Full text data of LYPLA1
LYPLA1
(APT1, LPL1)
[Confidence: low (only semi-automatic identification from reviews)]
Acyl-protein thioesterase 1; APT-1; hAPT1; 3.1.2.- (Lysophospholipase 1; Lysophospholipase I; LPL-I; LysoPLA I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Acyl-protein thioesterase 1; APT-1; hAPT1; 3.1.2.- (Lysophospholipase 1; Lysophospholipase I; LPL-I; LysoPLA I)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75608
ID LYPA1_HUMAN Reviewed; 230 AA.
AC O75608; O43202; Q9UQF9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 121.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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, AND SUBUNIT.
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
RT single 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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
RT project: 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 ENZYME REGULATION, AND FUNCTION.
RX PubMed=20418879; DOI=10.1038/nchembio.362;
RA Dekker F.J., Rocks O., Vartak N., Menninger S., Hedberg C.,
RA Balamurugan R., Wetzel S., Renner S., Gerauer M., Scholermann B.,
RA Rusch M., Kramer J.W., Rauh D., Coates G.W., Brunsveld L.,
RA 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 [7]
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.,
RA Buerckstuemmer T., 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 [8]
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).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues
CC in proteins such as trimeric G alpha proteins or HRAS. Has
CC depalmitoylating activity toward KCNMA1. Has low lysophospholipase
CC activity.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-protein + H(2)O = palmitate +
CC protein.
CC -!- ENZYME REGULATION: Inhibited by palmostatin-B, leading to impair
CC depalmitoylating of Ras.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase
CC 2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88180.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001266285.1; NM_001279356.1.
DR RefSeq; NP_001266286.1; NM_001279357.1.
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.
DR UniGene; Hs.744046; -.
DR PDB; 1FJ2; X-ray; 1.50 A; A/B=6-230.
DR PDBsum; 1FJ2; -.
DR ProteinModelPortal; O75608; -.
DR SMR; O75608; 6-229.
DR IntAct; O75608; 2.
DR MINT; MINT-5005801; -.
DR STRING; 9606.ENSP00000320043; -.
DR BindingDB; O75608; -.
DR ChEMBL; CHEMBL1681631; -.
DR MEROPS; S09.026; -.
DR PhosphoSite; O75608; -.
DR OGP; O75608; -.
DR PaxDb; O75608; -.
DR PeptideAtlas; O75608; -.
DR PRIDE; O75608; -.
DR DNASU; 10434; -.
DR Ensembl; ENST00000316963; ENSP00000320043; ENSG00000120992.
DR Ensembl; ENST00000343231; ENSP00000344477; ENSG00000120992.
DR GeneID; 10434; -.
DR KEGG; hsa:10434; -.
DR UCSC; uc003xry.3; human.
DR CTD; 10434; -.
DR GeneCards; GC08M055008; -.
DR HGNC; HGNC:6737; LYPLA1.
DR HPA; HPA050941; -.
DR MIM; 605599; gene.
DR neXtProt; NX_O75608; -.
DR PharmGKB; PA30499; -.
DR eggNOG; COG0400; -.
DR HOGENOM; HOG000260139; -.
DR HOVERGEN; HBG052378; -.
DR InParanoid; O75608; -.
DR KO; K06128; -.
DR OMA; VEWHEYS; -.
DR OrthoDB; EOG7M0NSQ; -.
DR PhylomeDB; O75608; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; LYPLA1; human.
DR EvolutionaryTrace; O75608; -.
DR GeneWiki; LYPLA1; -.
DR GenomeRNAi; 10434; -.
DR NextBio; 39546; -.
DR PRO; PR:O75608; -.
DR ArrayExpress; O75608; -.
DR Bgee; O75608; -.
DR CleanEx; HS_LYPLA1; -.
DR Genevestigator; O75608; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004622; F:lysophospholipase activity; TAS:ProtInc.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IMP: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:0046209; P:nitric oxide metabolic process; TAS:Reactome.
