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   27-MAR-2024, entry version 132.
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 transfer of an acyl group
CC       from an acyl-CoA to a lysophospholipid leading to the production of a
CC       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; 31.
DR   IntAct; Q6ZWT7; 3.
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; 9606-ENSP00000302177; -.
DR   PeptideAtlas; Q6ZWT7; -.
DR   ProteomicsDB; 68497; -.
DR   Pumba; Q6ZWT7; -.
DR   Antibodypedia; 12361; 92 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   AGR; HGNC:25193; -.
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; ASWPIRF; -.
DR   OrthoDB; 5297955at2759; -.
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; 32 hits in 1157 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 202 other cell types or tissues.
DR   ExpressionAtlas; Q6ZWT7; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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   PANTHER; PTHR13906:SF7; LYSOPHOSPHOLIPID ACYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR13906; PORCUPINE; 1.
DR   Pfam; PF03062; MBOAT; 1.
DR   Genevisible; Q6ZWT7; HS.
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
//