GPAT2_HUMAN
ID GPAT2_HUMAN Reviewed; 795 AA.
AC Q6NUI2; Q6P2E4; Q6ZNI3; Q6ZNI5; Q6ZWJ4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 2, mitochondrial {ECO:0000305};
DE Short=GPAT-2;
DE EC=2.3.1.15 {ECO:0000250|UniProtKB:Q14DK4};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase GPAT2 {ECO:0000250|UniProtKB:Q14DK4};
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q14DK4};
DE AltName: Full=xGPAT1 {ECO:0000250|UniProtKB:Q14DK4};
GN Name=GPAT2 {ECO:0000312|HGNC:HGNC:27168};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 165-795 (ISOFORM 3).
RC TISSUE=Brain, Heart, and Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transfers an acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate producing a lysophosphatidic acid (LPA), an
CC essential step for the triacylglycerol (TAG) and glycerophospholipids.
CC In vitro also transfers an acyl-group from acyl-ACP to the LPA
CC producing a phosphatidic acid (PA). Prefers arachidonoyl-CoA as the
CC acyl donor. Required for primary processing step during piRNA
CC biosynthesis. Molecular mechanisms by which it promotes piRNA
CC biosynthesis are unclear and do not involve its acyltransferase
CC activity. {ECO:0000250|UniProtKB:Q14DK4}.
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:0000250|UniProtKB:Q14DK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + sn-glycerol 3-phosphate
CC = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37463, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74938;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37464;
CC Evidence={ECO:0000250|UniProtKB:Q14DK4};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (NEM).
CC {ECO:0000250|UniProtKB:Q14DK4}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000250|UniProtKB:Q14DK4}.
CC -!- SUBUNIT: Interacts with PIWIL2. {ECO:0000250|UniProtKB:Q14DK4}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q14DK4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q14DK4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6NUI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NUI2-3; Sequence=VSP_032453, VSP_032454;
CC Name=3;
CC IsoId=Q6NUI2-4; Sequence=VSP_032452;
CC Name=4;
CC IsoId=Q6NUI2-5; Sequence=VSP_032450, VSP_032451;
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}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68596.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD18392.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122734; BAC85508.1; -; mRNA.
DR EMBL; AK131194; BAD18390.1; -; mRNA.
DR EMBL; AK131197; BAD18392.1; ALT_INIT; mRNA.
DR EMBL; BC068596; AAH68596.1; ALT_INIT; mRNA.
DR CCDS; CCDS42714.1; -. [Q6NUI2-1]
DR RefSeq; NP_001308454.1; NM_001321525.1. [Q6NUI2-4]
DR RefSeq; NP_001308455.1; NM_001321526.1. [Q6NUI2-4]
DR RefSeq; NP_001308456.1; NM_001321527.1. [Q6NUI2-4]
DR RefSeq; NP_001308459.1; NM_001321530.1.
DR RefSeq; NP_001308460.1; NM_001321531.1. [Q6NUI2-3]
DR RefSeq; NP_997211.2; NM_207328.3. [Q6NUI2-1]
DR RefSeq; XP_005263945.1; XM_005263888.3. [Q6NUI2-3]
DR RefSeq; XP_016858913.1; XM_017003424.1. [Q6NUI2-4]
DR AlphaFoldDB; Q6NUI2; -.
DR BioGRID; 127324; 73.
DR STRING; 9606.ENSP00000389395; -.
DR iPTMnet; Q6NUI2; -.
DR PhosphoSitePlus; Q6NUI2; -.
DR BioMuta; GPAT2; -.
DR DMDM; 172046129; -.
DR EPD; Q6NUI2; -.
DR jPOST; Q6NUI2; -.
DR MassIVE; Q6NUI2; -.
DR PaxDb; Q6NUI2; -.
DR PeptideAtlas; Q6NUI2; -.
DR PRIDE; Q6NUI2; -.
DR ProteomicsDB; 66676; -. [Q6NUI2-1]
DR ProteomicsDB; 66677; -. [Q6NUI2-3]
DR ProteomicsDB; 66678; -. [Q6NUI2-4]
DR ProteomicsDB; 66679; -. [Q6NUI2-5]
DR Antibodypedia; 32374; 51 antibodies from 11 providers.
DR DNASU; 150763; -.
DR Ensembl; ENST00000359548.8; ENSP00000352547.4; ENSG00000186281.13. [Q6NUI2-1]
DR Ensembl; ENST00000434632.6; ENSP00000389395.2; ENSG00000186281.13. [Q6NUI2-4]
DR Ensembl; ENST00000687910.1; ENSP00000509192.1; ENSG00000186281.13. [Q6NUI2-3]
DR Ensembl; ENST00000691940.1; ENSP00000509624.1; ENSG00000186281.13. [Q6NUI2-1]
DR GeneID; 150763; -.
