PMTL_ARATH
ID PMTL_ARATH Reviewed; 600 AA.
AC Q94II3; O49670;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable methyltransferase PMT21;
DE EC=2.1.1.-;
DE AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 3;
GN Name=ERD3; OrderedLocusNames=At4g19120; ORFNames=T18B16.90;
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], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8075396; DOI=10.1007/bf00028874;
RA Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
RT "Cloning of cDNAs for genes that are early-responsive to dehydration stress
RT (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP
RT cognate genes.";
RL Plant Mol. Biol. 25:791-798(1994).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- INDUCTION: By dehydration stress. {ECO:0000269|PubMed:8075396}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16701.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB039927; BAB63914.1; -; mRNA.
DR EMBL; AL021687; CAA16701.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78914.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84145.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84146.1; -; Genomic_DNA.
DR EMBL; AK317548; BAH20212.1; -; mRNA.
DR EMBL; AK317670; BAH20330.1; -; mRNA.
DR PIR; A85216; A85216.
DR PIR; T04433; T04433.
DR RefSeq; NP_567575.1; NM_118031.4.
DR RefSeq; NP_849408.1; NM_179077.2.
DR AlphaFoldDB; Q94II3; -.
DR STRING; 3702.AT4G19120.1; -.
DR PaxDb; Q94II3; -.
DR PRIDE; Q94II3; -.
DR ProteomicsDB; 234690; -.
DR EnsemblPlants; AT4G19120.1; AT4G19120.1; AT4G19120.
DR EnsemblPlants; AT4G19120.2; AT4G19120.2; AT4G19120.
DR GeneID; 827650; -.
DR Gramene; AT4G19120.1; AT4G19120.1; AT4G19120.
DR Gramene; AT4G19120.2; AT4G19120.2; AT4G19120.
DR KEGG; ath:AT4G19120; -.
DR Araport; AT4G19120; -.
DR TAIR; locus:2134756; AT4G19120.
DR eggNOG; ENOG502QQA9; Eukaryota.
DR HOGENOM; CLU_010485_2_2_1; -.
DR InParanoid; Q94II3; -.
DR OMA; NFERKEC; -.
DR OrthoDB; 312524at2759; -.
DR PhylomeDB; Q94II3; -.
DR PRO; PR:Q94II3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94II3; baseline and differential.
DR Genevisible; Q94II3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Endoplasmic reticulum; Glycoprotein; Membrane; Methyltransferase;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..600
FT /note="Probable methyltransferase PMT21"
FT /id="PRO_0000393261"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..600
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 68331 MW; 09D5C525EB070401 CRC64;
MKYKDEKYEK AEKGSRILPK TVLLILLCGL SFYLGGLYCG KNIIEVSDVA KAESSSLDVD
DSLQVKSVSF SECSSDYQDY TPCTDPRKWK KYGTHRLTFM ERHCPPVFDR KQCLVPPPDG
YKPPIRWPKS KDECWYRNVP YDWINKQKSN QNWLRKEGEK FIFPGGGTMF PHGVSAYVDL
MQDLIPEMKD GTIRTAIDTG CGVASWGGDL LDRGILTVSL APRDNHEAQV QFALERGIPA
ILGIISTQRL PFPSNSFDMA HCSRCLIPWT EFGGVYLLEV HRILRPGGFW VLSGPPVNYE
NRWKGWDTTI EEQRSNYEKL QELLSSMCFK MYAKKDDIAV WQKSPDNLCY NKLSNDPDAY
PPKCDDSLEP DSAWYTPLRP CVVVPSPKLK KTDLESTPKW PERLHTTPER ISDVPGGNGN
VFKHDDSKWK TRAKHYKKLL PAIGSDKIRN VMDMNTAYGG LAAALVNDPL WVMNVVSSYA
ANTLPVVFDR GLIGTYHDWC EAFSTYPRTY DLLHVDGLFT SESQRCDMKY VMLEMDRILR
PSGYAIIRES SYFADSIASV AKELRWSCRK EQTESASANE KLLICQKKLW YSSNASSETN
