Full text data of LYPLA2
LYPLA2
(APT2)
[Confidence: low (only semi-automatic identification from reviews)]
Acyl-protein thioesterase 2; APT-2; 3.1.2.- (Lysophospholipase II; LPL-II; LysoPLA II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Acyl-protein thioesterase 2; APT-2; 3.1.2.- (Lysophospholipase II; LPL-II; LysoPLA II)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O95372
ID LYPA2_HUMAN Reviewed; 231 AA.
AC O95372; Q7Z4Z2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Acyl-protein thioesterase 2;
DE Short=APT-2;
DE EC=3.1.2.-;
DE AltName: Full=Lysophospholipase II;
DE Short=LPL-II;
DE Short=LysoPLA II;
GN Name=LYPLA2; Synonyms=APT2;
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].
RC TISSUE=Testis;
RA Kuznetsov S.R., Jones T.L.Z.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yue P., Yu L., Tu Q., Ding J.B., Fu S.N., Zhao S.Y.;
RT "Cloning and expression of a novel human cDNA homology to murine
RT lysophospholipase I mRNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Placenta;
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 FUNCTION IN DEACYLATION OF GAP43.
RX PubMed=21152083; DOI=10.1371/journal.pone.0015045;
RA Tomatis V.M., Trenchi A., Gomez G.A., Daniotti J.L.;
RT "Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral
RT membrane-associated GAP-43.";
RL PLoS ONE 5:E15045-E15045(2010).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May hydrolyze fatty acids from S-acylated cysteine
CC residues in proteins such as trimeric G alpha proteins or HRAS.
CC Has lysophospholipase activity (By similarity). Deacylates GAP43.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-protein + H(2)O = palmitate +
CC protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase
CC 2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97210.1; Type=Frameshift; Positions=5, 164, 179;
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; AF098668; AAC72844.1; -; mRNA.
DR EMBL; AF090423; AAP97210.1; ALT_FRAME; mRNA.
DR EMBL; AL031295; CAB40158.1; -; Genomic_DNA.
DR EMBL; BC017034; AAH17034.1; -; mRNA.
DR EMBL; BC017193; AAH17193.1; -; mRNA.
DR RefSeq; NP_009191.1; NM_007260.2.
DR UniGene; Hs.533479; -.
DR ProteinModelPortal; O95372; -.
DR SMR; O95372; 6-231.
DR IntAct; O95372; 4.
DR STRING; 9606.ENSP00000363638; -.
DR ChEMBL; CHEMBL1932891; -.
DR PhosphoSite; O95372; -.
DR OGP; O95372; -.
DR PaxDb; O95372; -.
DR PRIDE; O95372; -.
DR DNASU; 11313; -.
DR Ensembl; ENST00000374514; ENSP00000363638; ENSG00000011009.
DR GeneID; 11313; -.
DR KEGG; hsa:11313; -.
DR UCSC; uc001bht.3; human.
DR CTD; 11313; -.
DR GeneCards; GC01P024117; -.
DR HGNC; HGNC:6738; LYPLA2.
DR neXtProt; NX_O95372; -.
DR PharmGKB; PA30500; -.
DR eggNOG; COG0400; -.
DR HOGENOM; HOG000260139; -.
DR HOVERGEN; HBG052378; -.
DR InParanoid; O95372; -.
DR KO; K06130; -.
DR OMA; LPLHRNF; -.
DR OrthoDB; EOG7M0NSQ; -.
DR PhylomeDB; O95372; -.
DR GenomeRNAi; 11313; -.
DR NextBio; 42975; -.
DR PRO; PR:O95372; -.
DR ArrayExpress; O95372; -.
DR Bgee; O95372; -.
DR CleanEx; HS_LYPLA2; -.
DR Genevestigator; O95372; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1 231 Acyl-protein thioesterase 2.
FT /FTId=PRO_0000102271.
FT ACT_SITE 122 122 Charge relay system (By similarity).
FT ACT_SITE 176 176 Charge relay system (By similarity).
FT ACT_SITE 210 210 Charge relay system (By similarity).
