-12025260;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell
CC       membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane
CC       {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic
CC       localization with a weak expression in the cell membrane, nuclear
CC       membrane and endoplasmic reticulum. {ECO:0000269|PubMed:19439193}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O75608-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75608-2; Sequence=VSP_009196;
CC   -!- TISSUE SPECIFICITY: Platelets. {ECO:0000269|PubMed:21393252}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB88180.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF081281; AAC31610.1; -; mRNA.
DR   EMBL; AF291053; AAG10063.1; -; mRNA.
DR   EMBL; AF077198; AAD26993.1; -; mRNA.
DR   EMBL; AF077199; AAD26994.1; -; mRNA.
DR   EMBL; BC008652; AAH08652.1; -; mRNA.
DR   EMBL; BC010397; AAH10397.1; -; mRNA.
DR   EMBL; AF035293; AAB88180.1; ALT_INIT; mRNA.
DR   CCDS; CCDS6157.1; -. [O75608-1]
DR   CCDS; CCDS64899.1; -. [O75608-2]
DR   RefSeq; NP_001266285.1; NM_001279356.1.
DR   RefSeq; NP_001266286.1; NM_001279357.1. [O75608-2]
DR   RefSeq; NP_001266287.1; NM_001279358.1.
DR   RefSeq; NP_001266288.1; NM_001279359.1.
DR   RefSeq; NP_001266289.1; NM_001279360.1.
DR   RefSeq; NP_006321.1; NM_006330.3. [O75608-1]
DR   PDB; 1FJ2; X-ray; 1.50 A; A/B=6-230.
DR   PDB; 5SYM; X-ray; 1.55 A; A/B=1-230.
DR   PDB; 6QGN; X-ray; 2.10 A; A/B/C/D=1-230.
DR   PDB; 6QGO; X-ray; 2.60 A; B/C=1-230.
DR   PDB; 6QGQ; X-ray; 2.60 A; A/B/C/D=1-230.
DR   PDB; 6QGS; X-ray; 2.75 A; A/B/C/D/E/F=1-230.
DR   PDBsum; 1FJ2; -.
DR   PDBsum; 5SYM; -.
DR   PDBsum; 6QGN; -.
DR   PDBsum; 6QGO; -.
DR   PDBsum; 6QGQ; -.
DR   PDBsum; 6QGS; -.
DR   SMR; O75608; -.
DR   BioGRID; 115701; 46.
DR   IntAct; O75608; 12.
DR   STRING; 9606.ENSP00000320043; -.
DR   BindingDB; O75608; -.
DR   ChEMBL; CHEMBL1681631; -.
DR   SwissLipids; SLP:000000734; -.
DR   ESTHER; human-LYPLA1; LYsophospholipase_carboxylesterase.
DR   MEROPS; S09.941; -.
DR   GlyGen; O75608; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O75608; -.
DR   PhosphoSitePlus; O75608; -.
DR   SwissPalm; O75608; -.
DR   BioMuta; LYPLA1; -.
DR   OGP; O75608; -.
DR   CPTAC; CPTAC-536; -.
DR   CPTAC; CPTAC-537; -.
DR   EPD; O75608; -.
DR   jPOST; O75608; -.
DR   MassIVE; O75608; -.
DR   PaxDb; O75608; -.
DR   PeptideAtlas; O75608; -.
DR   PRIDE; O75608; -.
DR   ProteomicsDB; 50117; -. [O75608-1]
DR   ProteomicsDB; 50118; -. [O75608-2]
DR   Antibodypedia; 24492; 313 antibodies.
DR   DNASU; 10434; -.
DR   Ensembl; ENST00000316963; ENSP00000320043; ENSG00000120992. [O75608-1]
DR   Ensembl; ENST00000343231; ENSP00000344477; ENSG00000120992. [O75608-2]
DR   GeneID; 10434; -.
DR   KEGG; hsa:10434; -.
DR   UCSC; uc003xrz.5; human. [O75608-1]
DR   CTD; 10434; -.
DR   DisGeNET; 10434; -.
DR   GeneCards; LYPLA1; -.
DR   HGNC; HGNC:6737; LYPLA1.
DR   HPA; ENSG00000120992; Low tissue specificity.
DR   MIM; 605599; gene.
DR   neXtProt; NX_O75608; -.
DR   OpenTargets; ENSG00000120992; -.
DR   PharmGKB; PA30499; -.
DR   VEuPathDB; HostDB:ENSG00000120992; -.
DR   eggNOG; KOG2112; Eukaryota.
DR   GeneTree; ENSGT00940000154185; -.
DR   InParanoid; O75608; -.
DR   OMA; HGWSEAL; -.
DR   PhylomeDB; O75608; -.
DR   TreeFam; TF314619; -.
DR   BRENDA; 3.1.2.22; 2681.
DR   PathwayCommons; O75608; -.
DR   Reactome; R-HSA-203615; eNOS activation.
DR   Reactome; R-HSA-9648002; RAS processing.
DR   BioGRID-ORCS; 10434; 22 hits in 1013 CRISPR screens.
DR   ChiTaRS; LYPLA1; human.
DR   EvolutionaryTrace; O75608; -.
DR   GeneWiki; LYPLA1; -.
DR   GenomeRNAi; 10434; -.
DR   Pharos; O75608; Tchem.
DR   PRO; PR:O75608; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O75608; protein.
DR   Bgee; ENSG00000120992; Expressed in placenta and 251 other tissues.
DR   ExpressionAtlas; O75608; baseline and differential.
DR   Genevisible; O75608; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0016298; F:lipase activity; IDA:CACAO.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; IEA:Ensembl.
DR   GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW   Endoplasmic reticulum; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW   Membrane; Nucleus; Reference proteome.
FT   CHAIN           1..230
FT                   /note="Acyl-protein thioesterase 1"
FT                   /id="PRO_0000102267"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000269|PubMed:19439193"
FT   ACT_SITE        174
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:11080636"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:11080636"
FT   MOD_RES         224
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97823"
FT   VAR_SEQ         57..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11042152"
FT                   /id="VSP_009196"
FT   VARIANT         153
FT                   /note="P -> S (in dbSNP:rs11549448)"
FT                   /id="VAR_060991"
FT   MUTAGEN         119
FT                   /note="S->A: Loss of thioesterase and lysophospholipase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:19439193"
FT   CONFLICT        127..131
FT                   /note="YTALT -> SLIRG (in Ref. 5; AAB88180)"
FT                   /evidence="ECO:0000305"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          17..19
FT                   /evidence="ECO:0007829|PDB:5SYM"
FT   STRAND          21..27
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           34..42
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           86..105
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          113..118
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           120..129
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   TURN            160..163
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          166..171
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           179..192
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   STRAND          198..203
FT                   /evidence="ECO:0007829|PDB:1FJ2"
FT   HELIX           212..225
FT                   /evidence="ECO:0007829|PDB:1FJ2"
SQ   SEQUENCE   230 AA;  24670 MW;  90C0522F765F1AC6 CRC64;
     MCGNNMSTPL PAIVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIRSSHIK YICPHAPVRP
     VTLNMNVAMP SWFDIIGLSP DSQEDESGIK QAAENIKALI DQEVKNGIPS NRIILGGFSQ
     GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFPQGPIGGA NRDISILQCH GDCDPLVPLM
     FGSLTVEKLK TLVNPANVTF KTYEGMMHSS CQQEMMDVKQ FIDKLLPPID
//
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