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Mannose-1-phosphate guanylyltransferase 1 (EC 2.7.7.13) (GDP-mannose pyrophosphorylase 1) (Protein CYTOKINESIS DEFECTIVE 1) (Protein EMBRYO DEFECTIVE 101) (Protein HYPERSENSITIVE TO AMMONIUM ION 1) (Protein SENSITIVE TO OZONE 1) (Protein VITAMIN C DEFECTIVE 1)

 GMPP1_ARATH             Reviewed;         361 AA.
O22287; Q9C5B8;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 127.
RecName: Full=Mannose-1-phosphate guanylyltransferase 1;
EC=2.7.7.13;
AltName: Full=GDP-mannose pyrophosphorylase 1;
AltName: Full=Protein CYTOKINESIS DEFECTIVE 1;
AltName: Full=Protein EMBRYO DEFECTIVE 101;
AltName: Full=Protein HYPERSENSITIVE TO AMMONIUM ION 1;
AltName: Full=Protein SENSITIVE TO OZONE 1;
AltName: Full=Protein VITAMIN C DEFECTIVE 1;
Name=CYT1; Synonyms=EMB101, GMP1, HSN1, SOZ1, VTC1;
OrderedLocusNames=At2g39770; ORFNames=T5I7.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Weers B., Thornburg R.;
"Characterization of the cDNA and gene for the Arabidopsis thaliana
GDP-mannose pyrophosphorylase.";
(er) Plant Gene Register PGR98-175(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Lukowitz W., Somerville C.;
"Positional cloning of the Arabidopsis cyt1 gene.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Avila C.;
"Genes responding to phosphate starvation placed together in
Arabidopsis genome.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=8790441; DOI=10.1073/pnas.93.18.9970;
Conklin P.L., Williams E.H., Last R.L.;
"Environmental stress sensitivity of an ascorbic acid-deficient
Arabidopsis mutant.";
Proc. Natl. Acad. Sci. U.S.A. 93:9970-9974(1996).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9390448; DOI=10.1104/pp.115.3.1277;
Conklin P.L., Pallanca J.E., Last R.L., Smirnoff N.;
"L-ascorbic acid metabolism in the ascorbate-deficient arabidopsis
mutant vtc1.";
Plant Physiol. 115:1277-1285(1997).
[10]
DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=9750345; DOI=10.1046/j.1365-313X.1998.00212.x;
Nickle T.C., Meinke D.W.;
"A cytokinesis-defective mutant of Arabidopsis (cyt1) characterized by
embryonic lethality, incomplete cell walls, and excessive callose
accumulation.";
Plant J. 15:321-332(1998).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-22.
PubMed=10097187; DOI=10.1073/pnas.96.7.4198;
Conklin P.L., Norris S.R., Wheeler G.L., Williams E.H., Smirnoff N.,
Last R.L.;
"Genetic evidence for the role of GDP-mannose in plant ascorbic acid
(vitamin C) biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 96:4198-4203(1999).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10655235;
Conklin P.L., Saracco S.A., Norris S.R., Last R.L.;
"Identification of ascorbic acid-deficient Arabidopsis thaliana
mutants.";
Genetics 154:847-856(2000).
[13]
FUNCTION, AND MUTAGENESIS OF PRO-89.
PubMed=11226227; DOI=10.1073/pnas.051625798;
Lukowitz W., Nickle T.C., Meinke D.W., Last R.L., Conklin P.L.,
Somerville C.R.;
"Arabidopsis cyt1 mutants are deficient in a mannose-1-phosphate
guanylyltransferase and point to a requirement of N-linked
glycosylation for cellulose biosynthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:2262-2267(2001).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12671089; DOI=10.1105/tpc.010538;
Pastori G.M., Kiddle G., Antoniw J., Bernard S.,
Veljovic-Jovanovic S., Verrier P.J., Noctor G., Foyer C.H.;
"Leaf vitamin C contents modulate plant defense transcripts and
regulate genes that control development through hormone signaling.";
Plant Cell 15:939-951(2003).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15064386; DOI=10.1104/pp.103.032185;
Barth C., Moeder W., Klessig D.F., Conklin P.L.;
"The timing of senescence and response to pathogens is altered in the
ascorbate-deficient Arabidopsis mutant vitamin c-1.";
Plant Physiol. 134:1784-1792(2004).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16244149; DOI=10.1104/pp.105.067686;
Pavet V., Olmos E., Kiddle G., Mowla S., Kumar S., Antoniw J.,
Alvarez M.E., Foyer C.H.;
"Ascorbic acid deficiency activates cell death and disease resistance
responses in Arabidopsis.";
Plant Physiol. 139:1291-1303(2005).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16720601; DOI=10.1093/jxb/erl010;
Olmos E., Kiddle G., Pellny T., Kumar S., Foyer C.H.;
"Modulation of plant morphology, root architecture, and cell structure
by low vitamin C in Arabidopsis thaliana.";
J. Exp. Bot. 57:1645-1655(2006).
[18]
FUNCTION.
