GPAT8_ARATH
ID GPAT8_ARATH Reviewed; 500 AA.
AC Q5XF03; O23061; O23062; Q0WQ37;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable glycerol-3-phosphate acyltransferase 8;
DE EC=2.3.1.15;
GN Name=GPAT8; OrderedLocusNames=At4g00400/At4g00410;
GN ORFNames=F5I10.4/F5I10.5;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62826.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
CC Sequence=AAB62827.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
CC Sequence=AAF02784.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
CC Sequence=AAF02785.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
CC Sequence=CAB80798.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
CC Sequence=CAB80799.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00400 and At4g00410.; Evidence={ECO:0000305};
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DR EMBL; AF013293; AAB62826.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF013293; AAB62827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02784.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02785.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81873.1; -; Genomic_DNA.
DR EMBL; BT015813; AAU94376.1; -; mRNA.
DR EMBL; AK228870; BAF00762.1; -; mRNA.
DR PIR; T01530; T01530.
DR PIR; T01531; T01531.
DR RefSeq; NP_191950.2; NM_116264.6.
DR AlphaFoldDB; Q5XF03; -.
DR SMR; Q5XF03; -.
DR BioGRID; 13429; 4.
DR IntAct; Q5XF03; 2.
DR STRING; 3702.AT4G00400.1; -.
DR iPTMnet; Q5XF03; -.
DR PaxDb; Q5XF03; -.
DR PRIDE; Q5XF03; -.
DR ProteomicsDB; 247026; -.
DR EnsemblPlants; AT4G00400.1; AT4G00400.1; AT4G00400.
DR GeneID; 828140; -.
DR Gramene; AT4G00400.1; AT4G00400.1; AT4G00400.
DR KEGG; ath:AT4G00400; -.
DR Araport; AT4G00400; -.
DR TAIR; locus:2126101; AT4G00400.
DR eggNOG; ENOG502RK50; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; Q5XF03; -.
DR OMA; YMVHATK; -.
DR OrthoDB; 470640at2759; -.
DR PhylomeDB; Q5XF03; -.
DR BioCyc; MetaCyc:AT4G00400-MON; -.
DR BRENDA; 2.3.1.15; 399.
DR BRENDA; 2.3.1.198; 399.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q5XF03; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XF03; baseline and differential.
DR Genevisible; Q5XF03; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
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:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010143; P:cutin biosynthetic process; IMP:TAIR.
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 2: Evidence at transcript level;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..500
FT /note="Probable glycerol-3-phosphate acyltransferase 8"
FT /id="PRO_0000195256"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 310..315
FT /note="HXXXXD motif"
FT CONFLICT 386
FT /note="F -> S (in Ref. 4; BAF00762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55867 MW; A1AD4675F0FC3F0D CRC64;
MSPEKKSQNF PPITECRDGE YDSIAADLDG TLLLSRSSFP YFMLVAVEAG SLLRGLILLL
SLPFVIISYL FVSESLGIQI LIFISFAGLK IRDIELVSRA VLPRFYAADV RKDSFEVFDK
CKRKVVVTAN PIVMVEAFVK DYLGGDKVLG TEIEVNPKTN RATGFVKKPG VLVGDLKRLA
ILKEFGNESP DLGLGDRTSD HDFMSLCKKG YMVHATKSAT TIPKERLKNR IVFHDGRLAQ
RPTPLNAIIT YLWLPFGFIL SIIRVYFNLP LPERFVRYTY EMLGIHLTIR GHRPPPPSPG
TLGNLYVLNH RTALDPIIVA IALGRKICCV TYSVSRLSLM LSPIPAVALT RDRATDAANM
RKLLEKGDLV ICPEGTTCRE EYLLRFSALF AELSDRIVPV AMNCKQGMFN GTTVRGVKFW
DPYFFFMNPR PSYEATFLDR LPEEMTVNGG GKTPIEVANY VQKVIGAVLG FECTELTRKD
KYLLLGGNDG KVESINNTKK
