Full text data of AGPAT3
AGPAT3
(LPAAT3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma; 2.3.1.51 (1-acylglycerol-3-phosphate O-acyltransferase 3; 1-AGP acyltransferase 3; 1-AGPAT 3; Lysophosphatidic acid acyltransferase gamma; LPAAT-gamma)
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma; 2.3.1.51 (1-acylglycerol-3-phosphate O-acyltransferase 3; 1-AGP acyltransferase 3; 1-AGPAT 3; Lysophosphatidic acid acyltransferase gamma; LPAAT-gamma)
UniProt
Q9NRZ7
ID PLCC_HUMAN Reviewed; 376 AA.
AC Q9NRZ7; D3DSL2; Q3ZCU2; Q6UWP6; Q6ZUC6; Q8N3Q7; Q9NRZ6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
DE EC=2.3.1.51;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3;
DE Short=1-AGP acyltransferase 3;
DE Short=1-AGPAT 3;
DE AltName: Full=Lysophosphatidic acid acyltransferase gamma;
DE Short=LPAAT-gamma;
GN Name=AGPAT3; Synonyms=LPAAT3; ORFNames=UNQ759/PRO1490;
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] (ISOFORMS 1 AND 2).
RX PubMed=11487472; DOI=10.2741/Leung;
RA Leung D.W.;
RT "The structure and functions of human lysophosphatidic acid
RT acyltransferases.";
RL Front. Biosci. 6:D944-D953(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Hase T., Shimizu N.;
RT "Isolation of a novel gene encoding 1-acylglycerol-3-phosphate O-
RT acyltransferase 3 (AGPAT3) from the human chromosome 21q22.3.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Skin, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372 (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-376.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=20537980; DOI=10.1016/j.bbrc.2010.05.149;
RA Schmidt J.A., Yvone G.M., Brown W.J.;
RT "Membrane topology of human AGPAT3 (LPAAT3).";
RL Biochem. Biophys. Res. Commun. 397:661-667(2010).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=21173190; DOI=10.1194/jlr.M007575;
RA Prasad S.S., Garg A., Agarwal A.K.;
RT "Enzymatic activities of the human AGPAT isoform 3 and isoform 5:
RT localization of AGPAT5 to mitochondria.";
RL J. Lipid Res. 52:451-462(2011).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC acid by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone. Acts on LPA containing saturated or unsaturated
CC fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or
CC C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine,
CC lysophosphatidylinositol and lysophosphatidylserine using C18:1 or
CC C20:4-CoA.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.78 uM for LPA sn-1 C18:1;
CC KM=21.53 uM for C18:1-CoA;
CC Vmax=6.35 nmol/min/mg enzyme toward LPA sn-1 C18:1;
CC Vmax=0.74 nmol/min/mg enzyme toward C18:1-CoA;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Nucleus envelope.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Gamma-1;
CC IsoId=Q9NRZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma-2;
CC IsoId=Q9NRZ7-2; Sequence=VSP_005072;
CC Name=3;
CC IsoId=Q9NRZ7-3; Sequence=VSP_013144;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in
CC testis, pancreas and kidney, followed by spleen, lung, adipose
CC tissue and liver.
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.
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DR EMBL; AF156774; AAF80336.1; -; mRNA.
DR EMBL; AF156775; AAF80337.1; -; mRNA.
DR EMBL; AB040138; BAB18943.1; -; mRNA.
DR EMBL; AY358704; AAQ89067.1; -; mRNA.
DR EMBL; AP001054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09461.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09463.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09464.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09465.1; -; Genomic_DNA.
DR EMBL; BC011971; AAH11971.1; -; mRNA.
DR EMBL; BC040603; AAH40603.1; -; mRNA.
DR EMBL; BC063552; AAH63552.1; -; mRNA.
DR EMBL; AK125804; BAC86299.1; -; mRNA.
DR EMBL; AL832919; CAD38635.2; -; mRNA.
DR RefSeq; NP_001032642.1; NM_001037553.1.
DR RefSeq; NP_064517.1; NM_020132.4.