DR GO; GO:0002084; P:protein depalmitoylation; IEA:Ensembl.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Polymorphism; Reference proteome.
FT CHAIN 1 230 Acyl-protein thioesterase 1.
FT /FTId=PRO_0000102267.
FT ACT_SITE 119 119 Charge relay system.
FT ACT_SITE 174 174 Charge relay system.
FT ACT_SITE 208 208 Charge relay system.
FT MOD_RES 224 224 N6-acetyllysine (By similarity).
FT VAR_SEQ 57 72 Missing (in isoform 2).
FT /FTId=VSP_009196.
FT VARIANT 153 153 P -> S (in dbSNP:rs11549448).
FT /FTId=VAR_060991.
FT CONFLICT 127 131 YTALT -> SLIRG (in Ref. 5; AAB88180).
FT STRAND 12 14
FT STRAND 21 27
FT STRAND 30 32
FT HELIX 34 42
FT STRAND 49 53
FT STRAND 58 60
FT HELIX 62 64
FT STRAND 68 70
FT HELIX 86 105
FT HELIX 110 112
FT STRAND 113 118
FT HELIX 120 129
FT STRAND 137 143
FT HELIX 149 151
FT TURN 160 163
FT STRAND 166 171
FT STRAND 175 177
FT HELIX 179 192
FT HELIX 195 197
FT STRAND 198 203
FT HELIX 212 225
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
//
ID LYPA1_HUMAN Reviewed; 230 AA.
AC O75608; O43202; Q9UQF9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 121.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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, AND SUBUNIT.
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
RT single 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
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor 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
RT project: 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 ENZYME REGULATION, AND FUNCTION.
RX PubMed=20418879; DOI=10.1038/nchembio.362;
RA Dekker F.J., Rocks O., Vartak N., Menninger S., Hedberg C.,
RA Balamurugan R., Wetzel S., Renner S., Gerauer M., Scholermann B.,
RA Rusch M., Kramer J.W., Rauh D., Coates G.W., Brunsveld L.,
RA 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 [7]
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.,
RA Buerckstuemmer T., 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 [8]
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).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues
CC in proteins such as trimeric G alpha proteins or HRAS. Has
CC depalmitoylating activity toward KCNMA1. Has low lysophospholipase
CC activity.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-protein + H(2)O = palmitate +
CC protein.
CC -!- ENZYME REGULATION: Inhibited by palmostatin-B, leading to impair
CC depalmitoylating of Ras.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase
CC 2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88180.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001266285.1; NM_001279356.1.
DR RefSeq; NP_001266286.1; NM_001279357.1.
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.
DR UniGene; Hs.744046; -.
DR PDB; 1FJ2; X-ray; 1.50 A; A/B=6-230.
DR PDBsum; 1FJ2; -.
DR ProteinModelPortal; O75608; -.
DR SMR; O75608; 6-229.
DR IntAct; O75608; 2.
DR MINT; MINT-5005801; -.
DR STRING; 9606.ENSP00000320043; -.
DR BindingDB; O75608; -.
DR ChEMBL; CHEMBL1681631; -.
DR MEROPS; S09.026; -.
DR PhosphoSite; O75608; -.
DR OGP; O75608; -.
DR PaxDb; O75608; -.
DR PeptideAtlas; O75608; -.
DR PRIDE; O75608; -.
DR DNASU; 10434; -.
DR Ensembl; ENST00000316963; ENSP00000320043; ENSG00000120992.
DR Ensembl; ENST00000343231; ENSP00000344477; ENSG00000120992.
DR GeneID; 10434; -.
DR KEGG; hsa:10434; -.
DR UCSC; uc003xry.3; human.
DR CTD; 10434; -.
DR GeneCards; GC08M055008; -.
DR HGNC; HGNC:6737; LYPLA1.
DR HPA; HPA050941; -.
DR MIM; 605599; gene.
DR neXtProt; NX_O75608; -.
DR PharmGKB; PA30499; -.
