GPAT4_MOUSE
ID GPAT4_MOUSE Reviewed; 456 AA.
AC Q8K2C8; Q3TF78; Q5QHR4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 4 {ECO:0000312|MGI:MGI:2142716};
DE Short=GPAT4;
DE EC=2.3.1.15 {ECO:0000269|PubMed:18238778};
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 AltName: Full=Testis spermatogenesis apoptosis-related protein 7 {ECO:0000303|PubMed:15944755};
DE Flags: Precursor;
GN Name=Gpat4 {ECO:0000312|MGI:MGI:2142716};
GN Synonyms=Agpat6, Tsarg7 {ECO:0000303|PubMed:15944755};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II;
RA Guo J.H., Dai F.Y., Yu L.;
RT "A novel gene encodes a product of putative lysophosphatidic acid
RT acyltransferase.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-402, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=15944755; DOI=10.1111/j.1745-7270.2005.00057.x;
RA Tan X.J., Xing X.W., Li L.Y., Wu Z.D., Zhong C.G., Nie D.S., Fu J.J.,
RA Xiang Y., Deng Y., Lu G.X.;
RT "Molecular cloning of a novel mouse testis-specific spermatogenic cell
RT apoptosis inhibitor gene mTSARG7 as a candidate oncogene.";
RL Acta Biochim. Biophys. Sin. 37:396-405(2005).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-
CC phosphate (lysophosphatidic acid or LPA) by incorporating an acyl
CC moiety at the sn-1 position of the glycerol backbone (PubMed:18238778).
CC Active against both saturated and unsaturated long-chain fatty acyl-
CC CoAs (By similarity). Protects cells against lipotoxicity (By
CC similarity). {ECO:0000250|UniProtKB:Q86UL3,
CC ECO:0000269|PubMed:18238778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:18238778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:18238778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74565; Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000250|UniProtKB:Q86UL3};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q86UL3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:15944755}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY489184; AAS75838.1; -; mRNA.
DR EMBL; AF406611; AAP97283.1; -; mRNA.
DR EMBL; AK045235; BAC32273.1; -; mRNA.
DR EMBL; AK077561; BAC36864.1; -; mRNA.
DR EMBL; AK083589; BAC38962.1; -; mRNA.
DR EMBL; AK161270; BAE36282.1; -; mRNA.
DR EMBL; AK169257; BAE41020.1; -; mRNA.
DR EMBL; BC031767; AAH31767.1; -; mRNA.
DR CCDS; CCDS22189.1; -.
DR RefSeq; NP_061213.2; NM_018743.4.
DR AlphaFoldDB; Q8K2C8; -.
DR BioGRID; 221833; 1.
DR STRING; 10090.ENSMUSP00000127325; -.
DR SwissLipids; SLP:000000104; -.
DR GlyGen; Q8K2C8; 4 sites.
DR iPTMnet; Q8K2C8; -.
DR PhosphoSitePlus; Q8K2C8; -.
DR SwissPalm; Q8K2C8; -.
DR EPD; Q8K2C8; -.
DR jPOST; Q8K2C8; -.
DR MaxQB; Q8K2C8; -.
DR PaxDb; Q8K2C8; -.
DR PRIDE; Q8K2C8; -.
DR ProteomicsDB; 271261; -.
DR Antibodypedia; 3092; 282 antibodies from 22 providers.
DR DNASU; 102247; -.
DR Ensembl; ENSMUST00000167004; ENSMUSP00000127325; ENSMUSG00000031545.
DR GeneID; 102247; -.
DR KEGG; mmu:102247; -.
DR UCSC; uc009leo.2; mouse.
DR CTD; 137964; -.
DR MGI; MGI:2142716; Gpat4.
DR VEuPathDB; HostDB:ENSMUSG00000031545; -.
DR eggNOG; KOG2898; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; Q8K2C8; -.
DR OMA; CVMFKKG; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; Q8K2C8; -.
DR TreeFam; TF315039; -.
DR BRENDA; 2.3.1.15; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 102247; 3 hits in 43 CRISPR screens.
DR ChiTaRS; Gpat4; mouse.
DR PRO; PR:Q8K2C8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K2C8; protein.
DR Bgee; ENSMUSG00000031545; Expressed in seminiferous tubule of testis and 242 other tissues.
DR ExpressionAtlas; Q8K2C8; baseline and differential.
DR Genevisible; Q8K2C8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR GO; GO:0002071; P:glandular epithelial cell maturation; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; 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
FT /evidence="ECO:0000255"
FT CHAIN 38..456
FT /note="Glycerol-3-phosphate acyltransferase 4"
FT /id="PRO_0000024704"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 248..253
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 119
FT /note="C -> G (in Ref. 4; AAS75838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 52181 MW; 2C3E1C37044C14FA CRC64;
MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKTL LKIFAWATLR
MERGAKERNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDKTPEF ELSDIFYFCR
KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TILWGLGVLI RYCFLLPLRI
ALAFTGIGLL VVGTTMVGYL PNGRFKEFLS KHVHLMCYRI CVRALTAIIT YHNRKNRPRN
GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL
VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF
WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREKDEDAV QFANRVKSAI ARQGGLVDLL
WDGGLKREKV KDTFKEEQQK LYSKMIVGNH EDRSRS
