MBOA5_DROME
ID MBOA5_DROME Reviewed; 497 AA.
AC Q9VVX5; A4V238; Q9XYV9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:19864461};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000269|PubMed:19864461};
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
DE Short=O-acyltransferase domain-containing protein 5;
DE AltName: Full=Protein nessy {ECO:0000303|PubMed:10446276, ECO:0000303|PubMed:19864461};
DE Short=Nes {ECO:0000303|PubMed:10446276, ECO:0000303|PubMed:19864461};
GN Name=nes {ECO:0000303|PubMed:10446276, ECO:0000312|EMBL:AAF49181.1,
GN ECO:0000312|FlyBase:FBgn0026630};
GN Synonyms=nessy {ECO:0000312|EMBL:AAD28257.1}; ORFNames=CG9655;
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] {ECO:0000312|EMBL:AAF49181.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000312|EMBL:AAF49181.1}
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:AAD28257.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10446276};
RX PubMed=10446276; DOI=10.1016/s0925-4773(99)00105-7;
RA Maurel-Zaffran C., Chauvet S., Jullien N., Miassod R., Pradel J.,
RA Aragnol D.;
RT "nessy, an evolutionary conserved gene controlled by Hox proteins during
RT Drosophila embryogenesis.";
RL Mech. Dev. 86:159-163(1999).
RN [4] {ECO:0000312|EMBL:AAL48558.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
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 lysophosphatidylcholine (1-acyl-sn-glycero-3-
CC phosphocholine or LPC) producing phosphatidylcholine (1,2-diacyl-sn-
CC glycero-3-phosphocholine or PC) (LPCAT activity), but also converts
CC lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine
CC or LPS) to phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine
CC or PS) (LPSAT activity). Has a preference for unsaturated fatty acids
CC of at least 16 carbons such as oleoyl-CoA ((9Z)-octadecenoyl-CoA) and
CC palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA). Glycerophospholipids are
CC important structural and functional components of cellular membrane,
CC acyl-chain remodeling regulates the molecular species distribution of
CC glycerophospholipids which can affect membrane fluidity and curvature.
CC Essential for fertility and viability together with Oysgedart (Oys).
CC Required for germ cells to migrate into the mesoderm.
CC {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-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)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
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 -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:19864461}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:19864461}. Membrane {ECO:0000269|PubMed:19864461};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: During gastrulation, expressed mainly along the
CC midline in the presumptive mesoderm. During germ band elongation,
CC expressed in mesoderm and endoderm primordia and in the cephalic
CC furrow. Expression in mesoderm and endoderm lineages continues during
CC germ band shortening. At the end of this process, no longer detected in
CC somatic mesoderm or endoderm layer with expression restricted to
CC anterior and posterior domains of the visceral mesoderm.
CC {ECO:0000269|PubMed:10446276}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development with highest
CC levels in adult females and preblastoderm embryos.
CC {ECO:0000269|PubMed:10446276}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although strongly related to the membrane-bound
CC acyltransferase family, it lacks the conserved His active site which is
CC replaced by an Asn-415 residue. {ECO:0000305}.
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DR EMBL; AE014296; AAF49181.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11657.1; -; Genomic_DNA.
DR EMBL; AE014296; AAO41223.1; -; Genomic_DNA.
DR EMBL; AF128112; AAD28257.1; -; mRNA.
DR EMBL; AY070936; AAL48558.1; -; mRNA.
DR RefSeq; NP_524157.2; NM_079433.3.
DR RefSeq; NP_730390.1; NM_168788.3.
DR RefSeq; NP_788527.1; NM_176349.2.
DR AlphaFoldDB; Q9VVX5; -.
DR SMR; Q9VVX5; -.
DR BioGRID; 65369; 1.
DR STRING; 7227.FBpp0074786; -.
DR SwissLipids; SLP:000001062; -.
DR GlyGen; Q9VVX5; 1 site.
DR iPTMnet; Q9VVX5; -.
DR PaxDb; Q9VVX5; -.
DR PRIDE; Q9VVX5; -.
DR DNASU; 40093; -.
DR EnsemblMetazoa; FBtr0075019; FBpp0074786; FBgn0026630.
DR EnsemblMetazoa; FBtr0075020; FBpp0074787; FBgn0026630.
DR EnsemblMetazoa; FBtr0075021; FBpp0074788; FBgn0026630.
DR GeneID; 40093; -.
DR KEGG; dme:Dmel_CG9655; -.
DR UCSC; CG9655-RA; d. melanogaster.
DR CTD; 10763; -.
DR FlyBase; FBgn0026630; nes.
DR VEuPathDB; VectorBase:FBgn0026630; -.
DR eggNOG; KOG2705; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_6_0_1; -.
DR InParanoid; Q9VVX5; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q9VVX5; -.
DR Reactome; R-DME-1482788; Acyl chain remodelling of PC.
DR Reactome; R-DME-1482801; Acyl chain remodelling of PS.
DR Reactome; R-DME-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 40093; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40093; -.
DR PRO; PR:Q9VVX5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0026630; Expressed in thoracico-abdominal ganglion (Drosophila) and 29 other tissues.
DR Genevisible; Q9VVX5; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IGI:FlyBase.
DR GO; GO:0030258; P:lipid modification; IMP:FlyBase.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IGI:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IGI:FlyBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..497
FT /note="Lysophospholipid acyltransferase 5"
FT /id="PRO_0000233380"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 469..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 322
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT ACT_SITE 358
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 75
FT /note="L -> R (in Ref. 3; AAD28257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 57394 MW; 4927EFBD784BF861 CRC64;
MAEFEEDLPH NGLMDGIASG VGVPVEALRL LLTILAGYPV AALYQKFISV IADKTVHHMF
FAGCGAGLCY FNYGLDTYHS LIAILTTYFL VLLLRKKTQI FLAINFVFHM SYLLLGYFYT
SSNDYDILWT MPHCILVLRM IGYGFDITDG LKEESELSKD QKETALKKPP SLLELLAFSY
FPSGFLVGPQ FPFRRYKAFV DGEFRQHEGN VEAGVRRFGA GAFYLIVCQV GLRYLPDSYF
LTPEFAQVSF VKRIYLLGFW AKFSLYKYIS CWLLTEGALI CIGLTYKGED KNGQPDWSGC
SNVKLKLLET GNTMEHYVQS FNVNTNQWVG QYIYKRLKFL NNRTISYGAA LGFLAVWHGY
HSGYYMTFLM EYMVVSTEKQ ITRFYTKVVL PQWGHILNNS DIYKLLYFIT LKSYNVVYMG
WCLTAFVFLK YERWIVVYGA VSYYGFTFLV LWAAFYHTFN HFFRSSSRKL AGEDQKLQDS
NTDKLVEEKK PEDKKSE
