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GPAT1_ARATH
ID   GPAT1_ARATH             Reviewed;         585 AA.
AC   Q9SHJ5; Q8L8V5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 1;
DE            Short=AtGPAT1;
DE            EC=2.3.1.15;
GN   Name=GPAT1; OrderedLocusNames=At1g06520; ORFNames=F12K11.15;
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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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       Involved in pollen development, by being required for tapetum
CC       differentiation and male fertility. In addition to the sporophytic
CC       effect, it also exerts a gametophytic effect on pollen performance.
CC       {ECO:0000269|PubMed:12897259}.
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         Evidence={ECO:0000269|PubMed:12897259};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=217.42 pmol/min/mg enzyme {ECO:0000269|PubMed:12897259};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12897259}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:12897259}. Mitochondrion
CC       {ECO:0000269|PubMed:12897259}. Note=According to PubMed:12897259 it is
CC       mitochondrial. However, no clear transit peptide is predicted by
CC       sequence analysis tools.
CC   -!- TISSUE SPECIFICITY: Highly expressed in developing siliques and flower
CC       buds. Weakly or not expressed in roots, seedlings and leaves.
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   -!- DISRUPTION PHENOTYPE: Plants display a massive pollen development
CC       arrest due to a perturbed degeneration of the tapetum, which is
CC       associated with altered endoplasmic reticulum profiles and reduced
CC       secretion. Defects correlate with several fatty acid composition
CC       changes in flower tissues and seeds. However, no significant change in
CC       seed oil content is observed. {ECO:0000269|PubMed:12897259}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR   EMBL; AC007592; AAF24816.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28001.1; -; Genomic_DNA.
DR   EMBL; AY088785; AAM67097.1; -; mRNA.
DR   PIR; G86200; G86200.
DR   RefSeq; NP_563768.1; NM_100531.3.
DR   AlphaFoldDB; Q9SHJ5; -.
DR   STRING; 3702.AT1G06520.1; -.
DR   PaxDb; Q9SHJ5; -.
DR   PRIDE; Q9SHJ5; -.
DR   ProteomicsDB; 248461; -.
DR   EnsemblPlants; AT1G06520.1; AT1G06520.1; AT1G06520.
DR   GeneID; 837163; -.
DR   Gramene; AT1G06520.1; AT1G06520.1; AT1G06520.
DR   KEGG; ath:AT1G06520; -.
DR   Araport; AT1G06520; -.
DR   TAIR; locus:2009225; AT1G06520.
DR   eggNOG; ENOG502QWBX; Eukaryota.
DR   HOGENOM; CLU_028504_1_0_1; -.
DR   InParanoid; Q9SHJ5; -.
DR   OMA; QDGETMQ; -.
DR   OrthoDB; 423986at2759; -.
DR   PhylomeDB; Q9SHJ5; -.
DR   BRENDA; 2.3.1.15; 399.
DR   UniPathway; UPA00557; UER00612.
DR   PRO; PR:Q9SHJ5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHJ5; baseline and differential.
DR   Genevisible; Q9SHJ5; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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; 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   GO; GO:0048235; P:pollen sperm cell differentiation; IMP:TAIR.
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   Mitochondrion; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..585
FT                   /note="Glycerol-3-phosphate acyltransferase 1"
FT                   /id="PRO_0000195249"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           403..408
FT                   /note="HXXXXD motif"
FT   CONFLICT        21
FT                   /note="K -> N (in Ref. 3; AAM67097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="F -> L (in Ref. 3; AAM67097)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   585 AA;  66514 MW;  3F7FDCE161C28EAF CRC64;
     MVLPELLVIL AEWVLYRLLA KSCYRAARKL RGYGFQLKNL LSLSKTQSLH NNSQHHLHNH
     HQQNHPNQTL QDSLDPLFPS LTKYQELLLD KNRACSVSSD HYRDTFFCDI DGVLLRQHSS
     KHFHTFFPYF MLVAFEGGSI IRAILLLLSC SFLWTLQQET KLRVLSFITF SGLRVKDMDN
     VSRSVLPKFF LENLNIQVYD IWARTEYSKV VFTSLPQVLV ERFLREHLNA DDVIGTKLQE
     IKVMGRKFYT GLASGSGFVL KHKSAEDYFF DSKKKPALGI GSSSSPQDHI FISICKEAYF
     WNEEESMSKN NALPRERYPK PLIFHDGRLA FLPTPLATLA MFIWLPIGFL LAVFRISVGV
     FLPYHVANFL ASMSGVRITF KTHNLNNGRP EKGNSGVLYV CNHRTLLDPV FLTTSLGKPL
     TAVTYSLSKF SEFIAPLKTV SLKRDRKKDG EAMQRLLSKG DLVVCPEGTT CREPYLLRFS
     PLFAELTEDI VPVAVDARVS MFYGTTASGL KCLDPIFFLM NPRPVYCLEI LKKLPKEMTC
     AGGKSSFEVA NFIQGELARV LGFECTNLTR RDKYLVLAGN EGIVR
 
 
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