PLAT2_HUMAN
ID PLAT2_HUMAN Reviewed; 162 AA.
AC Q9NWW9; B9A7L8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phospholipase A and acyltransferase 2 {ECO:0000312|HGNC:HGNC:17824};
DE EC=2.3.1.- {ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852};
DE EC=3.1.1.32 {ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852};
DE EC=3.1.1.4 {ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852};
DE AltName: Full=HRAS-like suppressor 2;
GN Name=PLAAT2 {ECO:0000312|HGNC:HGNC:17824}; Synonyms=HRASLS2;
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], FUNCTION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC TISSUE=Testis;
RX PubMed=19615464; DOI=10.1016/j.bbalip.2009.07.001;
RA Uyama T., Jin X.H., Tsuboi K., Tonai T., Ueda N.;
RT "Characterization of the human tumor suppressors TIG3 and HRASLS2 as
RT phospholipid-metabolizing enzymes.";
RL Biochim. Biophys. Acta 1791:1114-1124(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Signet-ring cell carcinoma;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18163183; DOI=10.1007/s00726-007-0612-2;
RA Shyu R.Y., Hsieh Y.C., Tsai F.M., Wu C.C., Jiang S.Y.;
RT "Cloning and functional characterization of the HRASLS2 gene.";
RL Amino Acids 35:129-137(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-113.
RX PubMed=22825852; DOI=10.1074/jbc.m112.368712;
RA Uyama T., Ikematsu N., Inoue M., Shinohara N., Jin X.H., Tsuboi K.,
RA Tonai T., Tokumura A., Ueda N.;
RT "Generation of N-acylphosphatidylethanolamine by members of the
RT phospholipase A/acyltransferase (PLA/AT) family.";
RL J. Biol. Chem. 287:31905-31919(2012).
RN [6]
RP REVIEW.
RX PubMed=26503625; DOI=10.1186/s12929-015-0210-7;
RA Mardian E.B., Bradley R.M., Duncan R.E.;
RT "The HRASLS (PLA/AT) subfamily of enzymes.";
RL J. Biomed. Sci. 22:99-99(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1-129, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, AND SUBCELLULAR LOCATION.
RX PubMed=22605381; DOI=10.1074/jbc.m112.361550;
RA Golczak M., Kiser P.D., Sears A.E., Lodowski D.T., Blaner W.S.,
RA Palczewski K.;
RT "Structural basis for the acyltransferase activity of lecithin:retinol
RT acyltransferase-like proteins.";
RL J. Biol. Chem. 287:23790-23807(2012).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (PubMed:19615464, PubMed:22825852, PubMed:22605381,
CC PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity,
CC catalyzing the calcium-independent release of fatty acids from the sn-1
CC or sn-2 position of glycerophospholipids (PubMed:19615464,
CC PubMed:22825852, PubMed:22605381). For most substrates, PLA1 activity
CC is much higher than PLA2 activity (PubMed:19615464). Shows O-
CC acyltransferase activity, catalyzing the transfer of a fatty acyl group
CC from glycerophospholipid to the hydroxyl group of lysophospholipid
CC (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the
CC calcium-independent transfer of a fatty acyl group at the sn-1 position
CC of phosphatidylcholine (PC) and other glycerophospholipids to the
CC primary amine of phosphatidylethanolamine (PE), forming N-
CC acylphosphatidylethanolamine (NAPE), which serves as precursor for N-
CC acylethanolamines (NAEs) (PubMed:19615464, PubMed:22825852,
CC PubMed:22605381). Catalyzes N-acylation of PE using both sn-1 and sn-2
CC palmitoyl groups of PC as acyl donor (PubMed:22605381). Exhibits high
CC phospholipase A1/2 activity and low N-acyltransferase activity
CC (PubMed:22825852). {ECO:0000269|PubMed:19615464,
CC ECO:0000269|PubMed:22605381, ECO:0000269|PubMed:22825852,
CC ECO:0000303|PubMed:26503625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381,
CC ECO:0000269|PubMed:22825852};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381,
CC ECO:0000269|PubMed:22825852};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-3-phosphocholine
CC + H(+) + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:62537, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45193;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine = a 2-acyl-sn-glycero-3-phosphocholine
CC + H(+) + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45188, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:57875, ChEBI:CHEBI:62537, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45189;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = 2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:45164,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:76090;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45165;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 2-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+) + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45172,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:74986,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:19615464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173;
