PLAT5_RAT
ID PLAT5_RAT Reviewed; 287 AA.
AC Q4KLN5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phospholipase A and acyltransferase 5 {ECO:0000305};
DE AltName: Full=Ca(2+)-independent N-acyltransferase;
DE Short=iNAT;
DE EC=2.3.1.- {ECO:0000269|PubMed:17158102};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:Q9CPX5};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q9CPX5};
DE AltName: Full=H-rev107-like protein 5;
DE AltName: Full=HRAS-like suppressor 5;
DE Short=HRSL5;
DE AltName: Full=Rat LRAT-like protein-1 {ECO:0000303|PubMed:17158102};
DE Short=RLP-1 {ECO:0000303|PubMed:17158102};
GN Name=Plaat5 {ECO:0000312|RGD:1308376};
GN Synonyms=Hrasls5 {ECO:0000312|EMBL:AAH99084.1, ECO:0000312|RGD:1308376},
GN Hrlp5, Rlp-1 {ECO:0000303|PubMed:17158102};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAH99084.1};
RN [1] {ECO:0000312|EMBL:BAF41148.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17158102; DOI=10.1074/jbc.m606369200;
RA Jin X.H., Okamoto Y., Morishita J., Tsuboi K., Tonai T., Ueda N.;
RT "Discovery and characterization of a Ca2+-independent
RT phosphatidylethanolamine N-acyltransferase generating the anandamide
RT precursor and its congeners.";
RL J. Biol. Chem. 282:3614-3623(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000312|EMBL:AAH99084.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH99084.1};
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:17158102).
CC {ECO:0000250|UniProtKB:Q96KN8, ECO:0000250|UniProtKB:Q9CPX5,
CC ECO:0000269|PubMed:17158102}.
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:0000250|UniProtKB:Q9CPX5};
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:0000250|UniProtKB:Q9CPX5};
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:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45477;
CC Evidence={ECO:0000305|PubMed:17158102};
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:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45177;
CC Evidence={ECO:0000305|PubMed:17158102};
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:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45173;
CC Evidence={ECO:0000305|PubMed:17158102};
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:0000250|UniProtKB:Q9CPX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45193;
CC Evidence={ECO:0000250|UniProtKB:Q9CPX5};
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:0000250|UniProtKB:Q9CPX5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45189;
CC Evidence={ECO:0000250|UniProtKB:Q9CPX5};
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:0000269|PubMed:17158102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56505;
CC Evidence={ECO:0000305|PubMed:17158102};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:17158102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17158102}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:17158102}.
CC -!- SIMILARITY: Belongs to the H-rev107 family. {ECO:0000305}.
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DR EMBL; AB255646; BAF41148.1; -; mRNA.
DR EMBL; AABR07006120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099084; AAH99084.1; -; mRNA.
DR RefSeq; NP_001034096.1; NM_001039007.1.
DR AlphaFoldDB; Q4KLN5; -.
DR SMR; Q4KLN5; -.
DR STRING; 10116.ENSRNOP00000037070; -.
DR SwissLipids; SLP:000001909; -.
DR PaxDb; Q4KLN5; -.
DR PRIDE; Q4KLN5; -.
DR GeneID; 293711; -.
DR KEGG; rno:293711; -.
DR UCSC; RGD:1308376; rat.
DR CTD; 117245; -.
DR RGD; 1308376; Plaat5.
DR VEuPathDB; HostDB:ENSRNOG00000023528; -.
DR eggNOG; ENOG502S0JN; Eukaryota.
DR HOGENOM; CLU_070482_0_0_1; -.
DR InParanoid; Q4KLN5; -.
DR OMA; QRAEWSS; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q4KLN5; -.
DR TreeFam; TF330836; -.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR PRO; PR:Q4KLN5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000023528; Expressed in testis and 12 other tissues.
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; ISO:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:RGD.
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; Cytoplasm; Hydrolase; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..287
FT /note="Phospholipase A and acyltransferase 5"
FT /id="PRO_0000450339"
FT DOMAIN 144..257
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 241
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
SQ SEQUENCE 287 AA; 31749 MW; 1F9FA50E46163148 CRC64;
MIPGHRGPWS APLCRRLVPA GHSGMGLSPA ASGEYGIRLF RVPWPSRPKQ ISRTASTESS
DTQPTNDSAS SQALVVQFLP KLPKQDRGLE QARSLRQGQK PEINLELIPS KKRTEMIPSS
DSEIEGNLKN QAAESNQKPR PGDLIEIFRI GYEHWAIYVE DDCVVHLAPP SEFEAGSITS
IFSNRAVVKY SRLQDVLHGC SWKINNKLDG TYLPLPVDKI IQRTKNMINK IVQYSLIEGN
CEHFVNDLRY GVPRSQQVEH VLVEGAKAAG AVLSAVVDSI RPKPITA
