ID   PLAT5_HUMAN             Reviewed;         279 AA.
AC   Q96KN8; B7X6T1; F5GZ87; F5H4Y9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   13-SEP-2023, entry version 139.
DE   RecName: Full=Phospholipase A and acyltransferase 5 {ECO:0000312|HGNC:HGNC:24978};
DE   AltName: Full=Ca(2+)-independent N-acyltransferase {ECO:0000303|PubMed:19000777};
DE            Short=iNAT {ECO:0000303|PubMed:19000777};
DE            EC=2.3.1.- {ECO:0000269|PubMed:19000777, ECO:0000269|PubMed:22825852};
DE            EC=3.1.1.32 {ECO:0000269|PubMed:19000777, ECO:0000269|PubMed:22825852};
DE            EC=3.1.1.4 {ECO:0000269|PubMed:19000777, ECO:0000269|PubMed:22825852};
DE   AltName: Full=H-rev107-like protein 5;
DE   AltName: Full=HRAS-like suppressor 5;
DE            Short=HRSL5;
GN   Name=PLAAT5 {ECO:0000312|HGNC:HGNC:24978}; Synonyms=HRASLS5, HRLP5;
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), VARIANT GLY-31, FUNCTION (ISOFORM
RP   1), AND CATALYTIC ACTIVITY (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=19000777; DOI=10.1016/j.bbalip.2008.09.006;
RA   Jin X.-H., Uyama T., Wang J., Okamoto Y., Tonai T., Ueda N.;
RT   "cDNA cloning and characterization of human and mouse Ca(2+)-independent
RT   phosphatidylethanolamine N-acyltransferases.";
RL   Biochim. Biophys. Acta 1791:32-38(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-31.
RA   Hughes P.J., Stanway G.;
RT   "Identification of a novel member of the H-rev107 protein family.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-31.
RA   Mural R.J., Istrail S., Sutton 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   [5]
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   [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).
CC   -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC       activities (PubMed:22825852, PubMed:26503625). Shows phospholipase A1
CC       (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent
CC       release of fatty acids from the sn-1 or sn-2 position of
CC       glycerophospholipids (PubMed:22825852). Shows N-acyltransferase
CC       activity, catalyzing the calcium-independent transfer of a fatty acyl
CC       group at the sn-1 position of phosphatidylcholine (PC) and other
CC       glycerophospholipids to the primary amine of phosphatidylethanolamine
CC       (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as
CC       precursor for N-acylethanolamines (NAEs) (PubMed:19000777,
CC       PubMed:22825852). {ECO:0000269|PubMed:19000777,
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:19000777, ECO:0000269|PubMed:22825852};
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:19000777, ECO:0000269|PubMed:22825852};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1-
CC         hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC         phosphocholine = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) +
CC         N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-octadecenoyl)-sn-
CC         glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:45476,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003,
CC         ChEBI:CHEBI:74986, ChEBI:CHEBI:85277;
CC         Evidence={ECO:0000269|PubMed:19000777};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45477;
CC         Evidence={ECO:0000269|PubMed:19000777};
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:19000777, ECO:0000269|PubMed:22825852};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45177;
CC         Evidence={ECO:0000269|PubMed:19000777, ECO:0000269|PubMed:22825852};
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:19000777, ECO:0000269|PubMed:22825852};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173;
CC         Evidence={ECO:0000269|PubMed:19000777, ECO:0000269|PubMed:22825852};
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:19000777};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45193;
CC         Evidence={ECO:0000269|PubMed:19000777};
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:19000777};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45189;
CC         Evidence={ECO:0000269|PubMed:19000777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1-
CC         hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + N,1,2-tri-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:56504,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001,
CC         ChEBI:CHEBI:74986, ChEBI:CHEBI:85291;
CC         Evidence={ECO:0000250|UniProtKB:Q4KLN5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56505;
CC         Evidence={ECO:0000250|UniProtKB:Q4KLN5};
CC   -!- INTERACTION:
CC       Q96KN8-3; Q9BVM4: GGACT; NbExp=8; IntAct=EBI-10290304, EBI-10299852;
CC       Q96KN8-3; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10290304, EBI-618309;
CC       Q96KN8-3; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-10290304, EBI-748420;
CC       Q96KN8-3; Q6ZMS7: ZNF783; NbExp=3; IntAct=EBI-10290304, EBI-10254978;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q4KLN5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96KN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96KN8-2; Sequence=VSP_045826;
CC       Name=3;
CC         IsoId=Q96KN8-3; Sequence=VSP_045825;
CC   -!- TISSUE SPECIFICITY: Highest expression level in testis and pancreas.
CC   -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR   EMBL; AB298804; BAH08633.1; -; mRNA.
DR   EMBL; AJ416558; CAC94942.1; -; mRNA.
DR   EMBL; AP000484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74150.1; -; Genomic_DNA.
DR   CCDS; CCDS53646.1; -. [Q96KN8-3]
DR   CCDS; CCDS53647.1; -. [Q96KN8-2]
DR   CCDS; CCDS8044.1; -. [Q96KN8-1]
DR   RefSeq; NP_473449.1; NM_054108.3. [Q96KN8-1]
DR   AlphaFoldDB; Q96KN8; -.
DR   SMR; Q96KN8; -.
DR   BioGRID; 125580; 7.
