Full text data of AGPAT6
AGPAT6
(GPAT4)
[Confidence: low (only semi-automatic identification from reviews)]
Glycerol-3-phosphate acyltransferase 4; GPAT4; 2.3.1.15 (1-acylglycerol-3-phosphate O-acyltransferase 6; 1-AGP acyltransferase 6; 1-AGPAT 6; Acyl-CoA:glycerol-3-phosphate acyltransferase 4; Lysophosphatidic acid acyltransferase zeta; LPAAT-zeta; Flags: Precursor)
Glycerol-3-phosphate acyltransferase 4; GPAT4; 2.3.1.15 (1-acylglycerol-3-phosphate O-acyltransferase 6; 1-AGP acyltransferase 6; 1-AGPAT 6; Acyl-CoA:glycerol-3-phosphate acyltransferase 4; Lysophosphatidic acid acyltransferase zeta; LPAAT-zeta; Flags: Precursor)
UniProt
Q86UL3
ID GPAT4_HUMAN Reviewed; 456 AA.
AC Q86UL3; Q86V89;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 4;
DE Short=GPAT4;
DE EC=2.3.1.15;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 6;
DE Short=1-AGP acyltransferase 6;
DE Short=1-AGPAT 6;
DE AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 4;
DE AltName: Full=Lysophosphatidic acid acyltransferase zeta;
DE Short=LPAAT-zeta;
DE Flags: Precursor;
GN Name=AGPAT6; Synonyms=GPAT4; ORFNames=UNQ551/PRO1108;
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], AND TISSUE SPECIFICITY.
RX PubMed=12938015; DOI=10.1007/s10038-003-0045-z;
RA Li D., Yu L., Wu H., Shan Y., Guo J., Dang Y., Wei Y., Zhao S.;
RT "Cloning and identification of the human LPAAT-zeta gene, a novel
RT member of the lysophosphatidic acid acyltransferase family.";
RL J. Hum. Genet. 48:438-442(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=18238778; DOI=10.1074/jbc.M708151200;
RA Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
RA Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
RA Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
RT "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
RL J. Biol. Chem. 283:10048-10057(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position
CC of glycerol-3-phosphate, an essential step in glycerolipid
CC biosynthesis. Active against both saturated and unsaturated long-
CC chain fatty acyl-CoAs.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC acyl-sn-glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (NEM).
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Relatively high level of
CC expression in skeletal muscle, heart and testis. Relatively low
CC level of expression in lung.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC and may constitute the binding site for the phosphate moiety of
CC the glycerol-3-phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family.
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; AF406612; AAP21893.1; -; mRNA.
DR EMBL; AY358670; AAQ89033.1; -; mRNA.
DR EMBL; BC051377; AAH51377.2; -; mRNA.
DR EMBL; BC061884; AAH61884.1; -; mRNA.
DR RefSeq; NP_848934.1; NM_178819.3.
DR RefSeq; XP_005273459.1; XM_005273402.1.
DR UniGene; Hs.355753; -.
DR ProteinModelPortal; Q86UL3; -.
DR IntAct; Q86UL3; 2.
DR MINT; MINT-2878746; -.
DR STRING; 9606.ENSP00000380184; -.
DR PhosphoSite; Q86UL3; -.
DR DMDM; 68052729; -.
DR PaxDb; Q86UL3; -.
DR PRIDE; Q86UL3; -.
DR Ensembl; ENST00000396987; ENSP00000380184; ENSG00000158669.
DR GeneID; 137964; -.
DR KEGG; hsa:137964; -.
DR UCSC; uc003xnz.2; human.
DR CTD; 137964; -.
DR GeneCards; GC08P041435; -.
DR HGNC; HGNC:20880; AGPAT6.
DR HPA; HPA016471; -.
DR MIM; 608143; gene.
DR neXtProt; NX_Q86UL3; -.
DR PharmGKB; PA142672637; -.
DR eggNOG; COG0204; -.
DR HOGENOM; HOG000265725; -.
DR InParanoid; Q86UL3; -.
DR KO; K13506; -.
DR OMA; ITYHDRK; -.
DR OrthoDB; EOG70GMFG; -.
DR PhylomeDB; Q86UL3; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00557; UER00612.
DR ChiTaRS; AGPAT6; human.
DR GenomeRNAi; 137964; -.
DR NextBio; 83709; -.
DR PRO; PR:Q86UL3; -.
DR ArrayExpress; Q86UL3; -.
DR Bgee; Q86UL3; -.
DR CleanEx; HS_AGPAT6; -.
DR Genevestigator; Q86UL3; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 37 Potential.
FT CHAIN 38 456 Glycerol-3-phosphate acyltransferase 4.
FT /FTId=PRO_0000024703.
FT TRANSMEM 156 176 Helical; (Potential).
FT TRANSMEM 180 200 Helical; (Potential).