DR eggNOG; COG0400; -.
DR HOGENOM; HOG000260139; -.
DR HOVERGEN; HBG052378; -.
DR InParanoid; O75608; -.
DR KO; K06128; -.
DR OMA; VEWHEYS; -.
DR OrthoDB; EOG7M0NSQ; -.
DR PhylomeDB; O75608; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; LYPLA1; human.
DR EvolutionaryTrace; O75608; -.
DR GeneWiki; LYPLA1; -.
DR GenomeRNAi; 10434; -.
DR NextBio; 39546; -.
DR PRO; PR:O75608; -.
DR ArrayExpress; O75608; -.
DR Bgee; O75608; -.
DR CleanEx; HS_LYPLA1; -.
DR Genevestigator; O75608; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004622; F:lysophospholipase activity; TAS:ProtInc.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IMP: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:0046209; P:nitric oxide metabolic process; TAS:Reactome.
DR GO; GO:0002084; P:protein depalmitoylation; IEA:Ensembl.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Polymorphism; Reference proteome.
FT CHAIN 1 230 Acyl-protein thioesterase 1.
FT /FTId=PRO_0000102267.
FT ACT_SITE 119 119 Charge relay system.
FT ACT_SITE 174 174 Charge relay system.
FT ACT_SITE 208 208 Charge relay system.
FT MOD_RES 224 224 N6-acetyllysine (By similarity).
FT VAR_SEQ 57 72 Missing (in isoform 2).
FT /FTId=VSP_009196.
FT VARIANT 153 153 P -> S (in dbSNP:rs11549448).
FT /FTId=VAR_060991.
FT CONFLICT 127 131 YTALT -> SLIRG (in Ref. 5; AAB88180).
FT STRAND 12 14
FT STRAND 21 27
FT STRAND 30 32
FT HELIX 34 42
FT STRAND 49 53
FT STRAND 58 60
FT HELIX 62 64
FT STRAND 68 70
FT HELIX 86 105
FT HELIX 110 112
FT STRAND 113 118
FT HELIX 120 129
FT STRAND 137 143
FT HELIX 149 151
FT TURN 160 163
FT STRAND 166 171
FT STRAND 175 177
FT HELIX 179 192
FT HELIX 195 197
FT STRAND 198 203
FT HELIX 212 225
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
//
MIM
605599
*RECORD*
*FIELD* NO
605599
*FIELD* TI
*605599 LYSOPHOSPHOLIPASE I; LYPLA1
;;ACYL PROTEIN THIOESTERASE 1; APT1
*FIELD* TX
read more
CLONING
Lysophospholipids (LysoPLs) are detergent-like intermediates in
phospholipid metabolism. Increased LysoPL levels have been detected in a
variety of diseases, including atherosclerosis and hyperlipidemia. In
some cases, increased levels of LysoPLs are hypothesized to result from
a dysfunction of LysoPL-regulating enzymes, including
lysophospholipases, which act on biologic membranes to regulate the
level of LysoPLs by hydrolysis. In a database search for sequences
homologous to mouse Lypla1, Wang et al. (1999) identified human LYPLA1
sequence fragments. They used RT-PCR on normal human brain RNA to
amplify a LYPLA1 cDNA encoding a 230-amino acid, 28-kD protein that
shares 92% sequence identity with the mouse protein. The catalytic triad
of LYPLA1 (ser119, asp174, his208) is conserved between human and mouse,
leading Wang et al. (1999) to conclude that the catalytic mechanism is
also conserved between these species. Using Northern blot analysis, Wang
et al. (1999) detected expression of LYPLA1 at varying levels in diverse
tissues including heart, placenta, skeletal muscle, liver, pancreas,
kidney, brain, lung, testis, adrenal, salivary gland, trachea, and
colon. Expression was also detected in a broad range of fetal tissues.
Western blot analysis supported the broad expression of LYPLA1.