DR RefSeq; XP_005261217.1; XM_005261160.1.
DR RefSeq; XP_005261218.1; XM_005261161.1.
DR UniGene; Hs.248785; -.
DR ProteinModelPortal; Q9NRZ7; -.
DR IntAct; Q9NRZ7; 2.
DR STRING; 9606.ENSP00000291572; -.
DR PhosphoSite; Q9NRZ7; -.
DR DMDM; 12643817; -.
DR PaxDb; Q9NRZ7; -.
DR PRIDE; Q9NRZ7; -.
DR DNASU; 56894; -.
DR Ensembl; ENST00000291572; ENSP00000291572; ENSG00000160216.
DR Ensembl; ENST00000327505; ENSP00000332989; ENSG00000160216.
DR Ensembl; ENST00000398058; ENSP00000381135; ENSG00000160216.
DR Ensembl; ENST00000398061; ENSP00000381138; ENSG00000160216.
DR Ensembl; ENST00000398063; ENSP00000381140; ENSG00000160216.
DR Ensembl; ENST00000546158; ENSP00000443510; ENSG00000160216.
DR GeneID; 56894; -.
DR KEGG; hsa:56894; -.
DR UCSC; uc002zdv.3; human.
DR CTD; 56894; -.
DR GeneCards; GC21P045285; -.
DR HGNC; HGNC:326; AGPAT3.
DR MIM; 614794; gene.
DR neXtProt; NX_Q9NRZ7; -.
DR PharmGKB; PA24623; -.
DR eggNOG; COG0204; -.
DR HOVERGEN; HBG008205; -.
DR InParanoid; Q9NRZ7; -.
DR KO; K13523; -.
DR OMA; MEVAESK; -.
DR OrthoDB; EOG7H7928; -.
DR PhylomeDB; Q9NRZ7; -.
DR BioCyc; MetaCyc:HS08470-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00557; UER00613.
DR ChiTaRS; AGPAT3; human.
DR GeneWiki; AGPAT3; -.
DR GenomeRNAi; 56894; -.
DR NextBio; 62319; -.
DR PRO; PR:Q9NRZ7; -.
DR ArrayExpress; Q9NRZ7; -.
DR Bgee; Q9NRZ7; -.
DR CleanEx; HS_AGPAT3; -.
DR Genevestigator; Q9NRZ7; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; NAS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleus; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 376 1-acyl-sn-glycerol-3-phosphate
FT acyltransferase gamma.
FT /FTId=PRO_0000208194.
FT TOPO_DOM 1 124 Cytoplasmic (Potential).
FT TRANSMEM 125 145 Helical; (Potential).
FT TOPO_DOM 146 316 Lumenal (Potential).
FT TRANSMEM 317 339 Helical; (Potential).
FT TOPO_DOM 340 376 Cytoplasmic (Potential).
FT MOTIF 96 101 HXXXXD motif.
FT VAR_SEQ 1 62 Missing (in isoform 2).
FT /FTId=VSP_005072.
FT VAR_SEQ 1 60 MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPV
FT SKQLYRRLNCRLAYSLWSQ -> MQSGGSLPFCCYLPSVSS
FT QLLLRESYCNFIKRTQCKSSKLMFSRDFLSGQKYCRCLLWA
FT LPDHPRRRGPTSANALPLSAE (in isoform 3).
FT /FTId=VSP_013144.
FT CONFLICT 74 74 T -> P (in Ref. 7; CAD38635).
FT CONFLICT 358 376 VTEIEKGSSYGNQEFKKKE -> ESLEPGRWRLQ (in
FT Ref. 3; AAQ89067).
SQ SEQUENCE 376 AA; 43381 MW; C12CDBB7CC363852 CRC64;
MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ
LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV
LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF
TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE
IEKGSSYGNQ EFKKKE
//
ID PLCC_HUMAN Reviewed; 376 AA.
