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MGDG2_ARATH
ID   MGDG2_ARATH             Reviewed;         468 AA.
AC   O82730; Q94JU8; W8Q2S4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Monogalactosyldiacylglycerol synthase 2, chloroplastic {ECO:0000305};
DE            Short=AtMGD2 {ECO:0000303|PubMed:11553816};
DE            EC=2.4.1.46 {ECO:0000269|PubMed:11553816};
DE   AltName: Full=MGDG synthase type B {ECO:0000303|PubMed:11553816};
DE   Flags: Precursor;
GN   Name=MGD2 {ECO:0000303|PubMed:11553816};
GN   Synonyms=MGDB {ECO:0000303|PubMed:11553816};
GN   OrderedLocusNames=At5g20410 {ECO:0000312|Araport:AT5G20410};
GN   ORFNames=F5O24.300, F7C8;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=11553816; DOI=10.1073/pnas.181331498;
RA   Awai K., Marechal E., Block M.A., Brun D., Masuda T., Shimada H.,
RA   Takamiya K., Ohta H., Joyard J.;
RT   "Two types of MGDG synthase genes, found widely in both 16:3 and 18:3
RT   plants, differentially mediate galactolipid syntheses in photosynthetic and
RT   nonphotosynthetic tissues in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10960-10965(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-468.
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   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14730084; DOI=10.1104/pp.103.032656;
RA   Kobayashi K., Awai K., Takamiya K., Ohta H.;
RT   "Arabidopsis type B monogalactosyldiacylglycerol synthase genes are
RT   expressed during pollen tube growth and induced by phosphate starvation.";
RL   Plant Physiol. 134:640-648(2004).
RN   [7]
RP   INDUCTION.
RX   PubMed=16762032; DOI=10.1111/j.1365-313x.2006.02778.x;
RA   Kobayashi K., Masuda T., Takamiya K., Ohta H.;
RT   "Membrane lipid alteration during phosphate starvation is regulated by
RT   phosphate signaling and auxin/cytokinin cross-talk.";
RL   Plant J. 47:238-248(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=18808455; DOI=10.1111/j.1365-313x.2008.03692.x;
RA   Kobayashi K., Awai K., Nakamura M., Nagatani A., Masuda T., Ohta H.;
RT   "Type-B monogalactosyldiacylglycerol synthases are involved in phosphate
RT   starvation-induced lipid remodeling, and are crucial for low-phosphate
RT   adaptation.";
RL   Plant J. 57:322-331(2009).
RN   [9]
RP   ACTIVITY REGULATION.
RX   PubMed=21946275; DOI=10.1038/nchembio.658;
RA   Botte C.Y., Deligny M., Roccia A., Bonneau A.L., Saidani N., Hardre H.,
RA   Aci S., Yamaryo-Botte Y., Jouhet J., Dubots E., Loizeau K., Bastien O.,
RA   Brehelin L., Joyard J., Cintrat J.C., Falconet D., Block M.A., Rousseau B.,
RA   Lopez R., Marechal E.;
RT   "Chemical inhibitors of monogalactosyldiacylglycerol synthases in
RT   Arabidopsis thaliana.";
RL   Nat. Chem. Biol. 7:834-842(2011).
RN   [10]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=31201686; DOI=10.1007/s11103-019-00891-1;
RA   Murakawa M., Ohta H., Shimojima M.;
RT   "Lipid remodeling under acidic conditions and its interplay with low Pi
RT   stress in Arabidopsis.";
RL   Plant Mol. Biol. 101:81-93(2019).
CC   -!- FUNCTION: Involved in the synthesis of monogalactosyldiacylglycerol,
CC       the major structural component of photosynthetic membranes and in the
CC       chloroplast envelope biogenesis. Can use both prokaryotic (18:1/16:0)
CC       or eukaryotic (18:2/18:2) 1,2-diacylglycerol species, but operates with
CC       some preference for the eukaryotic one. Plays a minor role in
CC       galactolipid synthesis in chloroplasts (PubMed:11553816). Is required
CC       for membrane lipid remodeling in phosphate-starved roots
CC       (PubMed:18808455, PubMed:31201686). Acts as the minor factor involved
CC       in digalactosyldiacylglycerol (DGDG) biosynthesis in phosphate-starved
CC       roots (PubMed:18808455). Does not seem to be required for plant growth
CC       under nutrient-sufficient conditions (PubMed:18808455). Required for
CC       membrane lipid remodeling in plants grown in acidic conditions
CC       (PubMed:31201686). {ECO:0000269|PubMed:11553816,
CC       ECO:0000269|PubMed:18808455, ECO:0000269|PubMed:31201686}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-galactose = a 1,2-
CC         diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+) + UDP;
CC         Xref=Rhea:RHEA:14945, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.46;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14946;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycerol + UDP-alpha-D-
CC         galactose = 1,2-di-(9Z,12Z-octadecadienoyl)-3-beta-D-galactosyl-sn-
CC         glycerol + H(+) + UDP; Xref=Rhea:RHEA:48492, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:77127,
CC         ChEBI:CHEBI:90506; Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48493;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + UDP-alpha-D-
CC         galactose = 1-(9Z-octadecenoyl)-2-hexadecanoyl-3-beta-D-galactosyl-
CC         sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:48496, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:75447,
CC         ChEBI:CHEBI:90507; Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48497;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + UDP-alpha-D-galactose =
CC         1,2-di-(9Z-octadecenoyl)-3-beta-D-galactosyl-sn-glycerol + H(+) +
CC         UDP; Xref=Rhea:RHEA:48480, ChEBI:CHEBI:15378, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:63775, ChEBI:CHEBI:66914;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48481;
CC         Evidence={ECO:0000269|PubMed:11553816};
CC   -!- ACTIVITY REGULATION: Inhibited by galvestine-1.
