NAPES_ARATH
ID NAPES_ARATH Reviewed; 284 AA.
AC Q9ZV87; Q94AQ5;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=N-acylphosphatidylethanolamine synthase;
DE Short=NAPE synthase;
DE EC=2.3.1.-;
DE AltName: Full=Lysoglycerophospholipid acyltransferase;
DE AltName: Full=Monolysocardiolipin acyltransferase;
GN OrderedLocusNames=At1g78690; ORFNames=F9K20.27;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19447891; DOI=10.1074/jbc.m109.005744;
RA Faure L., Coulon D., Laroche-Traineau J., Le Guedard M., Schmitter J.-M.,
RA Testet E., Lessire R., Bessoule J.-J.;
RT "Discovery and characterization of an Arabidopsis thaliana N-
RT acylphosphatidylethanolamine synthase.";
RL J. Biol. Chem. 284:18734-18741(2009).
RN [5]
RP FUNCTION.
RX PubMed=21803774; DOI=10.1074/jbc.m111.269779;
RA Bulat E., Garrett T.A.;
RT "Putative N-acylphosphatidylethanolamine synthase from Arabidopsis thaliana
RT is a lysoglycerophospholipid acyltransferase.";
RL J. Biol. Chem. 286:33819-33831(2011).
CC -!- FUNCTION: Acyltransferase that catalyzes the N-acylation of
CC phosphatidylethanolamine to form N-acylphosphatidylethanolamine (N-
CC acyl-PE) (e.g. NAPEs containing C16:0, C16:1, C18:0, and C18:1).
CC Mediates also the formation of acylphosphatidylglycerol (acyl-PG) from
CC lysoglycerophospholipid by O-acylation. Uses acyl-CoA as acyl donors.
CC Acylates 1-acyllysophosphatidylethanolamine (1-acyllyso-PE) and 1-
CC acyllysophosphatidylglycerol (1-acyllyso-PG) at the sn-2-position.
CC {ECO:0000269|PubMed:19447891, ECO:0000269|PubMed:21803774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19447891};
CC Single-pass membrane protein {ECO:0000269|PubMed:19447891}.
CC -!- TISSUE SPECIFICITY: Essentially present in young tissues. Expressed in
CC roots, cotyledons, leaves, and shoot and root apical meristems.
CC {ECO:0000269|PubMed:19447891}.
CC -!- DEVELOPMENTAL STAGE: In imbibed seeds, accumulates in cotyledons and
CC hypocotyls. In flowers, expressed in the filament of stamens, in the
CC style, and in ovary with eggs of pistil. {ECO:0000269|PubMed:19447891}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphocholine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the taffazin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK76548.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC005679; AAC83040.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36139.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60153.1; -; Genomic_DNA.
DR EMBL; AY045874; AAK76548.1; ALT_FRAME; mRNA.
DR PIR; G96815; G96815.
DR RefSeq; NP_001322457.1; NM_001334840.1.
DR RefSeq; NP_177990.1; NM_106516.3.
DR AlphaFoldDB; Q9ZV87; -.
DR STRING; 3702.AT1G78690.1; -.
DR PaxDb; Q9ZV87; -.
DR PRIDE; Q9ZV87; -.
DR EnsemblPlants; AT1G78690.1; AT1G78690.1; AT1G78690.
DR EnsemblPlants; AT1G78690.5; AT1G78690.5; AT1G78690.
DR GeneID; 844205; -.
DR Gramene; AT1G78690.1; AT1G78690.1; AT1G78690.
DR Gramene; AT1G78690.5; AT1G78690.5; AT1G78690.
DR KEGG; ath:AT1G78690; -.
DR Araport; AT1G78690; -.
DR TAIR; locus:2037538; AT1G78690.
DR eggNOG; KOG2847; Eukaryota.
DR HOGENOM; CLU_046747_2_0_1; -.
DR InParanoid; Q9ZV87; -.
DR OMA; GWPSIMP; -.
DR OrthoDB; 589285at2759; -.
DR PhylomeDB; Q9ZV87; -.
DR BRENDA; 2.3.1.23; 399.
DR PRO; PR:Q9ZV87; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZV87; baseline and differential.
DR Genevisible; Q9ZV87; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:TAIR.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497; PTHR12497; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR SMART; SM00563; PlsC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cell membrane; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..284
FT /note="N-acylphosphatidylethanolamine synthase"
FT /id="PRO_0000420700"
FT TRANSMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 122..163
FT /note="Hydrophilic"
FT /evidence="ECO:0000250"
FT MOTIF 67..72
FT /note="HXXXXD motif"
SQ SEQUENCE 284 AA; 31743 MW; BFC195F8F549B0B1 CRC64;
MGKIMEWAAR SDHLGGIPRN TVIMAVSAFA KAVANLCNKS SVHNADTLMN LVQSRPPGVP
LITVSNHMST LDDPVMWGAF KGLLSLDPEL ARWVLAAEDI CFRNPIFSYI FRTGKCIPIT
RGGGIYQENM NEALQRLKDG SWLHTFPEGK VFQDDVPIRR LKWGTASLIA RSPVTPIVLP
IIHRGFEEMM PENYNNGRRP LVPLPNKHLK VVVGEPIEFD VPMMVETAVL DSRHVTPPLQ
EVKWPVLTSA GQVLDETAQR HLYIALSEKI QSSLETLRLL AKRL