AC Q9NRZ7; D3DSL2; Q3ZCU2; Q6UWP6; Q6ZUC6; Q8N3Q7; Q9NRZ6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
DE EC=2.3.1.51;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3;
DE Short=1-AGP acyltransferase 3;
DE Short=1-AGPAT 3;
DE AltName: Full=Lysophosphatidic acid acyltransferase gamma;
DE Short=LPAAT-gamma;
GN Name=AGPAT3; Synonyms=LPAAT3; ORFNames=UNQ759/PRO1490;
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] (ISOFORMS 1 AND 2).
RX PubMed=11487472; DOI=10.2741/Leung;
RA Leung D.W.;
RT "The structure and functions of human lysophosphatidic acid
RT acyltransferases.";
RL Front. Biosci. 6:D944-D953(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Hase T., Shimizu N.;
RT "Isolation of a novel gene encoding 1-acylglycerol-3-phosphate O-
RT acyltransferase 3 (AGPAT3) from the human chromosome 21q22.3.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Skin, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372 (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-376.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=20537980; DOI=10.1016/j.bbrc.2010.05.149;
RA Schmidt J.A., Yvone G.M., Brown W.J.;
RT "Membrane topology of human AGPAT3 (LPAAT3).";
RL Biochem. Biophys. Res. Commun. 397:661-667(2010).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=21173190; DOI=10.1194/jlr.M007575;
RA Prasad S.S., Garg A., Agarwal A.K.;
RT "Enzymatic activities of the human AGPAT isoform 3 and isoform 5:
RT localization of AGPAT5 to mitochondria.";
RL J. Lipid Res. 52:451-462(2011).
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC acid by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone. Acts on LPA containing saturated or unsaturated
CC fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or
CC C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine,
CC lysophosphatidylinositol and lysophosphatidylserine using C18:1 or
CC C20:4-CoA.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.78 uM for LPA sn-1 C18:1;
CC KM=21.53 uM for C18:1-CoA;
CC Vmax=6.35 nmol/min/mg enzyme toward LPA sn-1 C18:1;
CC Vmax=0.74 nmol/min/mg enzyme toward C18:1-CoA;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Nucleus envelope.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Gamma-1;
CC IsoId=Q9NRZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma-2;
CC IsoId=Q9NRZ7-2; Sequence=VSP_005072;
CC Name=3;
CC IsoId=Q9NRZ7-3; Sequence=VSP_013144;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in
CC testis, pancreas and kidney, followed by spleen, lung, adipose
CC tissue and liver.
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 -----------------------------------------------------------------------
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DR EMBL; AF156774; AAF80336.1; -; mRNA.
DR EMBL; AF156775; AAF80337.1; -; mRNA.
DR EMBL; AB040138; BAB18943.1; -; mRNA.
DR EMBL; AY358704; AAQ89067.1; -; mRNA.
DR EMBL; AP001054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09461.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09463.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09464.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09465.1; -; Genomic_DNA.
DR EMBL; BC011971; AAH11971.1; -; mRNA.
DR EMBL; BC040603; AAH40603.1; -; mRNA.
DR EMBL; BC063552; AAH63552.1; -; mRNA.
DR EMBL; AK125804; BAC86299.1; -; mRNA.
DR EMBL; AL832919; CAD38635.2; -; mRNA.
DR RefSeq; NP_001032642.1; NM_001037553.1.
DR RefSeq; NP_064517.1; NM_020132.4.
DR RefSeq; XP_005261217.1; XM_005261160.1.
DR RefSeq; XP_005261218.1; XM_005261161.1.
DR UniGene; Hs.248785; -.
DR ProteinModelPortal; Q9NRZ7; -.
DR IntAct; Q9NRZ7; 2.
DR STRING; 9606.ENSP00000291572; -.
DR PhosphoSite; Q9NRZ7; -.
DR DMDM; 12643817; -.
DR PaxDb; Q9NRZ7; -.
DR PRIDE; Q9NRZ7; -.
DR DNASU; 56894; -.
DR Ensembl; ENST00000291572; ENSP00000291572; ENSG00000160216.
DR Ensembl; ENST00000327505; ENSP00000332989; ENSG00000160216.
DR Ensembl; ENST00000398058; ENSP00000381135; ENSG00000160216.
