GPAT2_MOUSE
ID GPAT2_MOUSE Reviewed; 801 AA.
AC Q14DK4; B1AW16; Q0KK60; Q14CH8; Q6KAQ3; Q8BRZ9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 2, mitochondrial {ECO:0000305};
DE Short=GPAT-2;
DE EC=2.3.1.15 {ECO:0000269|PubMed:22905194, ECO:0000305|PubMed:17013544, ECO:0000305|PubMed:17689486};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase GPAT2 {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000269|PubMed:22905194};
DE AltName: Full=xGPAT1 {ECO:0000303|PubMed:17013544};
GN Name=Gpat2 {ECO:0000312|MGI:MGI:2684962};
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 [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, FUNCTION,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=17689486; DOI=10.1016/j.abb.2007.06.033;
RA Wang S., Lee D.P., Gong N., Schwerbrock N.M.J., Mashek D.G.,
RA Gonzalez-Baro M.R., Stapleton C., Li L.O., Lewin T.M., Coleman R.A.;
RT "Cloning and functional characterization of a novel mitochondrial N-
RT ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2).";
RL Arch. Biochem. Biophys. 465:347-358(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=17013544; DOI=10.1007/s11010-006-9321-5;
RA Harada N., Hara S., Yoshida M., Zenitani T., Mawatari K., Nakano M.,
RA Takahashi A., Hosaka T., Yoshimoto K., Nakaya Y.;
RT "Molecular cloning of a murine glycerol-3-phosphate acyltransferase-like
RT protein 1 (xGPAT1).";
RL Mol. Cell. Biochem. 297:41-51(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-801.
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; THR-666; SER-668 AND
RP SER-670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
RN [8]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=22285183; DOI=10.1016/j.bbrc.2012.01.055;
RA Nakagawa T., Harada N., Miyamoto A., Kawanishi Y., Yoshida M., Shono M.,
RA Mawatari K., Takahashi A., Sakaue H., Nakaya Y.;
RT "Membrane topology of murine glycerol-3-phosphate acyltransferase 2.";
RL Biochem. Biophys. Res. Commun. 418:506-511(2012).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND PATHWAY.
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).
RN [10]
RP FUNCTION, INTERACTION WITH PIWIL2, AND MUTAGENESIS OF HIS-205 AND ASP-210.
RX PubMed=23611983; DOI=10.1261/rna.038521.113;
RA Shiromoto Y., Kuramochi-Miyagawa S., Daiba A., Chuma S., Katanaya A.,
RA Katsumata A., Nishimura K., Ohtaka M., Nakanishi M., Nakamura T.,
RA Yoshinaga K., Asada N., Nakamura S., Yasunaga T., Kojima-Kita K., Itou D.,
RA Kimura T., Nakano T.;
RT "GPAT2, a mitochondrial outer membrane protein, in piRNA biogenesis in
RT germline stem cells.";
RL RNA 19:803-810(2013).
RN [11]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=26268560; DOI=10.1042/bj20150730;
RA Garcia-Fabiani M.B., Montanaro M.A., Lacunza E., Cattaneo E.R.,
RA Coleman R.A., Pellon-Maison M., Gonzalez-Baro M.R.;
RT "Methylation of the Gpat2 promoter regulates transient expression during
RT mouse spermatogenesis.";
RL Biochem. J. 471:211-220(2015).
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 (PubMed:17013544, PubMed:17689486, PubMed:22905194). In vitro also
CC transfers an acyl-group from acyl-ACP to the LPA producing a
CC phosphatidic acid (PA) (PubMed:22905194). Prefers arachidonoyl-CoA as
CC the acyl donor (PubMed:22905194). Required for primary processing step
CC during piRNA biosynthesis (PubMed:23611983). Molecular mechanisms by
CC which it promotes piRNA biosynthesis are unclear and do not involve its
CC acyltransferase activity (PubMed:23611983).
CC {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486,
CC ECO:0000269|PubMed:22905194, ECO:0000269|PubMed:23611983}.
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:22905194, ECO:0000305|PubMed:17013544,
CC ECO:0000305|PubMed:17689486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000269|PubMed:22905194};
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:0000269|PubMed:22905194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:22905194};
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:0000269|PubMed:22905194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:22905194};
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:0000269|PubMed:22905194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000305|PubMed:22905194};
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:0000269|PubMed:22905194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37464;
CC Evidence={ECO:0000269|PubMed:22905194};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (NEM).
CC {ECO:0000269|PubMed:17689486}.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC {ECO:0000269|PubMed:22905194}.
CC -!- SUBUNIT: Interacts with PIWIL2 (PubMed:23611983).
CC {ECO:0000269|PubMed:23611983}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486,
CC ECO:0000269|PubMed:22285183}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486,
CC ECO:0000269|PubMed:22285183}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14DK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14DK4-2; Sequence=VSP_032457, VSP_032458;
CC Name=3;
CC IsoId=Q14DK4-3; Sequence=VSP_032457;
CC -!- TISSUE SPECIFICITY: Highly expressed in the testis (PubMed:26268560).