CC Evidence={ECO:0000269|PubMed:19615464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+) + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45176,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22825852};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45177;
CC Evidence={ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22825852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexanoyl-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:53500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:78215, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53501;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-hexadecanoyl-ethanolamine + 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53524, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:74667, ChEBI:CHEBI:138218, ChEBI:CHEBI:138220;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53525;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptadecanoyl-sn-glycero-3-phosphoethanolamine + 1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC diheptadecanoyl-sn-glycero-3-phospho-N-(9Z-octadecenoyl)-ethanolamine
CC + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:53528, ChEBI:CHEBI:15378, ChEBI:CHEBI:74667,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:138218, ChEBI:CHEBI:138222;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53529;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-dihexanoyl-
CC sn-glycero-3-phosphocholine = 1-heptanoyl-2-hexanoyl-sn-glycero-3-
CC phosphocholine + 1-hexanoyl-2-heptanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:54484, ChEBI:CHEBI:138194, ChEBI:CHEBI:138195,
CC ChEBI:CHEBI:138197, ChEBI:CHEBI:138198;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54485;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine = 1-heptanoyl-2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-2-
CC heptanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54488,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:138195, ChEBI:CHEBI:138199,
CC ChEBI:CHEBI:138200; Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54489;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diheptanoyl-sn-glycero-3-phosphocholine + 1,2-dihexanoyl-
CC sn-glycero-3-phosphoethanolamine = 1-heptanoyl-2-hexanoyl-sn-glycero-
CC 3-phosphoethanolamine + 1-hexanoyl-2-heptanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:54492, ChEBI:CHEBI:138195,
CC ChEBI:CHEBI:138197, ChEBI:CHEBI:138216, ChEBI:CHEBI:138217;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54493;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-
CC acyl-sn-glycero-3-phosphocholine + H(+) + hexanoate;
CC Xref=Rhea:RHEA:53496, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57875, ChEBI:CHEBI:137403;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53497;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + 2-heptanoyl-
CC sn-glycero-3-phosphocholine = 1-hexanoyl-2-heptanoyl-sn-glycero-3-
CC phosphocholine + hexanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:54544, ChEBI:CHEBI:138197, ChEBI:CHEBI:138216,
CC ChEBI:CHEBI:138266, ChEBI:CHEBI:138267;
CC Evidence={ECO:0000269|PubMed:22605381};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54545;
CC Evidence={ECO:0000269|PubMed:22605381};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=300 uM for dipalmitoyl-PC {ECO:0000269|PubMed:19615464};
CC Vmax=670 nmol/min/mg enzyme with dipalmitoyl-PC as substrate
CC {ECO:0000269|PubMed:19615464};
CC Vmax=122 nmol/min/mg enzyme with dipalmitoyl-PE as substrate
CC {ECO:0000269|PubMed:19615464};
CC Vmax=103 nmol/min/mg enzyme using dipalmitoyl-PC as an acyl donor and
CC PE as an acyl acceptor {ECO:0000269|PubMed:19615464};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:19615464};
CC -!- INTERACTION:
CC Q9NWW9; Q12797-6: ASPH; NbExp=3; IntAct=EBI-12253270, EBI-12092171;
CC Q9NWW9; P37235: HPCAL1; NbExp=3; IntAct=EBI-12253270, EBI-749311;
CC Q9NWW9; P61601: NCALD; NbExp=3; IntAct=EBI-12253270, EBI-749635;
CC Q9NWW9; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-12253270, EBI-749370;
CC Q9NWW9; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12253270, EBI-741480;
CC Q9NWW9; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-12253270, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18163183}. Membrane
CC {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC Note=Exhibits a granular pattern in the cytoplasm with preferential
CC perinuclear localization. {ECO:0000269|PubMed:18163183}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine testis
CC and colon (PubMed:19615464). Undetectable in testis, placenta, salivary
CC gland and fetal brain (PubMed:18163183). {ECO:0000269|PubMed:18163183,
CC ECO:0000269|PubMed:19615464}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AB453251; BAH22445.1; -; mRNA.
