ID   PLAT4_HUMAN             Reviewed;         164 AA.
AC   Q9UL19; B2R599; B4DDW2; E7ENZ7; O95200;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Phospholipase A and acyltransferase 4 {ECO:0000312|HGNC:HGNC:9869};
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 4;
DE            Short=HRSL4;
DE   AltName: Full=RAR-responsive protein TIG3;
DE   AltName: Full=Retinoic acid receptor responder protein 3;
DE   AltName: Full=Retinoid-inducible gene 1 protein;
DE   AltName: Full=Tazarotene-induced gene 3 protein;
GN   Name=PLAAT4 {ECO:0000312|HGNC:HGNC:9869};
GN   Synonyms=RARRES3, RIG1, TIG3;
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] (ISOFORM 1).
RC   TISSUE=Keratinocyte;
RX   PubMed=9843971; DOI=10.1073/pnas.95.25.14811;
RA   DiSepio D., Ghosn C., Eckert R.L., Deucher A., Robinson N., Duvic M.,
RA   Chandraratna R.A.S., Nagpal S.;
RT   "Identification and characterization of a retinoid-induced class II tumor
RT   suppressor/growth regulatory gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14811-14815(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Stomach cancer;
RX   PubMed=10687848; DOI=10.1016/s0303-7207(99)00207-5;
RA   Huang S.L., Shyu R.Y., Yeh M.Y., Jiang S.Y.;
RT   "Cloning and characterization of a novel retinoid-inducible gene 1(RIG1)
RT   deriving from human gastric cancer cells.";
RL   Mol. Cell. Endocrinol. 159:15-24(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Gastric adenocarcinoma;
RA   Kato S.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Spleen, and Urinary bladder;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TGM1.
RX   PubMed=17762858; DOI=10.1038/sj.jid.5701035;
RA   Jans R., Sturniolo M.T., Eckert R.L.;
RT   "Localization of the TIG3 transglutaminase interaction domain and
RT   demonstration that the amino-terminal region is required for TIG3 function
RT   as a keratinocyte differentiation regulator.";
RL   J. Invest. Dermatol. 128:517-529(2008).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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   [12]
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).
CC   -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC       activities (PubMed:19615464, PubMed:22605381, PubMed:22825852,
CC       PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2),
CC       catalyzing the calcium-independent release of fatty acids from the sn-1
CC       or sn-2 position of glycerophospholipids (PubMed:19615464,
CC       PubMed:22605381, PubMed:22825852). 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:22605381,
CC       PubMed:22825852). Promotes keratinocyte differentiation via activation
CC       of TGM1 (PubMed:17762858). {ECO:0000269|PubMed:17762858,
CC       ECO:0000269|PubMed:19615464, ECO:0000269|PubMed:22605381,
CC       ECO:0000269|PubMed:22825852, 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=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 = 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-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-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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=400 uM for dipalmitoyl-PC {ECO:0000269|PubMed:19615464};
CC         Vmax=530 nmol/min/mg enzyme with dipalmitoyl-PC as substrate
CC         {ECO:0000269|PubMed:19615464};
CC         Vmax=240 nmol/min/mg enzyme with dipalmitoyl-PE as substrate
CC         {ECO:0000269|PubMed:19615464};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:19615464};
CC   -!- SUBUNIT: Interacts with TGM1. {ECO:0000269|PubMed:17762858}.
CC   -!- INTERACTION:
CC       Q9UL19; Q92569: PIK3R3; NbExp=3; IntAct=EBI-10323452, EBI-79893;
CC       Q9UL19; O43765: SGTA; NbExp=4; IntAct=EBI-10323452, EBI-347996;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17762858}; Single-
CC       pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UL19-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UL19-2; Sequence=VSP_041496;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10687848,
CC       ECO:0000269|PubMed:19615464}.
CC   -!- INDUCTION: By all-trans-retinoic acid and synthetic retinoids.
CC       {ECO:0000269|PubMed:10687848}.
CC   -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42051/RARRES3";
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DR   EMBL; AF060228; AAC84000.1; -; mRNA.
DR   EMBL; AF092922; AAF02294.1; -; mRNA.
DR   EMBL; AB453252; BAH22446.1; -; mRNA.
DR   EMBL; AB030815; BAB08109.1; -; mRNA.
DR   EMBL; AK293357; BAG56873.1; -; mRNA.
DR   EMBL; AK312110; BAG35046.1; -; mRNA.
DR   EMBL; AP001591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74156.1; -; Genomic_DNA.
DR   EMBL; BC009678; AAH09678.1; -; mRNA.
DR   CCDS; CCDS41662.1; -. [Q9UL19-1]
DR   RefSeq; NP_004576.2; NM_004585.4. [Q9UL19-1]
DR   PDB; 2LKT; NMR; -; A=1-125.
DR   PDB; 2MY9; NMR; -; A=1-125.
DR   PDB; 7ZOT; X-ray; 1.74 A; A/B=1-123.
DR   PDBsum; 2LKT; -.
DR   PDBsum; 2MY9; -.
DR   PDBsum; 7ZOT; -.
DR   AlphaFoldDB; Q9UL19; -.
DR   BMRB; Q9UL19; -.
DR   SASBDB; Q9UL19; -.
DR   SMR; Q9UL19; -.
DR   BioGRID; 111855; 26.
DR   IntAct; Q9UL19; 2.
DR   STRING; 9606.ENSP00000255688; -.