PubMed=18849295; DOI=10.1093/jxb/ern229;
Colville L., Smirnoff N.;
"Antioxidant status, peroxidase activity, and PR protein transcript
levels in ascorbate-deficient Arabidopsis thaliana vtc mutants.";
J. Exp. Bot. 59:3857-3868(2008).
[19]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-11.
PubMed=19011088; DOI=10.1073/pnas.0806168105;
Qin C., Qian W., Wang W., Wu Y., Yu C., Jiang X., Wang D., Wu P.;
"GDP-mannose pyrophosphorylase is a genetic determinant of ammonium
sensitivity in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 105:18308-18313(2008).
[20]
DISRUPTION PHENOTYPE.
PubMed=20007685; DOI=10.1093/jxb/erp310;
Barth C., Gouzd Z.A., Steele H.P., Imperio R.M.;
"A mutation in GDP-mannose pyrophosphorylase causes conditional
hypersensitivity to ammonium, resulting in Arabidopsis root growth
inhibition, altered ammonium metabolism, and hormone homeostasis.";
J. Exp. Bot. 61:379-394(2010).
[21]
INTERACTION WITH CSN5A AND CSN5B, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=23424245; DOI=10.1105/tpc.112.106880;
Wang J., Yu Y., Zhang Z., Quan R., Zhang H., Ma L., Deng X.W.,
Huang R.;
"Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid
synthesis.";
Plant Cell 25:625-636(2013).
-!- FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway,
the major route to ascorbate biosynthesis in plants. Plays an
essential role in plant growth and development and cell-wall
architecture. Provides GDP-mannose, used for cell wall
carbohydrate biosynthesis, protein N-glycosylation, as well as for
the biosynthesis of the antioxidant ascorbate.
{ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:10655235,
ECO:0000269|PubMed:11226227, ECO:0000269|PubMed:12671089,
ECO:0000269|PubMed:15064386, ECO:0000269|PubMed:16244149,
ECO:0000269|PubMed:16720601, ECO:0000269|PubMed:18849295,
ECO:0000269|PubMed:19011088, ECO:0000269|PubMed:8790441,
ECO:0000269|PubMed:9390448}.
-!- CATALYTIC ACTIVITY:
Reaction=alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate +
GDP-alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
ChEBI:CHEBI:58409; EC=2.7.7.13;
-!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate
(GTP route): step 1/1.
-!- SUBUNIT: Interacts in vitro with CSN5A and CSN5B, but in planta
with CSN5B only, targeting CYT1 for degradation in the dark by the
26S proteasome. {ECO:0000269|PubMed:23424245}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23424245}.
Nucleus {ECO:0000269|PubMed:23424245}.
-!- DOMAIN: The N-terminus (1-40) is necessary for interaction with
CNS5B. {ECO:0000269|PubMed:23424245}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal. Deficient in N-
glycosylation, altered in cytokinesis and cell wall architecture
during embryogenesis. Mutants vtc1 and hsn1 with reduced enzyme
activity show reduced root length and leaf cell size, reduced
accumulation of ascorbate, increased sensitivity to ozone, UV-B
and oxidative stresses, increased levels of abscisic acid (ABA),
salicylic acid (SA) and resistance to virulent pathogens and root
growth inhibition in the presence of NH(4)(+).
{ECO:0000269|PubMed:10097187, ECO:0000269|PubMed:10655235,
ECO:0000269|PubMed:12671089, ECO:0000269|PubMed:15064386,
ECO:0000269|PubMed:16244149, ECO:0000269|PubMed:16720601,
ECO:0000269|PubMed:19011088, ECO:0000269|PubMed:20007685,
ECO:0000269|PubMed:8790441, ECO:0000269|PubMed:9390448,
ECO:0000269|PubMed:9750345}.
-!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF076484; AAC78474.1; -; mRNA.
EMBL; AF108660; AAD04627.1; -; mRNA.
EMBL; AJ275979; CAC35355.1; -; Genomic_DNA.
EMBL; AC003000; AAB87126.1; -; Genomic_DNA.
EMBL; CP002685; AEC09721.1; -; Genomic_DNA.
