GPAT2_ARATH
ID GPAT2_ARATH Reviewed; 530 AA.
AC Q9FZ22;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable glycerol-3-phosphate acyltransferase 2;
DE Short=AtGPAT2;
DE EC=2.3.1.15;
GN Name=GPAT2; OrderedLocusNames=At1g02390; ORFNames=T6A9.17, T6A9.8;
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 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).
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}. Note=Not mitochondrial.
CC -!- TISSUE SPECIFICITY: Weakly or not expressed in roots, leaves,
CC seedlings, developing siliques 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; AC064879; AAG00890.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27423.1; -; Genomic_DNA.
DR EMBL; AF419560; AAL31892.1; -; mRNA.
DR EMBL; AY097339; AAM19855.1; -; mRNA.
DR PIR; C86154; C86154.
DR RefSeq; NP_563651.1; NM_100120.3.
DR AlphaFoldDB; Q9FZ22; -.
DR STRING; 3702.AT1G02390.1; -.
DR PaxDb; Q9FZ22; -.
DR PRIDE; Q9FZ22; -.
DR ProteomicsDB; 248462; -.
DR EnsemblPlants; AT1G02390.1; AT1G02390.1; AT1G02390.
DR GeneID; 839558; -.
DR Gramene; AT1G02390.1; AT1G02390.1; AT1G02390.
DR KEGG; ath:AT1G02390; -.
DR Araport; AT1G02390; -.
DR TAIR; locus:2204818; AT1G02390.
DR eggNOG; ENOG502QRJ7; Eukaryota.
DR HOGENOM; CLU_028504_1_0_1; -.
DR InParanoid; Q9FZ22; -.
DR OMA; PLFSHCK; -.
DR OrthoDB; 855637at2759; -.
DR PhylomeDB; Q9FZ22; -.
DR BioCyc; ARA:AT1G02390-MON; -.
DR BRENDA; 2.3.1.15; 399.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q9FZ22; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ22; baseline and differential.
DR Genevisible; Q9FZ22; 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; IBA:GO_Central.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..530
FT /note="Probable glycerol-3-phosphate acyltransferase 2"
FT /id="PRO_0000195250"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 339..344
FT /note="HXXXXD motif"
SQ SEQUENCE 530 AA; 59968 MW; 600A3D3243F11071 CRC64;
MSGNKISTLQ ALVFFLYRFF ILRRWCHRSP KQKYQKCPSH GLHQYQDLSN HTLIFNVEGA
LLKSNSLFPY FMVVAFEAGG VIRSLFLLVL YPFISLMSYE MGLKTMVMLS FFGVKKESFR
VGKSVLPKYF LEDVGLEMFQ VLKRGGKRVA VSDLPQVMID VFLRDYLEIE VVVGRDMKMV
GGYYLGIVED KKNLEIAFDK VVQEERLGSG RRLIGITSFN SPSHRSLFSQ FCQEIYFVRN
SDKKSWQTLP QDQYPKPLIF HDGRLAVKPT PLNTLVLFMW APFAAVLAAA RLVFGLNLPY
SLANPFLAFS GIHLTLTVNN HNDLISADRK RGCLFVCNHR TLLDPLYISY ALRKKNMKAV
TYSLSRLSEL LAPIKTVRLT RDRVKDGQAM EKLLSQGDLV VCPEGTTCRE PYLLRFSPLF
SEVCDVIVPV AIDSHVTFFY GTTASGLKAF DPIFFLLNPF PSYTVKLLDP VSGSSSSTCR
GVPDNGKVNF EVANHVQHEI GNALGFECTN LTRRDKYLIL AGNNGVVKKK