CC       {ECO:0000269|PubMed:21946275}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000305|PubMed:11553816}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in floral buds. Detected in roots,
CC       leaves, stems, siliques and pollen tubes. {ECO:0000269|PubMed:11553816,
CC       ECO:0000269|PubMed:14730084}.
CC   -!- DEVELOPMENTAL STAGE: Low and continuous expression throughout whole
CC       developmental stages. {ECO:0000269|PubMed:11553816}.
CC   -!- INDUCTION: Induced by phosphate deprivation (PubMed:11553816,
CC       PubMed:14730084, PubMed:16762032). Induced in rosette leaves when grown
CC       in acidic soil (PubMed:31201686). {ECO:0000269|PubMed:11553816,
CC       ECO:0000269|PubMed:14730084, ECO:0000269|PubMed:16762032,
CC       ECO:0000269|PubMed:31201686}.
CC   -!- MISCELLANEOUS: Auxin activates expression during Pi starvation, whereas
CC       cytokinin represses it.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK50066.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ000331; CAA04005.1; -; mRNA.
DR   EMBL; KJ138675; AHL38615.1; -; mRNA.
DR   EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92840.1; -; Genomic_DNA.
DR   EMBL; AF372926; AAK50066.1; ALT_INIT; mRNA.
DR   EMBL; AY078038; AAL77739.1; -; mRNA.
DR   PIR; T52269; T52269.
DR   RefSeq; NP_568394.2; NM_122048.4.
DR   AlphaFoldDB; O82730; -.
DR   SMR; O82730; -.
DR   STRING; 3702.AT5G20410.1; -.
DR   SwissLipids; SLP:000001445; -.
DR   CAZy; GT28; Glycosyltransferase Family 28.
DR   iPTMnet; O82730; -.
DR   PaxDb; O82730; -.
DR   PRIDE; O82730; -.
DR   ProteomicsDB; 238336; -.
DR   EnsemblPlants; AT5G20410.1; AT5G20410.1; AT5G20410.
DR   GeneID; 832163; -.
DR   Gramene; AT5G20410.1; AT5G20410.1; AT5G20410.
DR   KEGG; ath:AT5G20410; -.
DR   Araport; AT5G20410; -.
DR   TAIR; locus:2149274; AT5G20410.
DR   eggNOG; ENOG502QPXV; Eukaryota.
DR   HOGENOM; CLU_028367_3_1_1; -.
DR   InParanoid; O82730; -.
DR   OMA; NIPYMLT; -.
DR   OrthoDB; 628561at2759; -.
DR   PhylomeDB; O82730; -.
DR   BioCyc; MetaCyc:AT5G20410-MON; -.
DR   BRENDA; 2.4.1.46; 399.
DR   PRO; PR:O82730; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O82730; baseline and differential.
DR   Genevisible; O82730; AT.
DR   GO; GO:0009707; C:chloroplast outer membrane; TAS:TAIR.
DR   GO; GO:0046509; F:1,2-diacylglycerol 3-beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035250; F:UDP-galactosyltransferase activity; TAS:TAIR.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IGI:TAIR.
DR   GO; GO:0006631; P:fatty acid metabolic process; IGI:TAIR.
DR   GO; GO:0019374; P:galactolipid metabolic process; IGI:TAIR.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR009695; Diacylglyc_glucosyltr_N.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   Pfam; PF06925; MGDG_synth; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Glycosyltransferase; Membrane; Plastid;
KW   Plastid outer membrane; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..468
FT                   /note="Monogalactosyldiacylglycerol synthase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000349422"
FT   BINDING         82
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O81770"
FT   BINDING         251
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O81770"
FT   BINDING         361..365
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O81770"
FT   BINDING         383
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O81770"
SQ   SEQUENCE   468 AA;  52727 MW;  58F56C3C1C383C24 CRC64;
     MATTVMALAE KVLERVYGTS KSAVSVTSGD GEKTHRHTHH HIHRIKSYDD IDEDESSLEL
     IQIGAERTKN VLILMSDTGG GHRASAEAIR DAFKIEFGDK YRVIVKDVWK EYTGWPLNDM
     ERSYKFMVKH VQLWKVAFHS TSPKWIHSCY LAAIAAYYAK EVEAGLMEYK PEIIISVHPL
     MQHIPLWVLK WQELQKRVLF VTVITDLNTC HPTWFHPGVN RCYCPSQEVA KRALFDGLDE
     SQVRVFGLPV RPSFARAVLV KDDLRKELEM DQDLRAVLLM GGGEGMGPVK ETAKALEEFL
     YDKENRKPIG QMVVICGRNK KLASALEAID WKIPVKVRGF ETQMEKWMGA CDCIITKAGP
     GTIAESLIRS LPIILNDYIP GQEKGNVPYV VENGAGVFTR SPKETARIVG EWFSTKTDEL
     EQTSDNARKL AQPEAVFDIV KDIDELSEQR GPLASVSYNL TSSFASLV
 
 
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