Full text data of LPCAT3
LPCAT3
(MBOAT5, OACT5)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Lysophospholipid acyltransferase 5; LPLAT 5; 2.3.1.- (1-acylglycerophosphocholine O-acyltransferase; 2.3.1.23; 1-acylglycerophosphoserine O-acyltransferase; 2.3.1.n6; Lysophosphatidylcholine acyltransferase; LPCAT; Lyso-PC acyltransferase; Lysophosphatidylcholine acyltransferase 3; Lyso-PC acyltransferase 3; Lysophosphatidylserine acyltransferase; LPSAT; Lyso-PS acyltransferase; Membrane-bound O-acyltransferase domain-containing protein 5; O-acyltransferase domain-containing protein 5)
Lysophospholipid acyltransferase 5; LPLAT 5; 2.3.1.- (1-acylglycerophosphocholine O-acyltransferase; 2.3.1.23; 1-acylglycerophosphoserine O-acyltransferase; 2.3.1.n6; Lysophosphatidylcholine acyltransferase; LPCAT; Lyso-PC acyltransferase; Lysophosphatidylcholine acyltransferase 3; Lyso-PC acyltransferase 3; Lysophosphatidylserine acyltransferase; LPSAT; Lyso-PS acyltransferase; Membrane-bound O-acyltransferase domain-containing protein 5; O-acyltransferase domain-containing protein 5)
hRBCD
IPI00306419
IPI00306419 gene rich cluster, C3f gene gene rich cluster, C3f gene membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a 1 n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00306419 gene rich cluster, C3f gene gene rich cluster, C3f gene membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a 1 n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q6P1A2
ID MBOA5_HUMAN Reviewed; 487 AA.
AC Q6P1A2; B2RDH0; Q7KZS1; Q92980; Q9BW40;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23;
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6;
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 3;
DE Short=Lyso-PC acyltransferase 3;
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;
GN Name=LPCAT3; Synonyms=MBOAT5, OACT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487.
RX PubMed=9074930;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-487.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18195019; DOI=10.1074/jbc.M710422200;
RA Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R.,
RA Moller D.E., Kowala M., Konrad R.J., Cao G.;
RT "Identification and characterization of a major liver
RT lysophosphatidylcholine acyltransferase.";
RL J. Biol. Chem. 283:8258-8265(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18772128; DOI=10.1074/jbc.M806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or
CC LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-
CC phosphocholine or PC) (LPCAT activity). Catalyzes also the
CC conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-
CC 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-
CC glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak
CC lysophosphatidylethanolamine acyltransferase activity (LPEAT
CC activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors
CC compared to saturated fatty acyl-CoAs. Seems to be the major
CC enzyme contributing to LPCAT activity in the liver.
CC Lysophospholipid acyltransferases (LPLATs) catalyze the
CC reacylation step of the phospholipid remodeling pathway also known
CC as the Lands cycle.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-
CC phosphatidylserine.
CC -!- ENZYME REGULATION: Activity is inhibited by thimerosal.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.29 uM for palmitoyl-CoA;
CC KM=36.65 uM for stearoyl-CoA;
CC KM=72.68 uM for oleoyl-CoA;
CC KM=201.4 uM for linoleoyl-CoA;
CC KM=71.56 uM for arachidonoyl-CoA;
CC KM=72.19 uM for 1-palmitoyl-lysophosphatidylcholine;
CC Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-
CC palmitoyl-lysophosphatidylcholine as substrates;
CC Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-
CC palmitoyl-lysophosphatidylcholine as substrates;
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, pancreas and
CC adipose tissue. Very low expression in skeletal muscle and heart.
CC Detected in neutrophils.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51326.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC51640.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG37917.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; BX648009; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC006512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000664; AAH00664.2; -; mRNA.
DR EMBL; BC065194; AAH65194.1; -; mRNA.
DR EMBL; U47924; AAB51326.1; ALT_INIT; Genomic_DNA.
DR EMBL; U72515; AAC51640.1; ALT_INIT; mRNA.
DR EMBL; AK315538; BAG37917.1; ALT_INIT; mRNA.
DR EMBL; BT007000; AAP35646.1; -; mRNA.
DR RefSeq; NP_005759.4; NM_005768.5.
DR UniGene; Hs.655248; -.
DR ProteinModelPortal; Q6P1A2; -.
DR MINT; MINT-3049790; -.
DR PhosphoSite; Q6P1A2; -.
DR DMDM; 74737127; -.
DR PaxDb; Q6P1A2; -.
DR PRIDE; Q6P1A2; -.
DR DNASU; 10162; -.
DR Ensembl; ENST00000261407; ENSP00000261407; ENSG00000111684.
DR GeneID; 10162; -.
