PLAT5_HUMAN
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 03-AUG-2022, entry version 134.
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 PRIDE; Q96KN8; -.
DR ProteomicsDB; 24961; -.
DR ProteomicsDB; 26717; -.
DR ProteomicsDB; 77095; -. [Q96KN8-1]
DR Antibodypedia; 43875; 87 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 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; 1602481at2759; -.
DR PhylomeDB; Q96KN8; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:ENSG00000168004-MON; -.
DR PathwayCommons; Q96KN8; -.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q96KN8; -.
DR BioGRID-ORCS; 117245; 15 hits in 1070 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 InterPro; IPR007053; LRAT_dom.
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
