PMTT_ARATH
ID PMTT_ARATH Reviewed; 684 AA.
AC Q9C9Q8; Q0WM11; Q9M9E5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable pectin methyltransferase QUA2;
DE EC=2.1.1.-;
DE AltName: Full=Protein OVERSENSITIVE TO SUGAR 1;
DE AltName: Full=Protein QUASIMODO 2;
DE AltName: Full=Protein TUMOROUS SHOOT DEVELOPMENT 2;
GN Name=QUA2; Synonyms=OSU1, TSD2; OrderedLocusNames=At1g78240;
GN ORFNames=F3F9.21, T11I11.18;
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] OF 633-684.
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17425712; DOI=10.1111/j.1365-313x.2007.03086.x;
RA Mouille G., Ralet M.C., Cavelier C., Eland C., Effroy D., Hematy K.,
RA McCartney L., Truong H.N., Gaudon V., Thibault J.F., Marchant A., Hofte H.;
RT "Homogalacturonan synthesis in Arabidopsis thaliana requires a Golgi-
RT localized protein with a putative methyltransferase domain.";
RL Plant J. 50:605-614(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17461780; DOI=10.1111/j.1365-313x.2007.03123.x;
RA Krupkova E., Immerzeel P., Pauly M., Schmulling T.;
RT "The TUMOROUS SHOOT DEVELOPMENT2 gene of Arabidopsis encoding a putative
RT methyltransferase is required for cell adhesion and co-ordinated plant
RT development.";
RL Plant J. 50:735-750(2007).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-560, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18167546; DOI=10.1371/journal.pone.0001387;
RA Gao P., Xin Z., Zheng Z.L.;
RT "The OSU1/QUA2/TSD2-encoded putative methyltransferase is a critical
RT modulator of carbon and nitrogen nutrient balance response in
RT Arabidopsis.";
RL PLoS ONE 3:E1387-E1387(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: May be involved in the synthesis of homogalacturonan.
CC Required for normal cell adhesion and plant development.
CC {ECO:0000269|PubMed:17425712, ECO:0000269|PubMed:17461780,
CC ECO:0000269|PubMed:18167546}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17425712, ECO:0000269|PubMed:17461780}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:17425712,
CC ECO:0000269|PubMed:17461780}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17425712,
CC ECO:0000269|PubMed:17461780, ECO:0000269|PubMed:18167546}.
CC -!- DISRUPTION PHENOTYPE: Deformed dwarf phenotype and reduced cell
CC adhesion. Hypersensitive to imbalanced C:N ratio.
CC {ECO:0000269|PubMed:17425712, ECO:0000269|PubMed:17461780,
CC ECO:0000269|PubMed:18167546}.
CC -!- MISCELLANEOUS: Co-expressed with the galacturonosyltransferase
CC GAUT8/QUASIMODO1.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012680; AAG52090.1; -; Genomic_DNA.
DR EMBL; AC013430; AAF71804.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36085.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36086.1; -; Genomic_DNA.
DR EMBL; AK230024; BAF01846.1; -; mRNA.
DR RefSeq; NP_001154475.1; NM_001161003.2.
DR RefSeq; NP_177948.3; NM_106474.5.
DR AlphaFoldDB; Q9C9Q8; -.
DR BioGRID; 29379; 1.
DR IntAct; Q9C9Q8; 1.
DR STRING; 3702.AT1G78240.1; -.
DR iPTMnet; Q9C9Q8; -.
DR PaxDb; Q9C9Q8; -.
DR PRIDE; Q9C9Q8; -.
DR ProteomicsDB; 226286; -.
DR EnsemblPlants; AT1G78240.1; AT1G78240.1; AT1G78240.
DR EnsemblPlants; AT1G78240.2; AT1G78240.2; AT1G78240.
DR GeneID; 844160; -.
DR Gramene; AT1G78240.1; AT1G78240.1; AT1G78240.
DR Gramene; AT1G78240.2; AT1G78240.2; AT1G78240.
DR KEGG; ath:AT1G78240; -.
DR Araport; AT1G78240; -.
DR TAIR; locus:2032130; AT1G78240.
DR eggNOG; ENOG502QT31; Eukaryota.
DR HOGENOM; CLU_010485_2_3_1; -.
DR InParanoid; Q9C9Q8; -.
DR OMA; QDETAVW; -.
DR OrthoDB; 203361at2759; -.
DR PhylomeDB; Q9C9Q8; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9C9Q8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9Q8; baseline and differential.
DR Genevisible; Q9C9Q8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA: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; IMP:TAIR.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0010289; P:homogalacturonan biosynthetic process; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004159; Put_SAM_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10108; PTHR10108; 1.
DR Pfam; PF03141; Methyltransf_29; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall biogenesis/degradation; Glycoprotein;
KW Golgi apparatus; Membrane; Methyltransferase; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..684
FT /note="Probable pectin methyltransferase QUA2"
FT /id="PRO_0000393240"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..684
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 560
FT /note="N->Y: In osu 1-2; loss of activity."
FT /evidence="ECO:0000269|PubMed:18167546"
SQ SEQUENCE 684 AA; 77897 MW; 9390610BABA8A792 CRC64;
MSMPLQRGIS GVRVSDSSDD LRDSQMKDKT ERARSTENNN LTLRFPFGFL FSNQSSSKHG
GGGENGFSAD PYSARSRHRL MLLFLKISLV LIVVIALAGS FWWTISISTS SRGHVYHNYR
RLQEQLVSDL WDIGEISLGP NRWKELEYCN IESENFVPCF NVSENLALGY SNGDENDRFC
GPGSKQECLE LPPVKYRVPL RWPTGKDIIW HSNVKITAQE VVSSGSITKR MMMMEDDQIS
FRSASPMSDE VEDYSHQIAE MIGIKKDNFI EAGVRTILDI GCGYGSFGAH LLSKQILTMC
IANYEASGSQ VQLTLERGLP AMIGSFISKQ LPYPSLSFDM LHCLRCGIDW DQKDGLLLVE
IDRVLKPGGY FVWTSPLTNP RNKDHLKRWN FVHDFAESIC WTLLNQQDET VVWKKTINTK
CYSSRKPGVG PSVCTKGHDV ESPYYRPLQM CIGGTRSRRW IPIEGRTRWP SRSNMNKTEL
SLYGLHPEVL GEDAENWKIT VREYWSLLSP LIFSDHPKRP GDEDPSPPYN MLRNVLDMNA
QFGGLNSALL EARKSVWVMN VVPTAGPNHL PMILDRGFVG VLHNWCEPFP TYPRTYDLVH
ADNLLSLQTS QPRKTCLLID IFTEIDRLLR PEGWVIIRDT AQLVEKARET ITQLKWEARV
IEVESSSEQR LLICQKPFTK RQSI