DR Ensembl; ENST00000398061; ENSP00000381138; ENSG00000160216.
DR Ensembl; ENST00000398063; ENSP00000381140; ENSG00000160216.
DR Ensembl; ENST00000546158; ENSP00000443510; ENSG00000160216.
DR GeneID; 56894; -.
DR KEGG; hsa:56894; -.
DR UCSC; uc002zdv.3; human.
DR CTD; 56894; -.
DR GeneCards; GC21P045285; -.
DR HGNC; HGNC:326; AGPAT3.
DR MIM; 614794; gene.
DR neXtProt; NX_Q9NRZ7; -.
DR PharmGKB; PA24623; -.
DR eggNOG; COG0204; -.
DR HOVERGEN; HBG008205; -.
DR InParanoid; Q9NRZ7; -.
DR KO; K13523; -.
DR OMA; MEVAESK; -.
DR OrthoDB; EOG7H7928; -.
DR PhylomeDB; Q9NRZ7; -.
DR BioCyc; MetaCyc:HS08470-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00557; UER00613.
DR ChiTaRS; AGPAT3; human.
DR GeneWiki; AGPAT3; -.
DR GenomeRNAi; 56894; -.
DR NextBio; 62319; -.
DR PRO; PR:Q9NRZ7; -.
DR ArrayExpress; Q9NRZ7; -.
DR Bgee; Q9NRZ7; -.
DR CleanEx; HS_AGPAT3; -.
DR Genevestigator; Q9NRZ7; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; NAS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Complete proteome;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleus; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 376 1-acyl-sn-glycerol-3-phosphate
FT acyltransferase gamma.
FT /FTId=PRO_0000208194.
FT TOPO_DOM 1 124 Cytoplasmic (Potential).
FT TRANSMEM 125 145 Helical; (Potential).
FT TOPO_DOM 146 316 Lumenal (Potential).
FT TRANSMEM 317 339 Helical; (Potential).
FT TOPO_DOM 340 376 Cytoplasmic (Potential).
FT MOTIF 96 101 HXXXXD motif.
FT VAR_SEQ 1 62 Missing (in isoform 2).
FT /FTId=VSP_005072.
FT VAR_SEQ 1 60 MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPV
FT SKQLYRRLNCRLAYSLWSQ -> MQSGGSLPFCCYLPSVSS
FT QLLLRESYCNFIKRTQCKSSKLMFSRDFLSGQKYCRCLLWA
FT LPDHPRRRGPTSANALPLSAE (in isoform 3).
FT /FTId=VSP_013144.
FT CONFLICT 74 74 T -> P (in Ref. 7; CAD38635).
FT CONFLICT 358 376 VTEIEKGSSYGNQEFKKKE -> ESLEPGRWRLQ (in
FT Ref. 3; AAQ89067).
SQ SEQUENCE 376 AA; 43381 MW; C12CDBB7CC363852 CRC64;
MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ
LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV
LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF
TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE
IEKGSSYGNQ EFKKKE
//
MIM
614794
*RECORD*
*FIELD* NO
614794
*FIELD* TI
*614794 1-@ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3; AGPAT3
;;1-@ACYL-sn-GLYCEROL 3-PHOSPHATE ACYLTRANSFERASE 3;;
read moreLYSOPHOSPHATIDIC ACID ACYLTRANSFERASE, GAMMA;;
LPAAT-GAMMA;;
LPAAT3
*FIELD* TX
DESCRIPTION
AGPAT3 is a member of a family of 1-acyl-sn-glycerol 3-phosphate
acyltransferases (EC 2.3.1.51), also known as lysophosphatidic acid
acyltransferases, that catalyze the acylation of lysophosphatidic acid
to phosphatidic acid, the precursor of all glycerolipids (summary by Lu
et al., 2005).
CLONING
Lu et al. (2005) cloned mouse Agpat3. The deduced 376-amino acid protein
has a putative N-terminal signal sequence and 3 transmembrane domains.
