PMTS_ARATH
ID PMTS_ARATH Reviewed; 724 AA.
AC Q9LN50;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable methyltransferase PMT28;
DE EC=2.1.1.-;
GN OrderedLocusNames=At1g19430; ORFNames=F18O14.20;
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].
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 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: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AC025808; AAF79446.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29851.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60983.1; -; Genomic_DNA.
DR EMBL; AY056127; AAL07206.1; -; mRNA.
DR EMBL; BT001953; AAN71952.1; -; mRNA.
DR RefSeq; NP_001323230.1; NM_001332395.1.
DR RefSeq; NP_564084.1; NM_101799.2.
DR AlphaFoldDB; Q9LN50; -.
DR SMR; Q9LN50; -.
DR STRING; 3702.AT1G19430.1; -.
DR PaxDb; Q9LN50; -.
DR PRIDE; Q9LN50; -.
DR ProteomicsDB; 226285; -.
DR EnsemblPlants; AT1G19430.1; AT1G19430.1; AT1G19430.
DR EnsemblPlants; AT1G19430.3; AT1G19430.3; AT1G19430.
DR GeneID; 838527; -.
DR Gramene; AT1G19430.1; AT1G19430.1; AT1G19430.
DR Gramene; AT1G19430.3; AT1G19430.3; AT1G19430.
DR KEGG; ath:AT1G19430; -.
DR Araport; AT1G19430; -.
DR TAIR; locus:2016392; AT1G19430.
DR eggNOG; ENOG502QRYM; Eukaryota.
DR HOGENOM; CLU_010485_2_4_1; -.
DR InParanoid; Q9LN50; -.
DR OMA; KGGIQHY; -.
DR OrthoDB; 421114at2759; -.
DR PhylomeDB; Q9LN50; -.
DR PRO; PR:Q9LN50; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LN50; baseline and differential.
DR Genevisible; Q9LN50; 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; 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; 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 Glycoprotein; Golgi apparatus; Membrane; Methyltransferase;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..724
FT /note="Probable methyltransferase PMT28"
FT /id="PRO_0000393268"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..724
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 63..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 724 AA; 82662 MW; 569F71B8D314DEAE CRC64;
MMERKREMGI AYFARRIKQP RGIWVKMTFI VVLGLCFVFF WSFLSSSAST FNVQRESFDD
IAEPVSSRTK SAHEVSESSK LHERGKVESG SKSKEGKKVG GSSVHKHETK KKKEHAVSHP
HKKKDVPKPV VEEVVVKEDQ EHEEAESDDS DQSNKEDGEE GTESDGNEGE SDGNGDGSVD
DSSASVDEEV EEKNEEVTVN EISKKRKRKG PVFDPKAEYS WRLCNTRSKH NYMPCIDNDG
LIGRLQSYRH RERSCPKKPV MCLVPLPHDG YDPPVSWPES KSKILYKNVA HPKLAAYIKK
HNWVNETGEY LSFPQNQTTF NGNVLQYLEF IQEMVPDIEW GKNVRIVLDI GCSDSSFVAA
LLDKDVLTVS LGLKDDLVDL AQVALERGFP TFVSSLASRR LPFPSGVFDT IHCAACGVHW
HSHGGKLLLE MNRILRPNGY FILSSNNDKI EDDEAMTALT ASICWNILAH KTEEASEMGV
RIYQKPESND IYELRRKKNP PLCEDNENPD AAWYVPMKTC IYEIPSAIEQ HGAEWPEEWP
KRLETYPEWL TSKEKAMEDT NHWNAMVNKS YLTGLGIDWL HIRNVMDMTA IYGGFGASLV
KQNVWVMNVV PVHSPDTLPF IYERGLLGIY HDWCEPFGTY PRSYDLLHAD HLFSRLKNRC
KQPASIVVEM DRLTRPGGWV VVRDKVEILE PLEEILRSLH WEIRMTYAQD KEGMLCAQKT
LWRP