EMBL; CP002685; AEC09722.1; -; Genomic_DNA.
EMBL; CP002685; ANM63165.1; -; Genomic_DNA.
EMBL; AF361812; AAK32825.1; -; mRNA.
EMBL; AY057541; AAL09781.1; -; mRNA.
EMBL; AF428297; AAL16129.1; -; mRNA.
EMBL; AY133643; AAM91473.1; -; mRNA.
EMBL; BT000697; AAN31841.1; -; mRNA.
EMBL; BT006365; AAP21173.1; -; mRNA.
EMBL; AY087698; AAM65235.1; -; mRNA.
PIR; T01007; T01007.
RefSeq; NP_001189713.1; NM_001202784.1.
RefSeq; NP_001325272.1; NM_001336797.1.
RefSeq; NP_181507.1; NM_129535.4.
UniGene; At.10348; -.
ProteinModelPortal; O22287; -.
SMR; O22287; -.
BioGrid; 3900; 5.
IntAct; O22287; 2.
STRING; 3702.AT2G39770.1; -.
PaxDb; O22287; -.
PRIDE; O22287; -.
EnsemblPlants; AT2G39770.1; AT2G39770.1; AT2G39770.
EnsemblPlants; AT2G39770.2; AT2G39770.2; AT2G39770.
EnsemblPlants; AT2G39770.3; AT2G39770.3; AT2G39770.
GeneID; 818562; -.
Gramene; AT2G39770.1; AT2G39770.1; AT2G39770.
Gramene; AT2G39770.2; AT2G39770.2; AT2G39770.
Gramene; AT2G39770.3; AT2G39770.3; AT2G39770.
KEGG; ath:AT2G39770; -.
Araport; AT2G39770; -.
TAIR; locus:2005504; AT2G39770.
eggNOG; KOG1322; Eukaryota.
eggNOG; COG1208; LUCA.
HOGENOM; HOG000283479; -.
InParanoid; O22287; -.
KO; K00966; -.
OMA; HIRSHSW; -.
OrthoDB; EOG09360CRU; -.
PhylomeDB; O22287; -.
BioCyc; MetaCyc:AT2G39770-MONOMER; -.
BRENDA; 2.7.7.13; 399.
UniPathway; UPA00126; UER00930.
PRO; PR:O22287; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O22287; baseline and differential.
Genevisible; O22287; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IMP:TAIR.
GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
GO; GO:0060359; P:response to ammonium ion; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
GO; GO:0010193; P:response to ozone; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001451; Hexapep.
InterPro; IPR005835; NTP_transferase_dom.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF00132; Hexapep; 1.
Pfam; PF00483; NTP_transferase; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
CHAIN 1 361 Mannose-1-phosphate guanylyltransferase
1.
/FTId=PRO_0000412464.
MUTAGEN 11 11 G->S: In hsn1; reduced enzyme activity,
ascorbate concentrations and N-
glycosylation, and increased sensitivity
to ammonium.
{ECO:0000269|PubMed:19011088}.
MUTAGEN 22 22 P->S: In vtc1-1 and vtc1-2; reduced
enzyme activity and ascorbate
concentrations, and ozone-sensitive.
{ECO:0000269|PubMed:10097187}.
MUTAGEN 89 89 P->L: In cyt1-1; deficient in N-
glycosylation and cellulose, and embryo
lethal. {ECO:0000269|PubMed:11226227}.
CONFLICT 121 121 M -> I (in Ref. 3; CAC35355).
{ECO:0000305}.
CONFLICT 208 208 L -> H (in Ref. 3; CAC35355).
{ECO:0000305}.
SEQUENCE 361 AA; 39577 MW; D282B510E22C2F06 CRC64;
MKALILVGGF GTRLRPLTLS FPKPLVDFAN KPMILHQIEA LKAVGVDEVV LAINYQPEVM
LNFLKDFETK LEIKITCSQE TEPLGTAGPL ALARDKLLDG SGEPFFVLNS DVISEYPLKE
MLEFHKSHGG EASIMVTKVD EPSKYGVVVM EESTGRVEKF VEKPKLYVGN KINAGIYLLN
PSVLDKIELR PTSIEKETFP KIAAAQGLYA MVLPGFWMDI GQPRDYITGL RLYLDSLRKK
SPAKLTSGPH IVGNVLVDET ATIGEGCLIG PDVAIGPGCI VESGVRLSRC TVMRGVRIKK
HACISSSIIG WHSTVGQWAR IENMTILGED VHVSDEIYSN GGVVLPHKEI KSNILKPEIV
M


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