DR   BindingDB; Q9UL19; -.
DR   ChEMBL; CHEMBL4630864; -.
DR   SwissLipids; SLP:000001076; -.
DR   iPTMnet; Q9UL19; -.
DR   PhosphoSitePlus; Q9UL19; -.
DR   BioMuta; RARRES3; -.
DR   DMDM; 20140910; -.
DR   MassIVE; Q9UL19; -.
DR   PaxDb; 9606-ENSP00000255688; -.
DR   PeptideAtlas; Q9UL19; -.
DR   ProteomicsDB; 84932; -. [Q9UL19-1]
DR   ProteomicsDB; 84933; -. [Q9UL19-2]
DR   Antibodypedia; 2443; 267 antibodies from 35 providers.
DR   DNASU; 5920; -.
DR   Ensembl; ENST00000255688.8; ENSP00000255688.3; ENSG00000133321.11. [Q9UL19-1]
DR   Ensembl; ENST00000439013.6; ENSP00000402943.2; ENSG00000133321.11. [Q9UL19-2]
DR   GeneID; 5920; -.
DR   KEGG; hsa:5920; -.
DR   MANE-Select; ENST00000255688.8; ENSP00000255688.3; NM_004585.5; NP_004576.2.
DR   UCSC; uc001nxf.5; human. [Q9UL19-1]
DR   AGR; HGNC:9869; -.
DR   CTD; 5920; -.
DR   DisGeNET; 5920; -.
DR   GeneCards; PLAAT4; -.
DR   HGNC; HGNC:9869; PLAAT4.
DR   HPA; ENSG00000133321; Low tissue specificity.
DR   MIM; 605092; gene.
DR   neXtProt; NX_Q9UL19; -.
DR   OpenTargets; ENSG00000133321; -.
DR   VEuPathDB; HostDB:ENSG00000133321; -.
DR   eggNOG; ENOG502S0JN; Eukaryota.
DR   GeneTree; ENSGT00940000162878; -.
DR   HOGENOM; CLU_109418_0_1_1; -.
DR   InParanoid; Q9UL19; -.
DR   OrthoDB; 3059772at2759; -.
DR   PhylomeDB; Q9UL19; -.
DR   TreeFam; TF330836; -.
DR   BioCyc; MetaCyc:ENSG00000133321-MONOMER; -.
DR   PathwayCommons; Q9UL19; -.
DR   Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR   SignaLink; Q9UL19; -.
DR   BioGRID-ORCS; 5920; 17 hits in 1153 CRISPR screens.
DR   ChiTaRS; RARRES3; human.
DR   GeneWiki; RARRES3; -.
DR   GenomeRNAi; 5920; -.
DR   Pharos; Q9UL19; Tchem.
DR   PRO; PR:Q9UL19; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9UL19; Protein.
DR   Bgee; ENSG00000133321; Expressed in granulocyte and 198 other cell types or tissues.
DR   ExpressionAtlas; Q9UL19; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0150074; P:positive regulation of protein-glutamine gamma-glutamyltransferase activity; IMP:UniProtKB.
DR   Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR   InterPro; IPR007053; LRAT_dom.
DR   PANTHER; PTHR13943; HRAS-LIKE SUPPRESSOR - RELATED; 1.
DR   PANTHER; PTHR13943:SF36; PHOSPHOLIPASE A AND ACYLTRANSFERASE 4; 1.
DR   Pfam; PF04970; LRAT; 1.
DR   PROSITE; PS51934; LRAT; 1.
DR   Genevisible; Q9UL19; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..164
FT                   /note="Phospholipase A and acyltransferase 4"
FT                   /id="PRO_0000152490"
FT   TOPO_DOM        1..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..164
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          13..129
FT                   /note="LRAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   REGION          1..40
FT                   /note="Essential for its ability regulate keratinocyte
FT                   differentiation"
FT                   /evidence="ECO:0000269|PubMed:17762858"
FT   REGION          124..164
FT                   /note="Interaction with TGM1"
FT                   /evidence="ECO:0000269|PubMed:17762858"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        113
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   VAR_SEQ         131..164
FT                   /note="EKAKVEVGVATALGILVVAGCSFAIRRYQKKATA -> RTSLDNPSPSAWGW
FT                   THGAVQPGDHCE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041496"
FT   VARIANT         69
FT                   /note="V -> L (in dbSNP:rs35502888)"
FT                   /id="VAR_049480"
FT   VARIANT         162
FT                   /note="A -> V (in dbSNP:rs35845275)"
FT                   /id="VAR_049481"
FT   CONFLICT        44
FT                   /note="G -> R (in Ref. 5; BAG56873)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="E -> G (in Ref. 1; AAC84000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="T -> A (in Ref. 1; AAC84000)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:2LKT"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   STRAND          19..29
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:2MY9"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:2LKT"
FT   TURN            53..56
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   HELIX           65..69
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:7ZOT"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:7ZOT"
SQ   SEQUENCE   164 AA;  18179 MW;  95625B8FD375FD38 CRC64;
     MASPHQEPKP GDLIEIFRLG YEHWALYIGD GYVIHLAPPS EYPGAGSSSV FSVLSNSAEV
     KRERLEDVVG GCCYRVNNSL DHEYQPRPVE VIISSAKEMV GQKMKYSIVS RNCEHFVTQL
     RYGKSRCKQV EKAKVEVGVA TALGILVVAG CSFAIRRYQK KATA
//