It contains catalytic and substrate-binding motifs and a third motif
conserved among AGPAT family members. RT-PCR analysis revealed variable
but ubiquitous Agpat3 expression in mouse tissues.
Schmidt et al. (2010) found that AGPAT3 contains 4 conserved motifs (I
through IV) thought to be important for enzymatic activity, and a
C-terminal trilysine (KKK) motif predicted to serve as an endoplasmic
reticulum (ER) retention signal. They stated that AGPAT3 localized to
both the ER and Golgi complex. Schmidt et al. (2010) also predicted that
AGPAT3 contains only 2 transmembrane domains, 1 of which separates
motifs I and II. Protease protection assays revealed that motif I was
located in the cytoplasm and motif II localized to the ER and Golgi
lumen.
Using real-time PCR, Prasad et al. (2011) found that AGPAT3 was variably
expressed in all human tissues examined, with highest expression in
lung, spleen, and leukocytes. Fluorescence-tagged AGPAT3 localized to
the ER and the nuclear envelope in transfected Chinese hamster ovary
cells. Database analysis revealed orthologs of AGPAT3 in vertebrates,
insects, and plants.
GENE FUNCTION
Using RT-PCR, Lu et al. (2005) found that Ppar-alpha (170998) activation
in mouse heart elevated Agpat3 expression.
Schmidt et al. (2010) stated that they had determined that AGPAT3 is
involved in regulating the structure and function of the Golgi complex
and that AGPAT3 negatively regulates formation of Golgi membrane
tubules. Mutagenesis experiments revealed that the C-terminal KKK motif
of AGPAT3 was not required for localization to the ER and Golgi.
Using a panel of lysophosphatidic acid (LPA) acceptor molecules and
acyl-CoA donors, Prasad et al. (2011) found that AGPAT3 had a broad
preference for LPA containing saturated or unsaturated long-chain fatty
acids as acceptors, and preferentially utilized long-chain acyl-CoAs as
acyl donors. This activity was similar to that of AGPAT5 (614796), but
the 2 enzymes showed distinct acceptor and donor preferences. AGPAT3
also showed appreciable enzyme activity with lysophosphatidylcholine,
lysophosphatidylinositol, and lysophosphatidylserine as acyl acceptor
molecules when C18:1-CoA was the acyl donor.
GENE STRUCTURE
Prasad et al. (2011) determined that the AGPAT3 gene contains 9 exons.
The first exon is untranslated.
MAPPING
Prasad et al. (2011) stated that the AGPAT3 gene maps to chromosome 21.
Hartz (2012) mapped the AGPAT3 gene to chromosome 21q22.3 based on an
alignment of the AGPAT3 sequence (GenBank GENBANK AF156774) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/30/2012.
2. Lu, B.; Jiang, Y. J.; Zhou, Y.; Xu, F. Y.; Hatch, G. M.; Choy,
P. C.: Cloning and characterization of murine 1-acyl-sn-glycerol
3-phosphate acyltransferases and their regulation by PPAR-alpha in
murine heart. Biochem. J. 385: 469-477, 2005.
3. Prasad, S. S.; Garg, A.; Agarwal, A. K.: Enzymatic activities
of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5
to mitochondria. J. Lipid Res. 52: 451-462, 2011.
4. Schmidt, J. A.; Yvone, G. M.; Brown, W. J.: Membrane topology
of human AGPAT3 (LPAAT3). Biochem. Biophys. Res. Commun. 397: 661-667,
2010.
*FIELD* CD
Particia A. Hartz: 8/31/2012
*FIELD* ED
alopez: 08/31/2012
alopez: 8/31/2012
*RECORD*
*FIELD* NO
614794
*FIELD* TI
*614794 1-@ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3; AGPAT3
;;1-@ACYL-sn-GLYCEROL 3-PHOSPHATE ACYLTRANSFERASE 3;;
read moreLYSOPHOSPHATIDIC ACID ACYLTRANSFERASE, GAMMA;;
LPAAT-GAMMA;;
LPAAT3
*FIELD* TX
DESCRIPTION
AGPAT3 is a member of a family of 1-acyl-sn-glycerol 3-phosphate
acyltransferases (EC 2.3.1.51), also known as lysophosphatidic acid
acyltransferases, that catalyze the acylation of lysophosphatidic acid
to phosphatidic acid, the precursor of all glycerolipids (summary by Lu
et al., 2005).
