PMTR_ARATH
ID PMTR_ARATH Reviewed; 895 AA.
AC Q9SD39;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable methyltransferase PMT27;
DE EC=2.1.1.-;
GN OrderedLocusNames=At3g51070; ORFNames=F24M12.110;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 -!- MISCELLANEOUS: This gene overlaps with At3g51075, a potential natural
CC antisense gene.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL132980; CAB62629.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78746.1; -; Genomic_DNA.
DR PIR; T45738; T45738.
DR RefSeq; NP_190676.1; NM_114967.2.
DR AlphaFoldDB; Q9SD39; -.
DR STRING; 3702.AT3G51070.1; -.
DR PaxDb; Q9SD39; -.
DR PRIDE; Q9SD39; -.
DR ProteomicsDB; 234988; -.
DR EnsemblPlants; AT3G51070.1; AT3G51070.1; AT3G51070.
DR GeneID; 824271; -.
DR Gramene; AT3G51070.1; AT3G51070.1; AT3G51070.
DR KEGG; ath:AT3G51070; -.
DR Araport; AT3G51070; -.
DR TAIR; locus:2080823; AT3G51070.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR HOGENOM; CLU_010485_1_1_1; -.
DR InParanoid; Q9SD39; -.
DR OMA; QNKPPMC; -.
DR OrthoDB; 325808at2759; -.
DR PhylomeDB; Q9SD39; -.
DR PRO; PR:Q9SD39; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD39; differential.
DR Genevisible; Q9SD39; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 2.
DR Pfam; PF03141; Methyltransf_29; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Methyltransferase;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..895
FT /note="Probable methyltransferase PMT27"
FT /id="PRO_0000393267"
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..895
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 43..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 895 AA; 101444 MW; 42C841E8BBDFED1E CRC64;
MAFGRGRGNK RTSTSSYAST ITMVIFVALC VFGVWMLSSN SVIPPQITQG STRAAVAETE
RSDVSASSNG NDEPEPTKQE SDEQQAFEDN PGKLPDDAVK SEDEQRKSAK EKSETTSSKT
QTQETQQNND DKISEEKEKD NGKENQTVQE SEEGQMKKVV KEFEKEQKQQ RDEDAGTQPK
GTQGQEQGQG KEQPDVEQGN KQGQEQDSNT DVTFTDATKQ EQPMETGQGE TSETSKNEEN
GQPEEQNSGN EETGQQNEEK TTASEENGKG EKSMKDENGQ QEEHTTAEEE SGNKEEESTS
KDENMEQQEE RKDEKKHEQG SEASGFGSGI PKESAESQKS WKSQATESKD EKQRQTSESN
TVERIMDGNA WVLCNATAGT DYIPCLDNEE AIMKLRSRRH FEHRERHCPE DPPTCLVPLP
EGYKEAIKWP ESRDKIWYHN VPHTKLAEVK GHQNWVKVTG EFLTFPGGGT QFIHGALHYI
DFLQQSLKNI AWGKRTRVIL DVGCGVASFG GFLFERDVIA MSLAPKDEHE AQVQFALERK
IPAISAVMGS KRLPFPSRVF DLIHCARCRV PWHNEGGMLL LELNRMLRPG GYFVWSATPV
YQKLEEDVQI WKEMSALTKS LCWELVTINK DKLNGIGAAI YQKPATNECY EKRKHNKPPL
CKNNDDANAA WYVPLQACMH KVPTNVVERG SKWPVNWPRR LQTPPYWLNS SQMGIYGKPA
PRDFTTDYEH WKHVVSKVYM NEIGISWSNV RNVMDMRAVY GGFAAALKDL QVWVMNVVNI
NSPDTLPIIY ERGLFGIYHD WCESFSTYPR SYDLLHADHL FSKLRTRCNL VPVMAEVDRI
VRPGGKLIVR DESNVIREVE NMLKSLHWDV HLTFSKHQEG ILSAQKGFWR PETSQ
