GPAT2_RAT
ID GPAT2_RAT Reviewed; 801 AA.
AC D3ZI76;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 2, mitochondrial {ECO:0000305};
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};
GN Name=Gpat2 {ECO:0000312|RGD:1304904};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22905194; DOI=10.1371/journal.pone.0042986;
RA Cattaneo E.R., Pellon-Maison M., Rabassa M.E., Lacunza E., Coleman R.A.,
RA Gonzalez-Baro M.R.;
RT "Glycerol-3-phosphate acyltransferase-2 is expressed in spermatic germ
RT cells and incorporates arachidonic acid into triacylglycerols.";
RL PLoS ONE 7:e42986-e42986(2012).
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:0000269|PubMed:22905194}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q14DK4}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatocytes and spermatides.
CC {ECO:0000269|PubMed:22905194}.
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}.
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DR EMBL; AABR07053681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001162001.1; NM_001168529.1.
DR RefSeq; XP_006235018.1; XM_006234956.3.
DR AlphaFoldDB; D3ZI76; -.
DR STRING; 10116.ENSRNOP00000018677; -.
DR iPTMnet; D3ZI76; -.
DR PhosphoSitePlus; D3ZI76; -.
DR PaxDb; D3ZI76; -.
DR Ensembl; ENSRNOT00000018677; ENSRNOP00000018677; ENSRNOG00000013906.
DR GeneID; 296130; -.
DR KEGG; rno:296130; -.
DR CTD; 150763; -.
DR RGD; 1304904; Gpat2.
DR eggNOG; KOG3729; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR HOGENOM; CLU_016910_0_0_1; -.
DR InParanoid; D3ZI76; -.
DR OMA; QEYTTNA; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; D3ZI76; -.
DR TreeFam; TF313360; -.
DR BRENDA; 2.3.1.15; 5301.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00557; UER00612.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000013906; Expressed in testis and 6 other tissues.
DR Genevisible; D3ZI76; RN.
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; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:RGD.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..801
FT /note="Glycerol-3-phosphate acyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000450953"
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..290
FT /note="Acyltransferase"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
FT MOTIF 205..210
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q14DK4"
SQ SEQUENCE 801 AA; 88969 MW; E565ABCC40D05B62 CRC64;
METMLKSNPQ MQQRNNHSGQ ETSLWSSGFG MKMEAITPFL GKYRPFMGRC CQTCTPKSWE
SLFHRSIMDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPTSSDA SQMIMENTGV
QNILLGKVPG AAGEGQAPDL VKKEVQRILG HIQTTPRPFL LRLFSWALLW FLNRLFLNVQ
LHKGQMKMVH KAAQEGSPLV FLSTHKSLLD GFLLPFVLFS QGLGVLRVAL DSRTCSPALR
ALLRKLGGLF LPPEANLSLD SSEGILARAV VRATVEQLLT SGQPLLIFLE EAPGYPGPRL
SALGQAWLGL VVQAVQAGIV PDATLVPVAT AYDLVPDAPC NMTHDLAPLG LWTGALAIFR
RLCNCWGCNR RVCVRVHLAQ PFSLQEYTIN ARSCWGSRQT LEHLLQPIVL GECSVVPDTE
KEQEWTPPTS LLLALKEEDQ LLVRRLSRHV LSASVASSAV MSTAIMATLL LLKHQKGVVL
SQLLGEFSWL TEETLLRGFD VGFSGQLRCL AQHTLSLLRA HVVLLRVHQG DLVVVPRPGP
GLTHLARLSM ELLPTFLSEA VGACAVRGLL AGRVPPEGPW ELQGIELLSQ NELYRQILLL
LHLLPQDLLL PQPCQSSYCY CQEVLDRLIQ CGLLVAEETP GSRPACDTGR QHLSAKLLWK
PSGDFTDSES DDFEEPGGRC FRLSQQSRCP DFFLFLCRLL SPILKAFAQA ATFLHLGQLP
DSEVGYSEKL LQFLQACAQE EGIFECADPN LAISAIWTFK DLGVLQQIPS PTGPQLHLSP
TFASRDNQDK LEQFIRQFIC S
