PLAT4_HUMAN
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 03-AUG-2022, entry version 154.
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}; 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="http://atlasgeneticsoncology.org/Genes/RARRES3ID42051ch11q12.html";
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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 PDBsum; 2LKT; -.
DR PDBsum; 2MY9; -.
DR AlphaFoldDB; Q9UL19; -.
DR BMRB; 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; Q9UL19; -.
DR PeptideAtlas; Q9UL19; -.
DR PRIDE; Q9UL19; -.
DR ProteomicsDB; 84932; -. [Q9UL19-1]
DR ProteomicsDB; 84933; -. [Q9UL19-2]
DR Antibodypedia; 2443; 240 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 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; 1602481at2759; -.
DR PhylomeDB; Q9UL19; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:ENSG00000133321-MON; -.
DR PathwayCommons; Q9UL19; -.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q9UL19; -.
DR BioGRID-ORCS; 5920; 17 hits in 1079 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 196 other tissues.
DR ExpressionAtlas; Q9UL19; baseline and differential.
DR Genevisible; Q9UL19; 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: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 InterPro; IPR007053; LRAT_dom.
DR InterPro; IPR033210; PLAAT4.
DR PANTHER; PTHR13943:SF36; PTHR13943:SF36; 1.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
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:2LKT"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2LKT"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:2LKT"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2LKT"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2MY9"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2LKT"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2LKT"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2LKT"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2LKT"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2LKT"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2LKT"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:2LKT"
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
