MBOA2_HUMAN
ID MBOA2_HUMAN Reviewed; 520 AA.
AC Q6ZWT7; A9EDR2; Q8NCE7; Q96KY4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000305};
DE Short=LPLAT 2;
DE EC=2.3.1.- {ECO:0000269|PubMed:18772128};
DE AltName: Full=1-acylglycerophosphate O-acyltransferase MBOAT2 {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000269|PubMed:18772128};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase MBOAT2 {ECO:0000305};
DE EC=2.3.1.23 {ECO:0000269|PubMed:18772128};
DE AltName: Full=1-acylglycerophosphoethanolamine MBOAT2 O-acyltransferase {ECO:0000305};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18772128};
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE Short=Lyso-PA acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase;
DE Short=LPCAT;
DE Short=Lyso-PC acyltransferase;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE Short=Lyso-PC acyltransferase 4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE Short=LPEAT;
DE Short=Lyso-PE acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE Short=O-acyltransferase domain-containing protein 2;
GN Name=MBOAT2 {ECO:0000312|HGNC:HGNC:25193};
GN Synonyms=LPCAT4 {ECO:0000250|UniProtKB:Q8R3I2}, OACT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-520.
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY,
RP AND ACTIVITY REGULATION.
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 catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophospholipid leading to the production
CC of a phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (PubMed:18772128). Catalyzes preferentially the acylation of
CC lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine
CC or LPE) and lysophosphatidic acid (LPA) and to a lesser extend
CC lysophosphatidylcholine (LPC) and lysophosphatidylserine (LPS)
CC (PubMed:18772128). Prefers oleoyl-CoA as the acyl donor
CC (PubMed:18772128). May be involved in chondrocyte differentiation (By
CC similarity). {ECO:0000250|UniProtKB:Q8R3I2,
CC ECO:0000269|PubMed:18772128}.
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-
CC phosphoserine + CoA; Xref=Rhea:RHEA:37415, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:74617, ChEBI:CHEBI:74909;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37416;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-[(9Z)-hexadec-9-enoyl]-sn-glycero-3-phosphate +
CC CoA; Xref=Rhea:RHEA:37223, ChEBI:CHEBI:57287, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73998;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37224;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphocholine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37627, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:77287, ChEBI:CHEBI:77294;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37628;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37523, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75036, ChEBI:CHEBI:75038;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphocholine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37519, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37520;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- ACTIVITY REGULATION: Partially inhibited by thimerosal.
CC {ECO:0000269|PubMed:18772128}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18772128}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8R3I2}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils.
CC {ECO:0000269|PubMed:18772128}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11204.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB305044; BAF93900.1; -; mRNA.
DR EMBL; AK027321; BAC85105.1; -; mRNA.
DR EMBL; AC012495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016005; AAH16005.1; -; mRNA.
DR EMBL; BC146871; AAI46872.1; -; mRNA.
DR EMBL; BC157827; AAI57828.1; -; mRNA.
DR EMBL; AK074779; BAC11204.1; ALT_INIT; mRNA.
DR CCDS; CCDS1660.1; -.
DR RefSeq; NP_001308194.1; NM_001321265.1.
DR RefSeq; NP_001308195.1; NM_001321266.1.
DR RefSeq; NP_001308196.1; NM_001321267.1.
DR RefSeq; NP_620154.2; NM_138799.3.
DR AlphaFoldDB; Q6ZWT7; -.
DR SMR; Q6ZWT7; -.
DR BioGRID; 126201; 26.
DR IntAct; Q6ZWT7; 4.
DR MINT; Q6ZWT7; -.
DR STRING; 9606.ENSP00000302177; -.
DR SwissLipids; SLP:000000134; -.
DR iPTMnet; Q6ZWT7; -.
DR PhosphoSitePlus; Q6ZWT7; -.
DR SwissPalm; Q6ZWT7; -.
DR BioMuta; MBOAT2; -.
DR DMDM; 143811417; -.
DR EPD; Q6ZWT7; -.
DR jPOST; Q6ZWT7; -.
DR MassIVE; Q6ZWT7; -.
DR MaxQB; Q6ZWT7; -.
DR PaxDb; Q6ZWT7; -.
DR PeptideAtlas; Q6ZWT7; -.
DR PRIDE; Q6ZWT7; -.
DR ProteomicsDB; 68497; -.
DR Antibodypedia; 12361; 79 antibodies from 19 providers.
DR DNASU; 129642; -.
DR Ensembl; ENST00000305997.8; ENSP00000302177.3; ENSG00000143797.12.
DR GeneID; 129642; -.
DR KEGG; hsa:129642; -.
DR MANE-Select; ENST00000305997.8; ENSP00000302177.3; NM_138799.4; NP_620154.2.
DR UCSC; uc002qzg.2; human.
DR CTD; 129642; -.
DR DisGeNET; 129642; -.
DR GeneCards; MBOAT2; -.
DR HGNC; HGNC:25193; MBOAT2.
DR HPA; ENSG00000143797; Low tissue specificity.
DR MIM; 611949; gene.
DR neXtProt; NX_Q6ZWT7; -.
DR OpenTargets; ENSG00000143797; -.
DR PharmGKB; PA134987740; -.
DR VEuPathDB; HostDB:ENSG00000143797; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q6ZWT7; -.
DR OMA; WAISIFE; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q6ZWT7; -.
DR TreeFam; TF314906; -.
DR BRENDA; 2.3.1.23; 2681.
DR PathwayCommons; Q6ZWT7; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q6ZWT7; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 129642; 31 hits in 1079 CRISPR screens.
DR ChiTaRS; MBOAT2; human.
DR GenomeRNAi; 129642; -.
DR Pharos; Q6ZWT7; Tbio.
DR PRO; PR:Q6ZWT7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6ZWT7; protein.
DR Bgee; ENSG00000143797; Expressed in corpus callosum and 201 other tissues.
DR ExpressionAtlas; Q6ZWT7; baseline and differential.
DR Genevisible; Q6ZWT7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..520
FT /note="Lysophospholipid acyltransferase 2"
FT /id="PRO_0000273020"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 342
FT /evidence="ECO:0000250"
FT ACT_SITE 373
FT /evidence="ECO:0000250"
FT VARIANT 501
FT /note="T -> A (in dbSNP:rs16866827)"
FT /id="VAR_030068"
FT CONFLICT 402
FT /note="H -> R (in Ref. 5; BAC11204)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="K -> R (in Ref. 2; BAC85105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 59527 MW; 27FFC44815B21288 CRC64;
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK TSSFIRHVVA
TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN YCFVFALGYL TVCQVTRVYI
FDYGQYSADF SGPMMIITQK ITSLACEIHD GMFRKDEELT SSQRDLAVRR MPSLLEYLSY
NCNFMGILAG PLCSYKDYIT FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC
GLSLLFHLTI CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN
AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK RVCYERTSFS
PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF RHYFIEPSQL KLFYDVITWI
VTQVAISYTV VPFVLLSIKP SLTFYSSWYY CLHILGILVL LLLPVKKTQR RKNTHENIQL
SQSKKFDEGE NSLGQNSFST TNNVCNQNQE IASRHSSLKQ
