MBOA7_DROME
ID MBOA7_DROME Reviewed; 489 AA.
AC Q9VMD5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lysophospholipid acyltransferase 7;
DE Short=LPLAT 7;
DE EC=2.3.1.- {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.23 {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:19864461};
DE AltName: Full=Farjavit {ECO:0000303|PubMed:19864461};
DE Short=Frj {ECO:0000303|PubMed:19864461};
DE AltName: Full=Membrane-bound acyltransferase 7;
DE Short=MBOA 7 {ECO:0000303|PubMed:19864461};
GN Name=frj {ECO:0000303|PubMed:19864461, ECO:0000312|EMBL:AAF52384.1,
GN ECO:0000312|FlyBase:FBgn0031815};
GN ORFNames=CG9526 {ECO:0000312|EMBL:AAF52384.1,
GN ECO:0000312|FlyBase:FBgn0031815};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAO25028.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO25028.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=19864461; DOI=10.1091/mbc.e09-05-0382;
RA Steinhauer J., Gijon M.A., Riekhof W.R., Voelker D.R., Murphy R.C.,
RA Treisman J.E.;
RT "Drosophila lysophospholipid acyltransferases are specifically required for
RT germ cell development.";
RL Mol. Biol. Cell 20:5224-5235(2009).
CC -!- FUNCTION: Acyltransferase that mediates the acylation of
CC lysophospholipids to produce phospholipids (glycerophospholipids).
CC Highest activity with lysophosphatidylinositol (1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) or LPI) producing phosphatidylinositol (1,2-
CC diacyl-sn-glycero-3-phospho-(1D-myo-inositol) or PI) (LPIAT activity),
CC but also converts lysophosphatidylcholine (1-acyl-sn-glycero-3-
CC phosphocholine or LPC) to phosphatidylcholine (1,2-diacyl-sn-glycero-3-
CC phosphocholine or PC) (LPCAT activity), lysophosphatidylserine (1-acyl-
CC 2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) to phosphatidylserine
CC (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity), and
CC lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine
CC or LPE) producing phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine or PE) (LPEAT activity). Has a preference for
CC unsaturated fatty acid arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-CoA). Glycerophospholipids are important structural
CC and functional components of cellular membrane, acyl-chain remodeling
CC regulates the molecular species distribution of glycerophospholipids
CC which can affect membrane fluidity and curvature.
CC {ECO:0000269|PubMed:19864461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37015, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64771, ChEBI:CHEBI:75243;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37399,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74901; Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37400;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:19864461}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19864461}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF52384.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64645.1; -; Genomic_DNA.
DR EMBL; BT003271; AAO25028.1; -; mRNA.
DR RefSeq; NP_609029.1; NM_135185.4.
DR RefSeq; NP_995637.1; NM_205915.3.
DR AlphaFoldDB; Q9VMD5; -.
DR SMR; Q9VMD5; -.
DR STRING; 7227.FBpp0078889; -.
DR SwissLipids; SLP:000001064; -.
DR PaxDb; Q9VMD5; -.
DR PRIDE; Q9VMD5; -.
DR DNASU; 33900; -.
DR EnsemblMetazoa; FBtr0079258; FBpp0078888; FBgn0031815.
DR EnsemblMetazoa; FBtr0079259; FBpp0078889; FBgn0031815.
DR GeneID; 33900; -.
DR KEGG; dme:Dmel_CG9526; -.
DR UCSC; CG9526-RA; d. melanogaster.
DR CTD; 33900; -.
DR FlyBase; FBgn0031815; frj.
DR VEuPathDB; VectorBase:FBgn0031815; -.
DR eggNOG; KOG2706; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; Q9VMD5; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q9VMD5; -.
DR Reactome; R-DME-1482922; Acyl chain remodelling of PI.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 33900; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33900; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031815; Expressed in cleaving embryo and 46 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:FlyBase.
DR GO; GO:0030258; P:lipid modification; IMP:FlyBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..489
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000453373"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 331
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
SQ SEQUENCE 489 AA; 56308 MW; 5F0B0501E663D8A9 CRC64;
MSIDDVIYVI CLLGCIGAGS YVKKIADEGQ RKLVSTGLGV LVVVIVSGLH SLHCFVSLAL
GTAAVLLVHP SKGHLVTFAV MFGYLVFFRI FDFYFGIPGH TNMIQMILTL KVSGIAFEKT
AAWKRLQAHD EQKKNDQRDV HQESPIEITD YDVELQSLSA AEILHYSFNY IGVLTGPYYR
YRTYRDYFEM PFKTYAPTVE ATLEKLKYAV FYCALYLATN YMWPLDYALS DEFFNDRSFV
YRLLYVWPTF FTFRARIYTG LTLSECVCTM AGFGAYPDES DPNNGEGPRK RYQHLKRDAD
KHTYNFTTIV NTRVLEVERC WTFREGMKHW NVCVQYWLAV NVYKLFPSKK YRTGATLLCS
AYWHGFRPGH YFCIMGAPFY VSLEDMWDKL VRKSATGTSR RVIDVIFWIF KWFAFSYLGE
AFLLSSFGNI WRFYSSVYHI GYISWAAMTA LGFYLTSQRK AAERRKKRAA EKAAGGDGIA
AAIEKEKAQ