DR   IntAct; Q96KN8; 5.
DR   STRING; 9606.ENSP00000301790; -.
DR   BindingDB; Q96KN8; -.
DR   ChEMBL; CHEMBL4630850; -.
DR   SwissLipids; SLP:000001126; -.
DR   iPTMnet; Q96KN8; -.
DR   BioMuta; HRASLS5; -.
DR   DMDM; 296434533; -.
DR   MassIVE; Q96KN8; -.
DR   PaxDb; Q96KN8; -.
DR   PeptideAtlas; Q96KN8; -.
DR   ProteomicsDB; 24961; -.
DR   ProteomicsDB; 26717; -.
DR   ProteomicsDB; 77095; -. [Q96KN8-1]
DR   Antibodypedia; 43875; 109 antibodies from 18 providers.
DR   DNASU; 117245; -.
DR   Ensembl; ENST00000301790.4; ENSP00000301790.4; ENSG00000168004.10. [Q96KN8-1]
DR   Ensembl; ENST00000539221.5; ENSP00000443873.1; ENSG00000168004.10. [Q96KN8-2]
DR   Ensembl; ENST00000540857.6; ENSP00000444809.1; ENSG00000168004.10. [Q96KN8-3]
DR   GeneID; 117245; -.
DR   KEGG; hsa:117245; -.
DR   MANE-Select; ENST00000540857.6; ENSP00000444809.1; NM_001146729.2; NP_001140201.2. [Q96KN8-3]
DR   UCSC; uc001nwy.3; human. [Q96KN8-1]
DR   AGR; HGNC:24978; -.
DR   CTD; 117245; -.
DR   GeneCards; PLAAT5; -.
DR   HGNC; HGNC:24978; PLAAT5.
DR   HPA; ENSG00000168004; Group enriched (adipose tissue, pancreas, testis).
DR   MIM; 611474; gene.
DR   neXtProt; NX_Q96KN8; -.
DR   OpenTargets; ENSG00000168004; -.
DR   VEuPathDB; HostDB:ENSG00000168004; -.
DR   eggNOG; ENOG502S0JN; Eukaryota.
DR   GeneTree; ENSGT00940000162436; -.
DR   HOGENOM; CLU_070482_0_0_1; -.
DR   InParanoid; Q96KN8; -.
DR   OMA; QRAEWSS; -.
DR   OrthoDB; 3059772at2759; -.
DR   PhylomeDB; Q96KN8; -.
DR   TreeFam; TF330836; -.
DR   BioCyc; MetaCyc:ENSG00000168004-MONOMER; -.
DR   PathwayCommons; Q96KN8; -.
DR   Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR   SignaLink; Q96KN8; -.
DR   BioGRID-ORCS; 117245; 19 hits in 1144 CRISPR screens.
DR   ChiTaRS; HRASLS5; human.
DR   GenomeRNAi; 117245; -.
DR   Pharos; Q96KN8; Tchem.
DR   PRO; PR:Q96KN8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q96KN8; Protein.
DR   Bgee; ENSG00000168004; Expressed in sperm and 130 other tissues.
DR   ExpressionAtlas; Q96KN8; baseline and differential.
DR   Genevisible; Q96KN8; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
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:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA: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:SF2; PHOSPHOLIPASE A AND ACYLTRANSFERASE 5; 1.
DR   Pfam; PF04970; LRAT; 1.
DR   PROSITE; PS51934; LRAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Cytoplasm; Hydrolase;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..279
FT                   /note="Phospholipase A and acyltransferase 5"
FT                   /id="PRO_0000152488"
FT   DOMAIN          135..249
FT                   /note="LRAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          70..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   ACT_SITE        233
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT   VAR_SEQ         50..59
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045825"
FT   VAR_SEQ         234..279
FT                   /note="EHFVNGLRYGVPRSQQVEHALMEGAKAAGAVISAVVDSIKPKPITA -> RA
FT                   RPDGRSEGCWSSYFSCSG (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_045826"
FT   VARIANT         31
FT                   /note="S -> G (in dbSNP:rs10897424)"
FT                   /evidence="ECO:0000269|PubMed:19000777, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_049477"
FT   VARIANT         93
FT                   /note="A -> P (in dbSNP:rs940611)"
FT                   /id="VAR_024486"
FT   VARIANT         214
FT                   /note="Q -> R (in dbSNP:rs35735923)"
FT                   /id="VAR_049478"
FT   VARIANT         258
FT                   /note="A -> V (in dbSNP:rs35375575)"
FT                   /id="VAR_049479"
SQ   SEQUENCE   279 AA;  30312 MW;  F388449962CA8E3D CRC64;
     MGLSPGAEGE YALRLPRIPP PLPKPASRTA STGPKDQPPA LRRSAVPHSG LNSISPLELE
     ESVGFAALVQ LPAKQPPPGT LEQGRSIQQG EKAVVSLETT PSQKADWSSI PKPENEGKLI
     KQAAEGKPRP RPGDLIEIFR IGYEHWAIYV EDDCVVHLAP PSEEFEVGSI TSIFSNRAVV
     KYSRLEDVLH GCSWKVNNKL DGTYLPLPVD KIIQRTKKMV NKIVQYSLIE GNCEHFVNGL
     RYGVPRSQQV EHALMEGAKA AGAVISAVVD SIKPKPITA
//