FT MOTIF 248 253 HXXXXD motif.
FT CARBOHYD 247 247 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 327 327 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 362 362 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 456 AA; 52071 MW; 5B9DEB2912E989E5 CRC64;
MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKSL LKIFAWATLR
MERGAKEKNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDNTPEF ELSDIFYFCR
KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TVLWGLGVLI RYCFLLPLRI
ALAFTGISLL VVGTTVVGYL PNGRFKEFMS KHVHLMCYRI CVRALTAIIT YHDRENRPRN
GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL
VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF
WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREADEDAV QFANRVKSAI ARQGGLVDLL
WDGGLKREKV KDTFKEEQQK LYSKMIVGNH KDRSRS
//
ID GPAT4_HUMAN Reviewed; 456 AA.
AC Q86UL3; Q86V89;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 4;
DE Short=GPAT4;
DE EC=2.3.1.15;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 6;
DE Short=1-AGP acyltransferase 6;
DE Short=1-AGPAT 6;
DE AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 4;
DE AltName: Full=Lysophosphatidic acid acyltransferase zeta;
DE Short=LPAAT-zeta;
DE Flags: Precursor;
GN Name=AGPAT6; Synonyms=GPAT4; ORFNames=UNQ551/PRO1108;
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], AND TISSUE SPECIFICITY.
RX PubMed=12938015; DOI=10.1007/s10038-003-0045-z;
RA Li D., Yu L., Wu H., Shan Y., Guo J., Dang Y., Wei Y., Zhao S.;
RT "Cloning and identification of the human LPAAT-zeta gene, a novel
RT member of the lysophosphatidic acid acyltransferase family.";
RL J. Hum. Genet. 48:438-442(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=18238778; DOI=10.1074/jbc.M708151200;
RA Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
RA Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
RA Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
RT "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
RL J. Biol. Chem. 283:10048-10057(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position
CC of glycerol-3-phosphate, an essential step in glycerolipid
CC biosynthesis. Active against both saturated and unsaturated long-
CC chain fatty acyl-CoAs.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC acyl-sn-glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (NEM).
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Relatively high level of
CC expression in skeletal muscle, heart and testis. Relatively low
CC level of expression in lung.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC and may constitute the binding site for the phosphate moiety of
CC the glycerol-3-phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family.
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; AF406612; AAP21893.1; -; mRNA.
DR EMBL; AY358670; AAQ89033.1; -; mRNA.
DR EMBL; BC051377; AAH51377.2; -; mRNA.
DR EMBL; BC061884; AAH61884.1; -; mRNA.
DR RefSeq; NP_848934.1; NM_178819.3.
DR RefSeq; XP_005273459.1; XM_005273402.1.
DR UniGene; Hs.355753; -.
DR ProteinModelPortal; Q86UL3; -.
DR IntAct; Q86UL3; 2.
DR MINT; MINT-2878746; -.
DR STRING; 9606.ENSP00000380184; -.
DR PhosphoSite; Q86UL3; -.
DR DMDM; 68052729; -.
DR PaxDb; Q86UL3; -.
DR PRIDE; Q86UL3; -.
DR Ensembl; ENST00000396987; ENSP00000380184; ENSG00000158669.
DR GeneID; 137964; -.
DR KEGG; hsa:137964; -.
DR UCSC; uc003xnz.2; human.
DR CTD; 137964; -.
DR GeneCards; GC08P041435; -.
DR HGNC; HGNC:20880; AGPAT6.
DR HPA; HPA016471; -.
DR MIM; 608143; gene.
DR neXtProt; NX_Q86UL3; -.
DR PharmGKB; PA142672637; -.
DR eggNOG; COG0204; -.
DR HOGENOM; HOG000265725; -.
DR InParanoid; Q86UL3; -.
DR KO; K13506; -.
DR OMA; ITYHDRK; -.
DR OrthoDB; EOG70GMFG; -.
DR PhylomeDB; Q86UL3; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00557; UER00612.
DR ChiTaRS; AGPAT6; human.
DR GenomeRNAi; 137964; -.
DR NextBio; 83709; -.
DR PRO; PR:Q86UL3; -.
DR ArrayExpress; Q86UL3; -.
DR Bgee; Q86UL3; -.
DR CleanEx; HS_AGPAT6; -.
DR Genevestigator; Q86UL3; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 37 Potential.
FT CHAIN 38 456 Glycerol-3-phosphate acyltransferase 4.
FT /FTId=PRO_0000024703.
FT TRANSMEM 156 176 Helical; (Potential).
FT TRANSMEM 180 200 Helical; (Potential).
FT MOTIF 248 253 HXXXXD motif.
FT CARBOHYD 247 247 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 327 327 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 362 362 N-linked (GlcNAc...) (Potential).