GENE FUNCTION
Wang et al. (1999) purified a recombinant LYPLA1 protein for kinetic
characterization and demonstrated that the catalytic activity of LYPLA1
exhibits saturation kinetics. LYPLA1 hydrolyzes both monomeric and
micellar substrates. LYPLA1 appears first to bind nonspecifically to the
mixed micellar surface and then specifically to substrate presented on
the surface. The activity of LYPLA1 is irreversibly inhibited by methyl
arachindonl fluorohosphonate, which the authors thought was likely due
to the covalent modification of the enzyme at the active site ser119. No
other enzymatic activities were detected. Wang et al. (1999) concluded
that LYPLA1 is a lysophospholipid-specific lysophospholipase.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LYPLA1
gene to chromosome 8 (TMAP RH80504).
*FIELD* RF
1. Wang, A.; Yang, H.-C.; Friedman, P.; Johnson, C. A.; Dennis, E.
A.: A specific human lysophospholipase: cDNA cloning, tissue distribution
and kinetic characterization. Biochim. Biophys. Acta 1437: 157-169,
1999.
*FIELD* CD
Dawn Watkins-Chow: 1/26/2001
*FIELD* ED
mgross: 05/03/2010
carol: 2/8/2001
carol: 1/29/2001
*RECORD*
*FIELD* NO
605599
*FIELD* TI
*605599 LYSOPHOSPHOLIPASE I; LYPLA1
;;ACYL PROTEIN THIOESTERASE 1; APT1
*FIELD* TX
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CLONING
Lysophospholipids (LysoPLs) are detergent-like intermediates in
phospholipid metabolism. Increased LysoPL levels have been detected in a
variety of diseases, including atherosclerosis and hyperlipidemia. In
some cases, increased levels of LysoPLs are hypothesized to result from
a dysfunction of LysoPL-regulating enzymes, including
lysophospholipases, which act on biologic membranes to regulate the
level of LysoPLs by hydrolysis. In a database search for sequences
homologous to mouse Lypla1, Wang et al. (1999) identified human LYPLA1
sequence fragments. They used RT-PCR on normal human brain RNA to
amplify a LYPLA1 cDNA encoding a 230-amino acid, 28-kD protein that
shares 92% sequence identity with the mouse protein. The catalytic triad
of LYPLA1 (ser119, asp174, his208) is conserved between human and mouse,
leading Wang et al. (1999) to conclude that the catalytic mechanism is
also conserved between these species. Using Northern blot analysis, Wang
et al. (1999) detected expression of LYPLA1 at varying levels in diverse
tissues including heart, placenta, skeletal muscle, liver, pancreas,
kidney, brain, lung, testis, adrenal, salivary gland, trachea, and
colon. Expression was also detected in a broad range of fetal tissues.
Western blot analysis supported the broad expression of LYPLA1.
GENE FUNCTION
Wang et al. (1999) purified a recombinant LYPLA1 protein for kinetic
characterization and demonstrated that the catalytic activity of LYPLA1
exhibits saturation kinetics. LYPLA1 hydrolyzes both monomeric and
micellar substrates. LYPLA1 appears first to bind nonspecifically to the
mixed micellar surface and then specifically to substrate presented on
the surface. The activity of LYPLA1 is irreversibly inhibited by methyl
arachindonl fluorohosphonate, which the authors thought was likely due
to the covalent modification of the enzyme at the active site ser119. No
other enzymatic activities were detected. Wang et al. (1999) concluded
that LYPLA1 is a lysophospholipid-specific lysophospholipase.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LYPLA1
gene to chromosome 8 (TMAP RH80504).
*FIELD* RF
1. Wang, A.; Yang, H.-C.; Friedman, P.; Johnson, C. A.; Dennis, E.
A.: A specific human lysophospholipase: cDNA cloning, tissue distribution
and kinetic characterization. Biochim. Biophys. Acta 1437: 157-169,
1999.
*FIELD* CD
Dawn Watkins-Chow: 1/26/2001
*FIELD* ED
mgross: 05/03/2010
carol: 2/8/2001
carol: 1/29/2001