DR KEGG; hsa:10162; -.
DR UCSC; uc001qsi.3; human.
DR CTD; 10162; -.
DR GeneCards; GC12M007085; -.
DR H-InvDB; HIX0129675; -.
DR HGNC; HGNC:30244; LPCAT3.
DR MIM; 611950; gene.
DR neXtProt; NX_Q6P1A2; -.
DR PharmGKB; PA162394266; -.
DR eggNOG; COG5202; -.
DR HOGENOM; HOG000019529; -.
DR HOVERGEN; HBG054659; -.
DR InParanoid; Q6P1A2; -.
DR KO; K13515; -.
DR OMA; WLKVYKS; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; LPCAT3; human.
DR GeneWiki; MBOAT5; -.
DR GenomeRNAi; 10162; -.
DR NextBio; 38474; -.
DR PRO; PR:Q6P1A2; -.
DR ArrayExpress; Q6P1A2; -.
DR Bgee; Q6P1A2; -.
DR CleanEx; HS_LPCAT3; -.
DR Genevestigator; Q6P1A2; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:MGI.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Complete proteome; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 487 Lysophospholipid acyltransferase 5.
FT /FTId=PRO_0000233382.
FT TRANSMEM 44 64 Helical; (Potential).
FT TRANSMEM 84 104 Helical; (Potential).
FT TRANSMEM 111 131 Helical; (Potential).
FT TRANSMEM 180 200 Helical; (Potential).
FT TRANSMEM 227 247 Helical; (Potential).
FT TRANSMEM 285 305 Helical; (Potential).
FT TRANSMEM 364 384 Helical; (Potential).
FT TRANSMEM 422 442 Helical; (Potential).
FT TRANSMEM 453 473 Helical; (Potential).
FT MOTIF 484 487 Di-lysine motif.
FT ACT_SITE 374 374 By similarity.
FT VARIANT 63 63 F -> L (in dbSNP:rs34196984).
FT /FTId=VAR_050027.
FT VARIANT 217 217 I -> T (in dbSNP:rs1984564).
FT /FTId=VAR_050028.
FT CONFLICT 387 387 E -> K (in Ref. 3; AAH00664 and 6;
FT AAP35646).
SQ SEQUENCE 487 AA; 56035 MW; 429258B54585B4A7 CRC64;
MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL GYPFALFYRH
YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ FLILRLMGRT ITAVLTTFCF
QMAYLLAGYY YTATGNYDIK WTMPHCVLTL KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY
LVGYTLLSPH ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL
GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL IQESPTLSKL AAITVLQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YKSIYFLGHI FFLSLLFILP YIHKAMVPRK
EKLKKME
//
ID MBOA5_HUMAN Reviewed; 487 AA.
AC Q6P1A2; B2RDH0; Q7KZS1; Q92980; Q9BW40;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23;
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6;
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 3;
DE Short=Lyso-PC acyltransferase 3;
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;
GN Name=LPCAT3; Synonyms=MBOAT5, OACT5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487.
RX PubMed=9074930;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-487.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18195019; DOI=10.1074/jbc.M710422200;
RA Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R.,
RA Moller D.E., Kowala M., Konrad R.J., Cao G.;
RT "Identification and characterization of a major liver
RT lysophosphatidylcholine acyltransferase.";
RL J. Biol. Chem. 283:8258-8265(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18772128; DOI=10.1074/jbc.M806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or
CC LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-
CC phosphocholine or PC) (LPCAT activity). Catalyzes also the
CC conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-
CC 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-
CC glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak
CC lysophosphatidylethanolamine acyltransferase activity (LPEAT
CC activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors
CC compared to saturated fatty acyl-CoAs. Seems to be the major
CC enzyme contributing to LPCAT activity in the liver.
CC Lysophospholipid acyltransferases (LPLATs) catalyze the
CC reacylation step of the phospholipid remodeling pathway also known
CC as the Lands cycle.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-
CC phosphatidylserine.
CC -!- ENZYME REGULATION: Activity is inhibited by thimerosal.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.29 uM for palmitoyl-CoA;
CC KM=36.65 uM for stearoyl-CoA;
CC KM=72.68 uM for oleoyl-CoA;
CC KM=201.4 uM for linoleoyl-CoA;
CC KM=71.56 uM for arachidonoyl-CoA;
CC KM=72.19 uM for 1-palmitoyl-lysophosphatidylcholine;
CC Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-
CC lysophosphatidylcholine as substrates;
CC Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-
CC palmitoyl-lysophosphatidylcholine as substrates;
CC Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-
CC palmitoyl-lysophosphatidylcholine as substrates;
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, pancreas and
CC adipose tissue. Very low expression in skeletal muscle and heart.