SQ SEQUENCE 456 AA; 52071 MW; 5B9DEB2912E989E5 CRC64;
MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKSL LKIFAWATLR
MERGAKEKNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDNTPEF ELSDIFYFCR
KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TVLWGLGVLI RYCFLLPLRI
ALAFTGISLL VVGTTVVGYL PNGRFKEFMS KHVHLMCYRI CVRALTAIIT YHDRENRPRN
GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL
VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF
WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREADEDAV QFANRVKSAI ARQGGLVDLL
WDGGLKREKV KDTFKEEQQK LYSKMIVGNH KDRSRS
//
MIM
608143
*RECORD*
*FIELD* NO
608143
*FIELD* TI
*608143 1-@ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 6; AGPAT6
;;LYSOPHOSPHATIDIC ACID ACYLTRANSFERASE-ZETA;;
read moreLPAAT-ZETA
*FIELD* TX
DESCRIPTION
Lysophosphatidic acid acyltransferases (EC 2.3.1.51) catalyze the
conversion of lysophosphatidic acid (LPA) to phosphatidic acid (PA). LPA
and PA are involved in signal transduction and lipid biosynthesis.
CLONING
By searching an EST database for sequences similar to a mouse Lpaat,
followed by PCR of a testis cDNA library, Li et al. (2003) cloned
LPAAT-zeta. The deduced 456-amino acid protein has a calculated
molecular mass of 52.1 kD. LPAAT-zeta contains an N-terminal signal
peptide, an acyltransferase domain containing 2 conserved motifs, and 4
putative transmembrane regions. Within the enzymatic domain, LPAAT-zeta
shares 17 to 21% identity with the corresponding domains of other LPAAT
family members. Northern blot analysis detected transcripts of 3.0, 4.3,
and 4.6 kb in all tissues examined. Highest expression was found in
skeletal muscle, heart, and testis. A transcript of 2.7 kb was also
detected in testis.
GENE STRUCTURE
Li et al. (2003) determined that the LPAAT-zeta gene contains 13 exons
and spans about 122 kb.
MAPPING
By genomic sequence analysis, Li et al. (2003) mapped the LPAAT-zeta
gene to chromosome 8p11.21, adjacent to the ANK1 gene (612641).
*FIELD* RF
1. Li, D.; Yu, L.; Wu, H.; Shan, Y.; Guo, J.; Dang, Y.; Wei, Y.; Zhao,
S.: Cloning and identification of the human LPAAT-zeta gene, a novel
member of the lysophosphatidic acid acyltransferase family. J. Hum.
Genet. 48: 438-442, 2003.
*FIELD* CD
Patricia A. Hartz: 10/1/2003
*FIELD* ED
carol: 02/26/2009
mgross: 5/9/2008
mgross: 10/1/2003
*RECORD*
*FIELD* NO
608143
*FIELD* TI
*608143 1-@ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 6; AGPAT6
;;LYSOPHOSPHATIDIC ACID ACYLTRANSFERASE-ZETA;;
read moreLPAAT-ZETA
*FIELD* TX
DESCRIPTION
Lysophosphatidic acid acyltransferases (EC 2.3.1.51) catalyze the
conversion of lysophosphatidic acid (LPA) to phosphatidic acid (PA). LPA
and PA are involved in signal transduction and lipid biosynthesis.
CLONING
By searching an EST database for sequences similar to a mouse Lpaat,
followed by PCR of a testis cDNA library, Li et al. (2003) cloned
LPAAT-zeta. The deduced 456-amino acid protein has a calculated
molecular mass of 52.1 kD. LPAAT-zeta contains an N-terminal signal
peptide, an acyltransferase domain containing 2 conserved motifs, and 4
putative transmembrane regions. Within the enzymatic domain, LPAAT-zeta
shares 17 to 21% identity with the corresponding domains of other LPAAT
family members. Northern blot analysis detected transcripts of 3.0, 4.3,
and 4.6 kb in all tissues examined. Highest expression was found in
skeletal muscle, heart, and testis. A transcript of 2.7 kb was also
detected in testis.
GENE STRUCTURE
Li et al. (2003) determined that the LPAAT-zeta gene contains 13 exons
and spans about 122 kb.
MAPPING
By genomic sequence analysis, Li et al. (2003) mapped the LPAAT-zeta
gene to chromosome 8p11.21, adjacent to the ANK1 gene (612641).
*FIELD* RF
1. Li, D.; Yu, L.; Wu, H.; Shan, Y.; Guo, J.; Dang, Y.; Wei, Y.; Zhao,
S.: Cloning and identification of the human LPAAT-zeta gene, a novel
member of the lysophosphatidic acid acyltransferase family. J. Hum.
Genet. 48: 438-442, 2003.
*FIELD* CD
Patricia A. Hartz: 10/1/2003
*FIELD* ED
carol: 02/26/2009
mgross: 5/9/2008
mgross: 10/1/2003