PMTD_ARATH
ID PMTD_ARATH Reviewed; 600 AA.
AC Q93W95; A0A097PKM4; Q9ZPI0;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable pectin methyltransferase QUA3 {ECO:0000305};
DE EC=2.1.1.-;
DE AltName: Full=Protein QUASIMODO 3 {ECO:0000303|PubMed:25249442};
GN Name=QUA3 {ECO:0000303|PubMed:25249442}; Synonyms=PMT13 {ECO:0000305};
GN OrderedLocusNames=At4g00740 {ECO:0000312|Araport:AT4G00740};
GN ORFNames=F15P23.2 {ECO:0000312|EMBL:AAD17338.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE OF 84-588.
RX PubMed=25249442; DOI=10.1038/ncomms5956;
RA Zeng L., Zhang Q., Sun R., Kong H., Zhang N., Ma H.;
RT "Resolution of deep angiosperm phylogeny using conserved nuclear genes and
RT estimates of early divergence times.";
RL Nat. Commun. 5:4956-4956(2014).
RN [5]
RP GENE FAMILY.
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, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND PATHWAY.
RC STRAIN=cv. No-0;
RX PubMed=21725030; DOI=10.1093/jxb/err211;
RA Miao Y., Li H.-Y., Shen J., Wang J., Jiang L.;
RT "QUASIMODO 3 (QUA3) is a putative homogalacturonan methyltransferase
RT regulating cell wall biosynthesis in Arabidopsis suspension-cultured
RT cells.";
RL J. Exp. Bot. 62:5063-5078(2011).
CC -!- FUNCTION: S-adenosyl-L-methionine (SAM)-dependent methyltransferase
CC (MTase) which mediates the methylesterification of the pectin
CC homogalacturonan (HG) and thus regulates cell wall biosynthesis, at
CC least in suspension-cultured cells. {ECO:0000269|PubMed:21725030}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC {ECO:0000305|PubMed:21725030}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21725030}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21725030}.
CC -!- TISSUE SPECIFICITY: Highly expressed and abundant in suspension-
CC cultured cells, but low levels in seedlings.
CC {ECO:0000269|PubMed:21725030}.
CC -!- DISRUPTION PHENOTYPE: In seedlings, no altered phenotypes or changes in
CC pectin methylation (PubMed:21725030). In contrast, suspension-cultured
CC cells exhibit less pectin methylation as well as altered composition
CC and assembly of cell wall polysaccharides (PubMed:21725030).
CC {ECO:0000269|PubMed:21725030}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17338.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80883.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF128392; AAD17338.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80883.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81928.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66439.1; -; Genomic_DNA.
DR EMBL; AY059835; AAL24317.1; -; mRNA.
DR EMBL; AY059913; AAL24395.1; -; mRNA.
DR EMBL; BT000151; AAN15470.1; -; mRNA.
DR EMBL; BT008377; AAP37736.1; -; mRNA.
DR EMBL; KM397924; AIU48586.1; -; mRNA.
DR PIR; B85010; B85010.
DR RefSeq; NP_001328335.1; NM_001340266.1.
DR RefSeq; NP_567184.1; NM_116299.3.
DR AlphaFoldDB; Q93W95; -.
DR BioGRID; 13311; 3.
DR STRING; 3702.AT4G00740.1; -.
DR iPTMnet; Q93W95; -.
DR SwissPalm; Q93W95; -.
DR PaxDb; Q93W95; -.
DR PRIDE; Q93W95; -.
DR ProteomicsDB; 234884; -.
DR EnsemblPlants; AT4G00740.1; AT4G00740.1; AT4G00740.
DR EnsemblPlants; AT4G00740.2; AT4G00740.2; AT4G00740.
DR GeneID; 828020; -.
DR Gramene; AT4G00740.1; AT4G00740.1; AT4G00740.
DR Gramene; AT4G00740.2; AT4G00740.2; AT4G00740.
DR KEGG; ath:AT4G00740; -.
DR Araport; AT4G00740; -.
DR TAIR; locus:2117733; AT4G00740.
DR eggNOG; ENOG502QU6Q; Eukaryota.
DR HOGENOM; CLU_010485_2_2_1; -.
DR InParanoid; Q93W95; -.
DR OMA; KCVSKVS; -.
DR OrthoDB; 357884at2759; -.
DR PhylomeDB; Q93W95; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q93W95; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93W95; baseline and differential.
DR Genevisible; Q93W95; 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; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0052546; P:cell wall pectin metabolic process; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Glycoprotein; Golgi apparatus; Membrane; Methyltransferase;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..600
FT /note="Probable pectin methyltransferase QUA3"
FT /id="PRO_0000393253"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..600
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 382
FT /note="Missing (in Ref. 4; AIU48586)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..521
FT /note="LIKRQ -> IKR (in Ref. 4; AIU48586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 67555 MW; 4145CF8917A1980D CRC64;
MGHVNLPASK RGNPRQWRLL DIVTAAFFGI VLLFFILLFT PLGDSMAASG RQTLLLSTAS
DPRQRQRLVT LVEAGQHLQP IEYCPAEAVA HMPCEDPRRN SQLSREMNFY RERHCPLPEE
TPLCLIPPPS GYKIPVPWPE SLHKIWHANM PYNKIADRKG HQGWMKREGE YFTFPGGGTM
FPGGAGQYIE KLAQYIPLNG GTLRTALDMG CGVASFGGTL LSQGILALSF APRDSHKSQI
QFALERGVPA FVAMLGTRRL PFPAYSFDLM HCSRCLIPFT AYNATYFIEV DRLLRPGGYL
VISGPPVQWP KQDKEWADLQ AVARALCYEL IAVDGNTVIW KKPVGDSCLP SQNEFGLELC
DESVPPSDAW YFKLKRCVTR PSSVKGEHAL GTISKWPERL TKVPSRAIVM KNGLDVFEAD
ARRWARRVAY YRDSLNLKLK SPTVRNVMDM NAFFGGFAAT LASDPVWVMN VIPARKPLTL
DVIYDRGLIG VYHDWCEPFS TYPRTYDFIH VSGIESLIKR QDSSKSRCSL VDLMVEMDRI
LRPEGKVVIR DSPEVLDKVA RMAHAVRWSS SIHEKEPESH GREKILIATK SLWKLPSNSH