CC Detected in neutrophils.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51326.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC51640.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAG37917.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; BX648009; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC006512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000664; AAH00664.2; -; mRNA.
DR EMBL; BC065194; AAH65194.1; -; mRNA.
DR EMBL; U47924; AAB51326.1; ALT_INIT; Genomic_DNA.
DR EMBL; U72515; AAC51640.1; ALT_INIT; mRNA.
DR EMBL; AK315538; BAG37917.1; ALT_INIT; mRNA.
DR EMBL; BT007000; AAP35646.1; -; mRNA.
DR RefSeq; NP_005759.4; NM_005768.5.
DR UniGene; Hs.655248; -.
DR ProteinModelPortal; Q6P1A2; -.
DR MINT; MINT-3049790; -.
DR PhosphoSite; Q6P1A2; -.
DR DMDM; 74737127; -.
DR PaxDb; Q6P1A2; -.
DR PRIDE; Q6P1A2; -.
DR DNASU; 10162; -.
DR Ensembl; ENST00000261407; ENSP00000261407; ENSG00000111684.
DR GeneID; 10162; -.
DR KEGG; hsa:10162; -.
DR UCSC; uc001qsi.3; human.
DR CTD; 10162; -.
DR GeneCards; GC12M007085; -.
DR H-InvDB; HIX0129675; -.
DR HGNC; HGNC:30244; LPCAT3.
DR MIM; 611950; gene.
DR neXtProt; NX_Q6P1A2; -.
DR PharmGKB; PA162394266; -.
DR eggNOG; COG5202; -.
DR HOGENOM; HOG000019529; -.
DR HOVERGEN; HBG054659; -.
DR InParanoid; Q6P1A2; -.
DR KO; K13515; -.
DR OMA; WLKVYKS; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; LPCAT3; human.
DR GeneWiki; MBOAT5; -.
DR GenomeRNAi; 10162; -.
DR NextBio; 38474; -.
DR PRO; PR:Q6P1A2; -.
DR ArrayExpress; Q6P1A2; -.
DR Bgee; Q6P1A2; -.
DR CleanEx; HS_LPCAT3; -.
DR Genevestigator; Q6P1A2; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:MGI.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Complete proteome; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 487 Lysophospholipid acyltransferase 5.
FT /FTId=PRO_0000233382.
FT TRANSMEM 44 64 Helical; (Potential).
FT TRANSMEM 84 104 Helical; (Potential).
FT TRANSMEM 111 131 Helical; (Potential).
FT TRANSMEM 180 200 Helical; (Potential).
FT TRANSMEM 227 247 Helical; (Potential).
FT TRANSMEM 285 305 Helical; (Potential).
FT TRANSMEM 364 384 Helical; (Potential).
FT TRANSMEM 422 442 Helical; (Potential).
FT TRANSMEM 453 473 Helical; (Potential).
FT MOTIF 484 487 Di-lysine motif.
FT ACT_SITE 374 374 By similarity.
FT VARIANT 63 63 F -> L (in dbSNP:rs34196984).
FT /FTId=VAR_050027.
FT VARIANT 217 217 I -> T (in dbSNP:rs1984564).
FT /FTId=VAR_050028.
FT CONFLICT 387 387 E -> K (in Ref. 3; AAH00664 and 6;
FT AAP35646).
SQ SEQUENCE 487 AA; 56035 MW; 429258B54585B4A7 CRC64;
MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL GYPFALFYRH
YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ FLILRLMGRT ITAVLTTFCF
QMAYLLAGYY YTATGNYDIK WTMPHCVLTL KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY
LVGYTLLSPH ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL
GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL IQESPTLSKL AAITVLQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YKSIYFLGHI FFLSLLFILP YIHKAMVPRK
EKLKKME
//
MIM
611950
*RECORD*
*FIELD* NO
611950
*FIELD* TI
*611950 MEMBRANE-BOUND O-ACYLTRANSFERASE DOMAIN-CONTAINING 5; MBOAT5
;;MEMBRANE-BOUND O-ACYLTRANSFERASE 5;;
read moreLYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE 3; LPCAT3;;
NESSY, DROSOPHILA, HOMOLOG OF
*FIELD* TX
CLONING
Maurel-Zaffran et al. (1999) identified human and mouse MBOAT5 as
homologs of Drosophila nessy. The deduced 487-amino acid human and mouse
MBOAT5 proteins contain 11 predicted transmembrane domains and share 88%
amino acid identity. Human MBOAT5 shares 35% amino acid identity with
Drosophila nessy.
Hishikawa et al. (2008) cloned mouse Mboat5, which they called Lpcat3.