DR EMBL; AK000563; BAA91256.1; -; mRNA.
DR EMBL; CH471076; EAW74157.1; -; Genomic_DNA.
DR CCDS; CCDS8046.1; -.
DR RefSeq; NP_060348.1; NM_017878.1.
DR PDB; 4DPZ; X-ray; 1.25 A; X=1-129.
DR PDBsum; 4DPZ; -.
DR AlphaFoldDB; Q9NWW9; -.
DR SMR; Q9NWW9; -.
DR BioGRID; 120315; 17.
DR IntAct; Q9NWW9; 6.
DR STRING; 9606.ENSP00000255695; -.
DR BindingDB; Q9NWW9; -.
DR ChEMBL; CHEMBL4630860; -.
DR SwissLipids; SLP:000001075; -.
DR iPTMnet; Q9NWW9; -.
DR PhosphoSitePlus; Q9NWW9; -.
DR BioMuta; HRASLS2; -.
DR DMDM; 23396611; -.
DR MassIVE; Q9NWW9; -.
DR PaxDb; Q9NWW9; -.
DR PeptideAtlas; Q9NWW9; -.
DR PRIDE; Q9NWW9; -.
DR ProteomicsDB; 82995; -.
DR Antibodypedia; 28975; 94 antibodies from 25 providers.
DR DNASU; 54979; -.
DR Ensembl; ENST00000255695.2; ENSP00000255695.1; ENSG00000133328.4.
DR GeneID; 54979; -.
DR KEGG; hsa:54979; -.
DR MANE-Select; ENST00000255695.2; ENSP00000255695.1; NM_017878.2; NP_060348.1.
DR UCSC; uc001nxg.1; human.
DR CTD; 54979; -.
DR DisGeNET; 54979; -.
DR GeneCards; PLAAT2; -.
DR HGNC; HGNC:17824; PLAAT2.
DR HPA; ENSG00000133328; Tissue enriched (intestine).
DR MIM; 613866; gene.
DR neXtProt; NX_Q9NWW9; -.
DR OpenTargets; ENSG00000133328; -.
DR VEuPathDB; HostDB:ENSG00000133328; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR GeneTree; ENSGT00940000154853; -.
DR HOGENOM; CLU_109418_0_1_1; -.
DR InParanoid; Q9NWW9; -.
DR OMA; RQVQKAG; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q9NWW9; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:ENSG00000133328-MON; -.
DR BRENDA; 2.7.1.22; 2681.
DR PathwayCommons; Q9NWW9; -.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q9NWW9; -.
DR BioGRID-ORCS; 54979; 14 hits in 1068 CRISPR screens.
DR GenomeRNAi; 54979; -.
DR Pharos; Q9NWW9; Tchem.
DR PRO; PR:Q9NWW9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NWW9; protein.
DR Bgee; ENSG00000133328; Expressed in duodenum and 148 other tissues.
DR Genevisible; Q9NWW9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; TAS:Reactome.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR DisProt; DP02737; -.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..162
FT /note="Phospholipase A and acyltransferase 2"
FT /id="PRO_0000152483"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..162
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 13..129
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:22605381"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:22605381"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283,
FT ECO:0000269|PubMed:22605381"
FT MUTAGEN 113
FT /note="C->S: Loss of N-acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22825852"
SQ SEQUENCE 162 AA; 17394 MW; BF89C10698D4F1D7 CRC64;
MALARPRPRL GDLIEISRFG YAHWAIYVGD GYVVHLAPAS EIAGAGAASV LSALTNKAIV
KKELLSVVAG GDNYRVNNKH DDRYTPLPSN KIVKRAEELV GQELPYSLTS DNCEHFVNHL
RYGVSRSDQV TGAVTTVGVA AGLLAAASLV GILLARSKRE RQ
