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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
 
 
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