The deduced protein contains 10 putative transmembrane domains and a
C-terminal endoplasmic reticulum (ER) retention motif (KKxx). RT-PCR
detected ubiquitous Lpcat3 expression, with highest level in testis.
Lpcat3 colocalized with an ER marker protein in transfected Chinese
hamster ovary cells.
GENE FUNCTION
Hishikawa et al. (2008) found that mouse Lpcat3 converted
lysophosphatidylcholine, lysophosphatidylethanolamine, and
lysophosphatidylserine to phosphatidylcholine, phosphatidylethanolamine,
and phosphatidylserine, respectively, using polyunsaturated fatty
acyl-CoAs as acyl donors. Knockdown of Lpcat3 in mouse melanoma cells
with small interfering RNA significantly reduced cellular
acyltransferase activity toward endogenous lysophosphatidylcholine,
lysophosphatidylethanolamine, and lysophosphatidylserine.
Maurel-Zaffran et al. (1999) found that expression of Drosophila nessy
was controlled by Hox proteins (e.g., HOXA7; 142950) during
embryogenesis.
MAPPING
Maurel-Zaffran et al. (1999) stated that the MBOAT5 gene maps to
chromosome 12p13.
*FIELD* RF
1. Hishikawa, D.; Shindou, H.; Kobayashi, S.; Nakanishi, H.; Taguchi,
R.; Shimizu, T.: Discovery of a lysophospholipid acyltransferase
family essential for membrane asymmetry and diversity. Proc. Nat.
Acad. Sci. 105: 2830-2835, 2008.
2. Maurel-Zaffran, C.; Chauvet, S.; Jullien, N.; Miassod, R.; Pradel,
J.; Aragnol, D.: nessy, an evolutionary conserved gene controlled
by Hox proteins during Drosophila embryogenesis. Mech. Dev. 86:
159-163, 1999.
*FIELD* CD
Patricia A. Hartz: 4/14/2008
*FIELD* ED
mgross: 04/14/2008
*RECORD*
*FIELD* NO
611950
*FIELD* TI
*611950 MEMBRANE-BOUND O-ACYLTRANSFERASE DOMAIN-CONTAINING 5; MBOAT5
;;MEMBRANE-BOUND O-ACYLTRANSFERASE 5;;
read moreLYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE 3; LPCAT3;;
NESSY, DROSOPHILA, HOMOLOG OF
*FIELD* TX
CLONING
Maurel-Zaffran et al. (1999) identified human and mouse MBOAT5 as
homologs of Drosophila nessy. The deduced 487-amino acid human and mouse
MBOAT5 proteins contain 11 predicted transmembrane domains and share 88%
amino acid identity. Human MBOAT5 shares 35% amino acid identity with
Drosophila nessy.
Hishikawa et al. (2008) cloned mouse Mboat5, which they called Lpcat3.
The deduced protein contains 10 putative transmembrane domains and a
C-terminal endoplasmic reticulum (ER) retention motif (KKxx). RT-PCR
detected ubiquitous Lpcat3 expression, with highest level in testis.
Lpcat3 colocalized with an ER marker protein in transfected Chinese
hamster ovary cells.
GENE FUNCTION
Hishikawa et al. (2008) found that mouse Lpcat3 converted
lysophosphatidylcholine, lysophosphatidylethanolamine, and
lysophosphatidylserine to phosphatidylcholine, phosphatidylethanolamine,
and phosphatidylserine, respectively, using polyunsaturated fatty
acyl-CoAs as acyl donors. Knockdown of Lpcat3 in mouse melanoma cells
with small interfering RNA significantly reduced cellular
acyltransferase activity toward endogenous lysophosphatidylcholine,
lysophosphatidylethanolamine, and lysophosphatidylserine.
Maurel-Zaffran et al. (1999) found that expression of Drosophila nessy
was controlled by Hox proteins (e.g., HOXA7; 142950) during
embryogenesis.
MAPPING
Maurel-Zaffran et al. (1999) stated that the MBOAT5 gene maps to
chromosome 12p13.
*FIELD* RF
1. Hishikawa, D.; Shindou, H.; Kobayashi, S.; Nakanishi, H.; Taguchi,
R.; Shimizu, T.: Discovery of a lysophospholipid acyltransferase
family essential for membrane asymmetry and diversity. Proc. Nat.
Acad. Sci. 105: 2830-2835, 2008.
2. Maurel-Zaffran, C.; Chauvet, S.; Jullien, N.; Miassod, R.; Pradel,
J.; Aragnol, D.: nessy, an evolutionary conserved gene controlled
by Hox proteins during Drosophila embryogenesis. Mech. Dev. 86:
159-163, 1999.
*FIELD* CD
Patricia A. Hartz: 4/14/2008
*FIELD* ED
mgross: 04/14/2008