DR KEGG; hsa:150763; -.
DR MANE-Select; ENST00000434632.6; ENSP00000389395.2; NM_001321527.2; NP_001308456.1. [Q6NUI2-4]
DR UCSC; uc002svf.4; human. [Q6NUI2-1]
DR CTD; 150763; -.
DR DisGeNET; 150763; -.
DR GeneCards; GPAT2; -.
DR HGNC; HGNC:27168; GPAT2.
DR HPA; ENSG00000186281; Low tissue specificity.
DR MIM; 616431; gene.
DR neXtProt; NX_Q6NUI2; -.
DR OpenTargets; ENSG00000186281; -.
DR PharmGKB; PA165696677; -.
DR VEuPathDB; HostDB:ENSG00000186281; -.
DR eggNOG; KOG3729; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; Q6NUI2; -.
DR OMA; QEYTTNA; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; Q6NUI2; -.
DR TreeFam; TF313360; -.
DR BRENDA; 2.3.1.15; 2681.
DR PathwayCommons; Q6NUI2; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 150763; 84 hits in 1061 CRISPR screens.
DR GenomeRNAi; 150763; -.
DR Pharos; Q6NUI2; Tbio.
DR PRO; PR:Q6NUI2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6NUI2; protein.
DR Bgee; ENSG00000186281; Expressed in apex of heart and 97 other tissues.
DR ExpressionAtlas; Q6NUI2; baseline and differential.
DR Genevisible; Q6NUI2; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; EXP:Reactome.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:1990511; P:piRNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR SMART; SM00563; PlsC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..795
FT /note="Glycerol-3-phosphate acyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000325853"
FT TOPO_DOM 1..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..449
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..331
FT /note="Acyltransferase"
FT MOTIF 205..210
FT /note="HXXXXD motif"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
FT MOD_RES 660
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032450"
FT VAR_SEQ 274..344
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032451"
FT VAR_SEQ 476
FT /note="K -> KGVFLSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032452"
FT VAR_SEQ 633..671
FT /note="TPGSRPACDTGRQRLSRKLLWKPSGDFTDSDSDDFGEAD -> SWATQSSCS
FT SSCRPPPRKKGSSSVRTQSSPSVLSGPSET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032453"
FT VAR_SEQ 672..795
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032454"
FT CONFLICT 336
FT /note="P -> Q (in Ref. 2; AAH68596)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="F -> L (in Ref. 1; BAC85508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 87835 MW; EE8E387A87A9EE21 CRC64;
MATMLEGRCQ TQPRSSPSGR EASLWSSGFG MKLEAVTPFL GKYRPFVGRC CQTCTPKSWE
SLFHRSITDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPPCQDV PQKIMESTGV
QNLLSGRVPG GTGEGQVPDL VKKEVQRILG HIQAPPRPFL VRLFSWALLR FLNCLFLNVQ
LHKGQMKMVQ KAAQAGLPLV LLSTHKTLLD GILLPFMLLS QGLGVLRVAW DSRACSPALR
ALLRKLGGLF LPPEASLSLD SSEGLLARAV VQAVIEQLLV SGQPLLIFLE EPPGALGPRL
SALGQAWVGF VVQAVQVGIV PDALLVPVAV TYDLVPDAPC DIDHASAPLG LWTGALAVLR
SLWSRWGCSH RICSRVHLAQ PFSLQEYIVS ARSCWGGRQT LEQLLQPIVL GQCTAVPDTE
KEQEWTPITG PLLALKEEDQ LLVRRLSCHV LSASVGSSAV MSTAIMATLL LFKHQKLLGE
FSWLTEEILL RGFDVGFSGQ LRSLLQHSLS LLRAHVALLR IRQGDLLVVP QPGPGLTHLA
QLSAELLPVF LSEAVGACAV RGLLAGRVPP QGPWELQGIL LLSQNELYRQ ILLLMHLLPQ
DLLLLKPCQS SYCYCQEVLD RLIQCGLLVA EETPGSRPAC DTGRQRLSRK LLWKPSGDFT
DSDSDDFGEA DGRYFRLSQQ SHCPDFFLFL CRLLSPLLKA FAQAAAFLRQ GQLPDTELGY
TEQLFQFLQA TAQEEGIFEC ADPKLAISAV WTFRDLGVLQ QTPSPAGPRL HLSPTFASLD
NQEKLEQFIR QFICS
