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   24-JAN-2024, entry version 142.
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   CCDS; CCDS92810.1; -. [Q6NUI2-3]
DR   CCDS; CCDS92811.1; -. [Q6NUI2-4]
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.
DR   RefSeq; XP_016858913.1; XM_017003424.1. [Q6NUI2-4]
DR   AlphaFoldDB; Q6NUI2; -.
DR   SMR; 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; 9606-ENSP00000389395; -.
DR   PeptideAtlas; Q6NUI2; -.
DR   ProteomicsDB; 66676; -. [Q6NUI2-1]
DR   ProteomicsDB; 66677; -. [Q6NUI2-3]
DR   ProteomicsDB; 66678; -. [Q6NUI2-4]
DR   ProteomicsDB; 66679; -. [Q6NUI2-5]
DR   Antibodypedia; 32374; 58 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   AGR; HGNC:27168; -.
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; 2874405at2759; -.
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; 85 hits in 1136 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 99 other cell types or tissues.
DR   ExpressionAtlas; Q6NUI2; baseline and differential.
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:0034587; P:piRNA processing; 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; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563:SF15; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   Genevisible; Q6NUI2; HS.
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
//