GPAT4_ARATH
ID GPAT4_ARATH Reviewed; 503 AA.
AC Q9LMM0; Q8W4N0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Glycerol-3-phosphate 2-O-acyltransferase 4;
DE Short=AtGPAT4;
DE EC=2.3.1.198;
DE AltName: Full=Glycerol-3-phosphate acyltransferase 4;
GN Name=GPAT4; OrderedLocusNames=At1g01610; ORFNames=F22L4.15;
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 ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=12897259; DOI=10.1105/tpc.012427;
RA Zheng Z., Xia Q., Dauk M., Shen W., Selvaraj G., Zou J.;
RT "Arabidopsis AtGPAT1, a member of the membrane-bound glycerol-3-phosphate
RT acyltransferase gene family, is essential for tapetum differentiation and
RT male fertility.";
RL Plant Cell 15:1872-1887(2003).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20551224; DOI=10.1073/pnas.0914149107;
RA Yang W., Pollard M., Li-Beisson Y., Beisson F., Feig M., Ohlrogge J.;
RT "A distinct type of glycerol-3-phosphate acyltransferase with sn-2
RT preference and phosphatase activity producing 2-monoacylglycerol.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12040-12045(2010).
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-2 position of
CC glycerol-3-phosphate, a step in cutin biosynthesis.
CC {ECO:0000269|PubMed:20551224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 2-acyl-sn-glycerol
CC 3-phosphate + CoA; Xref=Rhea:RHEA:33559, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:58342, ChEBI:CHEBI:64982;
CC EC=2.3.1.198; Evidence={ECO:0000269|PubMed:12897259,
CC ECO:0000269|PubMed:20551224};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=58.92 pmol/min/mg enzyme {ECO:0000269|PubMed:12897259};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed at high level. Highly expressed in
CC seedlings, developing seedlings and flower buds.
CC {ECO:0000269|PubMed:12897259}.
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-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AC061957; AAF81319.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27311.1; -; Genomic_DNA.
DR EMBL; AY062466; AAL32544.1; -; mRNA.
DR EMBL; AY093294; AAM13293.1; -; mRNA.
DR PIR; H86146; H86146.
DR RefSeq; NP_171667.1; NM_100043.5.
DR AlphaFoldDB; Q9LMM0; -.
DR SMR; Q9LMM0; -.
DR BioGRID; 24532; 3.
DR IntAct; Q9LMM0; 1.
DR STRING; 3702.AT1G01610.1; -.
DR PaxDb; Q9LMM0; -.
DR PRIDE; Q9LMM0; -.
DR ProteomicsDB; 248504; -.
DR EnsemblPlants; AT1G01610.1; AT1G01610.1; AT1G01610.
DR GeneID; 839297; -.
DR Gramene; AT1G01610.1; AT1G01610.1; AT1G01610.
DR KEGG; ath:AT1G01610; -.
DR Araport; AT1G01610; -.
DR TAIR; locus:2025381; AT1G01610.
DR eggNOG; ENOG502RK50; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; Q9LMM0; -.
DR OMA; CERKVVV; -.
DR OrthoDB; 470640at2759; -.
DR PhylomeDB; Q9LMM0; -.
DR BRENDA; 2.3.1.198; 399.
DR BRENDA; 3.1.3.B13; 399.
DR PRO; PR:Q9LMM0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMM0; baseline and differential.
DR Genevisible; Q9LMM0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0090447; F:glycerol-3-phosphate 2-O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0102419; F:sn-2-glycerol-3-phosphate omega-OH-C22:0-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Glycerol-3-phosphate 2-O-acyltransferase 4"
FT /id="PRO_0000195252"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 311..316
FT /note="HXXXXD motif"
FT CONFLICT 205
FT /note="M -> K (in Ref. 3; AAL32544/AAM13293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 56262 MW; 827EEB7EBE337766 CRC64;
MSPAKKSRSF PPISECKSRE YDSIAADLDG TLLLSRSSFP YFMLVAIEAG SLFRGLILLL
SLPIVIIAYL FVSESLGIQI LIFISFAGIK IKNIELVSRA VLTRFYAADV RKDSFEVFDK
CKKRKVVVTA NPIVMVEPFV KDYLGGDKVL GTEIEVNPKT MKATGFVKKP GVLVGDLKRL
AILKEFGDDS PDLGLGDRTS DHDFMSICKE GYMVHETKSA TTVPIESLKN RIIFHDGRLV
QRPTPLNALI IYLWLPFGFM LSVFRVYFNL PLPERFVRYT YEILGIHLTI RGHRPPPPSP
GKPGNLYVLN HRTALDPIII AIALGRKITC VTYSVSRLSL MLSPIPAVAL TRDRVADAAR
MRQLLEKGDL VICPEGTTCR EPYLLRFSAL FAELSDRIVP VAMNCKQGMF NGTTVRGVKF
WDPYFFFMNP RPSYEATFLD RLPEEMTVNG GGKTPFEVAN YVQKVIGGVL GFECTELTRK
DKYLLLGGND GKVESINKTK SME