SQ SEQUENCE 231 AA; 24737 MW; 813C9C71757C5135 CRC64;
MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP
RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG
FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP
VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V
//
ID LYPA2_HUMAN Reviewed; 231 AA.
AC O95372; Q7Z4Z2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Acyl-protein thioesterase 2;
DE Short=APT-2;
DE EC=3.1.2.-;
DE AltName: Full=Lysophospholipase II;
DE Short=LPL-II;
DE Short=LysoPLA II;
GN Name=LYPLA2; Synonyms=APT2;
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].
RC TISSUE=Testis;
RA Kuznetsov S.R., Jones T.L.Z.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yue P., Yu L., Tu Q., Ding J.B., Fu S.N., Zhao S.Y.;
RT "Cloning and expression of a novel human cDNA homology to murine
RT lysophospholipase I mRNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Placenta;
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 FUNCTION IN DEACYLATION OF GAP43.
RX PubMed=21152083; DOI=10.1371/journal.pone.0015045;
RA Tomatis V.M., Trenchi A., Gomez G.A., Daniotti J.L.;
RT "Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral
RT membrane-associated GAP-43.";
RL PLoS ONE 5:E15045-E15045(2010).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May hydrolyze fatty acids from S-acylated cysteine
CC residues in proteins such as trimeric G alpha proteins or HRAS.
CC Has lysophospholipase activity (By similarity). Deacylates GAP43.
CC -!- CATALYTIC ACTIVITY: Palmitoyl-protein + H(2)O = palmitate +
CC protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase
CC 2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97210.1; Type=Frameshift; Positions=5, 164, 179;
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; AF098668; AAC72844.1; -; mRNA.
DR EMBL; AF090423; AAP97210.1; ALT_FRAME; mRNA.
DR EMBL; AL031295; CAB40158.1; -; Genomic_DNA.
DR EMBL; BC017034; AAH17034.1; -; mRNA.
DR EMBL; BC017193; AAH17193.1; -; mRNA.
DR RefSeq; NP_009191.1; NM_007260.2.
DR UniGene; Hs.533479; -.
DR ProteinModelPortal; O95372; -.
DR SMR; O95372; 6-231.
DR IntAct; O95372; 4.
DR STRING; 9606.ENSP00000363638; -.
DR ChEMBL; CHEMBL1932891; -.
DR PhosphoSite; O95372; -.
DR OGP; O95372; -.
DR PaxDb; O95372; -.
DR PRIDE; O95372; -.
DR DNASU; 11313; -.
DR Ensembl; ENST00000374514; ENSP00000363638; ENSG00000011009.
DR GeneID; 11313; -.
DR KEGG; hsa:11313; -.
DR UCSC; uc001bht.3; human.
DR CTD; 11313; -.
DR GeneCards; GC01P024117; -.
DR HGNC; HGNC:6738; LYPLA2.
DR neXtProt; NX_O95372; -.
DR PharmGKB; PA30500; -.
DR eggNOG; COG0400; -.
DR HOGENOM; HOG000260139; -.
DR HOVERGEN; HBG052378; -.
DR InParanoid; O95372; -.
DR KO; K06130; -.
DR OMA; LPLHRNF; -.
DR OrthoDB; EOG7M0NSQ; -.
DR PhylomeDB; O95372; -.
DR GenomeRNAi; 11313; -.
DR NextBio; 42975; -.
DR PRO; PR:O95372; -.
DR ArrayExpress; O95372; -.
DR Bgee; O95372; -.
DR CleanEx; HS_LYPLA2; -.
DR Genevestigator; O95372; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Reference proteome.
FT CHAIN 1 231 Acyl-protein thioesterase 2.
FT /FTId=PRO_0000102271.
FT ACT_SITE 122 122 Charge relay system (By similarity).
FT ACT_SITE 176 176 Charge relay system (By similarity).
FT ACT_SITE 210 210 Charge relay system (By similarity).
SQ SEQUENCE 231 AA; 24737 MW; 813C9C71757C5135 CRC64;
MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP
RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG
FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP
VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V
//