CLONING
Lu et al. (2005) cloned mouse Agpat3. The deduced 376-amino acid protein
has a putative N-terminal signal sequence and 3 transmembrane domains.
It contains catalytic and substrate-binding motifs and a third motif
conserved among AGPAT family members. RT-PCR analysis revealed variable
but ubiquitous Agpat3 expression in mouse tissues.
Schmidt et al. (2010) found that AGPAT3 contains 4 conserved motifs (I
through IV) thought to be important for enzymatic activity, and a
C-terminal trilysine (KKK) motif predicted to serve as an endoplasmic
reticulum (ER) retention signal. They stated that AGPAT3 localized to
both the ER and Golgi complex. Schmidt et al. (2010) also predicted that
AGPAT3 contains only 2 transmembrane domains, 1 of which separates
motifs I and II. Protease protection assays revealed that motif I was
located in the cytoplasm and motif II localized to the ER and Golgi
lumen.
Using real-time PCR, Prasad et al. (2011) found that AGPAT3 was variably
expressed in all human tissues examined, with highest expression in
lung, spleen, and leukocytes. Fluorescence-tagged AGPAT3 localized to
the ER and the nuclear envelope in transfected Chinese hamster ovary
cells. Database analysis revealed orthologs of AGPAT3 in vertebrates,
insects, and plants.
GENE FUNCTION
Using RT-PCR, Lu et al. (2005) found that Ppar-alpha (170998) activation
in mouse heart elevated Agpat3 expression.
Schmidt et al. (2010) stated that they had determined that AGPAT3 is
involved in regulating the structure and function of the Golgi complex
and that AGPAT3 negatively regulates formation of Golgi membrane
tubules. Mutagenesis experiments revealed that the C-terminal KKK motif
of AGPAT3 was not required for localization to the ER and Golgi.
Using a panel of lysophosphatidic acid (LPA) acceptor molecules and
acyl-CoA donors, Prasad et al. (2011) found that AGPAT3 had a broad
preference for LPA containing saturated or unsaturated long-chain fatty
acids as acceptors, and preferentially utilized long-chain acyl-CoAs as
acyl donors. This activity was similar to that of AGPAT5 (614796), but
the 2 enzymes showed distinct acceptor and donor preferences. AGPAT3
also showed appreciable enzyme activity with lysophosphatidylcholine,
lysophosphatidylinositol, and lysophosphatidylserine as acyl acceptor
molecules when C18:1-CoA was the acyl donor.
GENE STRUCTURE
Prasad et al. (2011) determined that the AGPAT3 gene contains 9 exons.
The first exon is untranslated.
MAPPING
Prasad et al. (2011) stated that the AGPAT3 gene maps to chromosome 21.
Hartz (2012) mapped the AGPAT3 gene to chromosome 21q22.3 based on an
alignment of the AGPAT3 sequence (GenBank GENBANK AF156774) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/30/2012.
2. Lu, B.; Jiang, Y. J.; Zhou, Y.; Xu, F. Y.; Hatch, G. M.; Choy,
P. C.: Cloning and characterization of murine 1-acyl-sn-glycerol
3-phosphate acyltransferases and their regulation by PPAR-alpha in
murine heart. Biochem. J. 385: 469-477, 2005.
3. Prasad, S. S.; Garg, A.; Agarwal, A. K.: Enzymatic activities
of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5
to mitochondria. J. Lipid Res. 52: 451-462, 2011.
4. Schmidt, J. A.; Yvone, G. M.; Brown, W. J.: Membrane topology
of human AGPAT3 (LPAAT3). Biochem. Biophys. Res. Commun. 397: 661-667,
2010.
*FIELD* CD
Particia A. Hartz: 8/31/2012
*FIELD* ED
alopez: 08/31/2012
alopez: 8/31/2012