CC Expressed at lower levels in the heart, liver, kidney, spleen and
CC adipose cells (PubMed:17013544, PubMed:17689486). Only detected in
CC primary spermatocytes (PubMed:22905194). {ECO:0000269|PubMed:17013544,
CC ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:22905194,
CC ECO:0000269|PubMed:26268560}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in pachytene spermatocytes (at
CC protein level) (PubMed:26268560). {ECO:0000269|PubMed:26268560}.
CC -!- INDUCTION: Up-regulated by retinoic acid (PubMed:26268560).
CC {ECO:0000269|PubMed:26268560}.
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=AAI13777.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD21404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB257502; BAF03614.1; -; mRNA.
DR EMBL; AK131154; BAD21404.1; ALT_INIT; mRNA.
DR EMBL; AL731831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113776; AAI13777.1; ALT_INIT; mRNA.
DR EMBL; BC113165; AAI13166.1; -; mRNA.
DR EMBL; AK040991; BAC30772.1; -; mRNA.
DR CCDS; CCDS38232.2; -. [Q14DK4-1]
DR RefSeq; NP_001074558.2; NM_001081089.2. [Q14DK4-1]
DR RefSeq; XP_006499201.1; XM_006499138.3. [Q14DK4-1]
DR AlphaFoldDB; Q14DK4; -.
DR STRING; 10090.ENSMUSP00000049619; -.
DR SwissLipids; SLP:000000102; -.
DR iPTMnet; Q14DK4; -.
DR PhosphoSitePlus; Q14DK4; -.
DR PaxDb; Q14DK4; -.
DR PRIDE; Q14DK4; -.
DR ProteomicsDB; 271140; -. [Q14DK4-1]
DR ProteomicsDB; 271141; -. [Q14DK4-2]
DR ProteomicsDB; 271142; -. [Q14DK4-3]
DR Antibodypedia; 32374; 51 antibodies from 11 providers.
DR Ensembl; ENSMUST00000062211; ENSMUSP00000049619; ENSMUSG00000046338. [Q14DK4-1]
DR GeneID; 215456; -.
DR KEGG; mmu:215456; -.
DR UCSC; uc008mfj.2; mouse. [Q14DK4-1]
DR UCSC; uc012cdn.1; mouse. [Q14DK4-2]
DR CTD; 150763; -.
DR MGI; MGI:2684962; Gpat2.
DR VEuPathDB; HostDB:ENSMUSG00000046338; -.
DR eggNOG; KOG3729; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR HOGENOM; CLU_016910_0_0_1; -.
DR InParanoid; Q14DK4; -.
DR OMA; QEYTTNA; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; Q14DK4; -.
DR TreeFam; TF313360; -.
DR BRENDA; 2.3.1.15; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 215456; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q14DK4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q14DK4; protein.
DR Bgee; ENSMUSG00000046338; Expressed in spermatocyte and 38 other tissues.
DR Genevisible; Q14DK4; MM.
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; IDA:MGI.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:1990511; P:piRNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:MGI.
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 Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein 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..801
FT /note="Glycerol-3-phosphate acyltransferase 2,
FT mitochondrial"
FT /id="PRO_0000325854"
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..801
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 MOTIF 205..210
FT /note="HXXXXD motif"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..3
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17689486"
FT /id="VSP_032457"
FT VAR_SEQ 414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032458"
FT MUTAGEN 205
FT /note="H->G: Does not affect ability to promote piRNA
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:23611983"
FT MUTAGEN 210
FT /note="D->G: Does not affect ability to promote piRNA
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:23611983"
FT CONFLICT 150
FT /note="G -> S (in Ref. 5; AAI13166/AAI13777)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="A -> V (in Ref. 3; BAD21404)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="R -> H (in Ref. 5; AAI13166/AAI13777)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="Q -> E (in Ref. 6; BAC30772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 89150 MW; 438B6E1530F27BBC CRC64;
MDTMLKSNPQ TQQRSNHNGQ ETSLWSSSFG MKMEAITPFL GKYRPFMGRC CQTCTPKSWE
SLFHRSIMDL GFCNVILVKE ENTRFRGWLV RRLCYFLWSL EQHIPTSFDA SQKIMENTGV
QNLLSGRVPG AAGEGQAPEL VKKEVQRILG HIQTTPRPFL LRLFSWALLW FLNRLFLNVQ
LHKGQMKMVQ KAVQEGSPLV FLSTHKSLLD GFLLPFVLFS QGLGVVRVAL DSRTCSPALR
ALLRKLGGLF LPPEVNLSLD NSEGILARAV VRATVEELLT SGQPLLIFLE EPPGSPGPRL
SALGQAWLGV VIQAVQAGII SDATLVPVAI AYDLVPDAPC NMNHDLAPLG LWTGALAVFR
RLCNCWGCNR RVCVRVHLAQ PFSLQEYTIN ARSCWDSRQT LEHLLQPIVL GECSVVPDTE
KEQEWTPPTG 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
DSEVAYSEKL FQFLQACAQE EGIFECADPN LAISAVWTFK DLGVLQEMPS PTGPQLHLSP
TFATRDNQDK LEQFIRQFIC S
