CGR3_ARATH
ID CGR3_ARATH Reviewed; 258 AA.
AC Q0WPN7; Q8LAU7; Q9FH88;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable pectin methylesterase CGR3 {ECO:0000303|PubMed:25704846};
DE EC=2.1.1.- {ECO:0000305|PubMed:27208234};
DE AltName: Full=Cotton Golgi-related 3 {ECO:0000303|PubMed:21422118};
GN Name=CGR3 {ECO:0000303|PubMed:21422118};
GN OrderedLocusNames=At5g65810 {ECO:0000312|Araport:AT5G65810};
GN ORFNames=K22J17.2 {ECO:0000312|EMBL:BAB09049.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21422118; DOI=10.1093/mp/ssr012;
RA Held M.A., Be E., Zemelis S., Withers S., Wilkerson C., Brandizzi F.;
RT "CGR3: a Golgi-localized protein influencing homogalacturonan
RT methylesterification.";
RL Mol. Plant 4:832-844(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25704846; DOI=10.1111/tpj.12802;
RA Kim S.-J., Held M.A., Zemelis S., Wilkerson C., Brandizzi F.;
RT "CGR2 and CGR3 have critical overlapping roles in pectin
RT methylesterification and plant growth in Arabidopsis thaliana.";
RL Plant J. 82:208-220(2015).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27208234; DOI=10.1104/pp.16.00173;
RA Weraduwage S.M., Kim S.-J., Renna L., Anozie F.C., Sharkey T.D.,
RA Brandizzi F.;
RT "Pectin Methylesterification Impacts the Relationship between
RT Photosynthesis and Plant Growth.";
RL Plant Physiol. 171:833-848(2016).
CC -!- FUNCTION: Together with CGR2, required for homogalacturonan pectins
CC (HG) methylesterification in the Golgi apparatus prior to integration
CC into cell walls, essential for general growth and development
CC (PubMed:21422118, PubMed:25704846, PubMed:27208234). Promotes petiole
CC elongation (PubMed:21422118). Impacts photosynthesis and respiration
CC efficiency by influencing leaf mesophyll morphology and physiology;
CC pectin methylesterification modulates both expansion and positioning of
CC cells in leaves, probably by changing cell walls plasticity
CC (PubMed:27208234). {ECO:0000269|PubMed:21422118,
CC ECO:0000269|PubMed:25704846, ECO:0000269|PubMed:27208234}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21422118, ECO:0000269|PubMed:25704846}; Single-pass
CC membrane protein {ECO:0000269|PubMed:21422118,
CC ECO:0000269|PubMed:25704846}.
CC -!- DISRUPTION PHENOTYPE: Reduced homogalacturonan pectins (HG)
CC methylesterification in cell walls (PubMed:21422118). Plants lacking
CC both CGR2 and CGR3 (cgr2-1 cgr3-1) exihibit severe defects in plant
CC growth and development (e.g. shorter hypocotyl and primary root length
CC due to reduced cell elongation, and abnormal pollen tube elongation),
CC as well as reduced levels of pectin methylesterification associated
CC with decreased microsomal pectin methyltransferase activity. The double
CC mutant cgr2-1 cgr3-1 also lacks uronic acids and methyl ester
CC (PubMed:25704846). Reduced HG methylesterification in cgr2-1 cgr3-1
CC double mutant results in thin but dense leaf mesophyll that limits
CC CO(2) diffusion to chloroplasts and reduces leaf area, thus impairing
CC photosynthesis efficiency and carbon (C) partitioning
CC (PubMed:27208234). {ECO:0000269|PubMed:21422118,
CC ECO:0000269|PubMed:25704846, ECO:0000269|PubMed:27208234}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020743; BAB09049.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98110.1; -; Genomic_DNA.
DR EMBL; AK229026; BAF00912.1; -; mRNA.
DR EMBL; BT033154; ACF75543.1; -; mRNA.
DR EMBL; AY087599; AAM65141.1; -; mRNA.
DR RefSeq; NP_569020.1; NM_125978.4.
DR AlphaFoldDB; Q0WPN7; -.
DR STRING; 3702.AT5G65810.1; -.
DR iPTMnet; Q0WPN7; -.
DR PaxDb; Q0WPN7; -.
DR PRIDE; Q0WPN7; -.
DR ProteomicsDB; 241233; -.
DR EnsemblPlants; AT5G65810.1; AT5G65810.1; AT5G65810.
DR GeneID; 836710; -.
DR Gramene; AT5G65810.1; AT5G65810.1; AT5G65810.
DR KEGG; ath:AT5G65810; -.
DR Araport; AT5G65810; -.
DR TAIR; locus:2156208; AT5G65810.
DR eggNOG; ENOG502QR9D; Eukaryota.
DR HOGENOM; CLU_071215_0_0_1; -.
DR InParanoid; Q0WPN7; -.
DR OMA; WWIRFFS; -.
DR OrthoDB; 1210334at2759; -.
DR PhylomeDB; Q0WPN7; -.
DR PRO; PR:Q0WPN7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WPN7; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015976; P:carbon utilization; IMP:UniProtKB.
DR GO; GO:0010394; P:homogalacturonan metabolic process; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IGI:TAIR.
DR GO; GO:0045488; P:pectin metabolic process; IMP:UniProtKB.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:UniProtKB.
DR GO; GO:1905157; P:positive regulation of photosynthesis; IMP:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; IMP:UniProtKB.
DR GO; GO:0051512; P:positive regulation of unidimensional cell growth; IGI:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR044689; CGR2/3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR34208; PTHR34208; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Golgi apparatus; Membrane;
KW Methyltransferase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..258
FT /note="Probable pectin methylesterase CGR3"
FT /id="PRO_0000444196"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25704846"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..258
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:25704846"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 200
FT /note="G -> A (in Ref. 5; AAM65141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28296 MW; DF065DD8B4D272F5 CRC64;
MSRRQVRRVG DSGSFPFVGA LHSKSRSSPL LSVCLVLVGA CLLIGYAYSG PGMFKSIREV
SKITGDYSCT AEVQRAIPIL KSAYGDSMRK VLHVGPETCS VVSSLLNEEE TEAWGVEPYD
VEDADSNCKS LLHKGLVRVA DIKFPLPYRS KSFSLVIVSD ALDYLSPRYL NKTVPELARV
ASDGVVLLAG NPGQQKAKGG ELSKFGRPAK MRSSSWWIRF FSQTNLEENE AASKKFEQAA
SKSSYKPACQ VFHLKPLH
