PLAT5_MOUSE
ID PLAT5_MOUSE Reviewed; 270 AA.
AC Q9CPX5; Q6P8Y6; Q9CVQ2; Q9CVS0;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phospholipase A and acyltransferase 5 {ECO:0000250|UniProtKB:Q96KN8};
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};
DE EC=3.1.1.32 {ECO:0000269|PubMed:19000777};
DE EC=3.1.1.4 {ECO:0000269|PubMed:19000777};
DE AltName: Full=H-rev107-like protein 5;
DE AltName: Full=HRAS-like suppressor 5 {ECO:0000312|MGI:MGI:1913977};
DE Short=HRSL5;
GN Name=Plaat5 {ECO:0000312|MGI:MGI:1913977};
GN Synonyms=Hrasls5 {ECO:0000312|MGI:MGI:1913977}, Hrlp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (ISOFORM 4), TISSUE
RP SPECIFICITY (ISOFORM 4), AND CATALYTIC ACTIVITY (ISOFORM 4).
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 4).
RA Okamoto Y., Jin X., Ueda N.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2)
CC activity, catalyzing the calcium-independent release of fatty acids
CC from the sn-1 or sn-2 position of glycerophospholipids (By similarity).
CC Shows N-acyltransferase activity, catalyzing the calcium-independent
CC transfer of a fatty acyl group at the sn-1 position of
CC phosphatidylcholine (PC) and other glycerophospholipids to the primary
CC amine of phosphatidylethanolamine (PE), forming N-
CC acylphosphatidylethanolamine (NAPE), which serves as precursor for N-
CC acylethanolamines (NAEs) (PubMed:19000777).
CC {ECO:0000250|UniProtKB:Q96KN8, ECO:0000269|PubMed:19000777}.
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};
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};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45177;
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 = 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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173;
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 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q4KLN5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9CPX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CPX5-2; Sequence=VSP_007450;
CC Name=3;
CC IsoId=Q9CPX5-3; Sequence=VSP_044623, VSP_007448, VSP_007449;
CC Name=4;
CC IsoId=Q9CPX5-4; Sequence=VSP_044623;
CC -!- TISSUE SPECIFICITY: Isoform 4 shows highest expression level in testis.
CC {ECO:0000269|PubMed:19000777}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AB447517; BAH11080.1; -; mRNA.
DR EMBL; AB261168; BAF41149.1; -; mRNA.
DR EMBL; AK006527; BAB24636.2; -; mRNA.
DR EMBL; AK006790; BAB24741.1; -; mRNA.
DR EMBL; AK007015; BAB24828.1; -; mRNA.
DR EMBL; AK014971; BAB29646.1; -; mRNA.
DR EMBL; AC109225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466612; EDL33320.1; -; Genomic_DNA.
DR EMBL; BC061008; AAH61008.1; -; mRNA.
DR CCDS; CCDS29530.1; -. [Q9CPX5-1]
DR RefSeq; NP_080007.1; NM_025731.2. [Q9CPX5-1]
DR AlphaFoldDB; Q9CPX5; -.
DR SMR; Q9CPX5; -.
DR STRING; 10090.ENSMUSP00000025929; -.
DR SwissLipids; SLP:000001127; -. [Q9CPX5-4]
DR iPTMnet; Q9CPX5; -.
DR PaxDb; Q9CPX5; -.
DR PRIDE; Q9CPX5; -.
DR ProteomicsDB; 267159; -. [Q9CPX5-1]
DR ProteomicsDB; 267160; -. [Q9CPX5-2]
DR ProteomicsDB; 267161; -. [Q9CPX5-3]
DR ProteomicsDB; 267162; -. [Q9CPX5-4]
DR Antibodypedia; 43875; 87 antibodies from 18 providers.
DR Ensembl; ENSMUST00000025929; ENSMUSP00000025929; ENSMUSG00000024973. [Q9CPX5-1]
DR Ensembl; ENSMUST00000239394; ENSMUSP00000159309; ENSMUSG00000024973. [Q9CPX5-4]
DR GeneID; 66727; -.
DR KEGG; mmu:66727; -.
DR UCSC; uc008glm.1; mouse. [Q9CPX5-3]
DR UCSC; uc008gln.1; mouse. [Q9CPX5-4]
DR CTD; 117245; -.
DR MGI; MGI:1913977; Plaat5.
DR VEuPathDB; HostDB:ENSMUSG00000024973; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR GeneTree; ENSGT00940000162436; -.
DR HOGENOM; CLU_070482_0_0_1; -.
DR InParanoid; Q9CPX5; -.
DR OMA; QRAEWSS; -.
DR OrthoDB; 1602481at2759; -.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR BioGRID-ORCS; 66727; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9CPX5; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CPX5; protein.
DR Bgee; ENSMUSG00000024973; Expressed in seminiferous tubule of testis and 24 other tissues.
DR ExpressionAtlas; Q9CPX5; baseline and differential.
DR Genevisible; Q9CPX5; MM.
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:MGI.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:MGI.
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..270
FT /note="Phospholipase A and acyltransferase 5"
FT /id="PRO_0000152489"
FT DOMAIN 127..240
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 224
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT VAR_SEQ 1
FT /note="M -> MIPGLGGPWSAPPCRRVVPAGPSGM (in isoform 4 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:19000777,
FT ECO:0000303|Ref.2"
FT /id="VSP_044623"
FT VAR_SEQ 118..151
FT /note="GNPRPRPGDLIEIFRIGYEHWAIYVEDDCVVHLA -> VRIPGIHRMSVLVS
FT WSLLTASCFTLRLINICTDM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007448"
FT VAR_SEQ 152..270
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007449"
FT VAR_SEQ 242..270
FT /note="EHALVEGAKAAGAVLSAVVDSIRPKPITA -> YFVELGNHRKHSENLLRTF
FT PVMKNSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007450"
FT CONFLICT 21
FT /note="P -> S (in Ref. 3; BAB24741)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="L -> Q (in Ref. 3; BAB24741)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29866 MW; 158034CF485288F7 CRC64;
MGLSPAASGE FGIRLSRVPW PRPTQISKTS STESSDTQSA TGQSTVPHSD SASSQALLVQ
FLPKQLKQDR RLEQARSFQQ GEKPETSLEL TPSKKRTELI PTSNSEIEST QKNQAVEGNP
RPRPGDLIEI FRIGYEHWAI YVEDDCVVHL APPSEFEAGS ITSIFSNRAV VKYSRLEDVL
HGCSWKINNK LDGTYLPLPV DKIMQRTKNM INKIVQYSLI EGNCEHFVND LRYGVPRSQQ
VEHALVEGAK AAGAVLSAVV DSIRPKPITA
