PMTO_ARATH
ID PMTO_ARATH Reviewed; 770 AA.
AC Q6NPR7; Q0WUW9; Q9C7Q4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable methyltransferase PMT24;
DE EC=2.1.1.-;
GN OrderedLocusNames=At1g29470; ORFNames=F15D2.5;
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;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [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: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC068667; AAG51752.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31093.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31094.1; -; Genomic_DNA.
DR EMBL; BT010751; AAR23721.1; -; mRNA.
DR EMBL; AK227015; BAE99079.1; -; mRNA.
DR PIR; E86417; E86417.
DR RefSeq; NP_001031109.1; NM_001036032.1.
DR RefSeq; NP_174240.2; NM_102687.4.
DR AlphaFoldDB; Q6NPR7; -.
DR STRING; 3702.AT1G29470.1; -.
DR PaxDb; Q6NPR7; -.
DR PRIDE; Q6NPR7; -.
DR ProteomicsDB; 234886; -.
DR EnsemblPlants; AT1G29470.1; AT1G29470.1; AT1G29470.
DR EnsemblPlants; AT1G29470.2; AT1G29470.2; AT1G29470.
DR GeneID; 839823; -.
DR Gramene; AT1G29470.1; AT1G29470.1; AT1G29470.
DR Gramene; AT1G29470.2; AT1G29470.2; AT1G29470.
DR KEGG; ath:AT1G29470; -.
DR Araport; AT1G29470; -.
DR TAIR; locus:2013628; AT1G29470.
DR eggNOG; ENOG502QTUG; Eukaryota.
DR HOGENOM; CLU_010485_1_2_1; -.
DR InParanoid; Q6NPR7; -.
DR OMA; NLGENHA; -.
DR OrthoDB; 325808at2759; -.
DR PhylomeDB; Q6NPR7; -.
DR PRO; PR:Q6NPR7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NPR7; baseline and differential.
DR Genevisible; Q6NPR7; 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:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
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..770
FT /note="Probable methyltransferase PMT24"
FT /id="PRO_0000393264"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..770
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 54..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 310
FT /note="I -> T (in Ref. 4; BAE99079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 87205 MW; 6B3E128132554EB0 CRC64;
MAMGKYSRVD GKKSSGYGLT ITIVLIVSLC LVGAWMFMSS WSAPTESIDF SANERTKDVD
TTKSDFKSEE VDRGSKSFPD EKNEETEVVT ETNEEKTDPE KSGEENSGEK TESAEERKEF
DDKNGDGDRK NGDGEKDTES ESDETKQKEK TQLEESSEEN KSEDSNGTEE NAGESEENTE
KKSEENAGET EESTEKSKDV FPAGDQAEIT KESSTGSGAW STQLVESQNE KKAQVSSIKW
KVCNVTAGPD YIPCLDNWQA IRKLHSTKHY EHRERHCPEE SPRCLVSLPE GYKRSIKWPK
SREKIWYTNI PHTKLAEVKG HQNWVKMSGE YLTFPGGGTQ FKNGALHYID FLQESYPDIA
WGNRTRVILD VGCGVASFGG YLFDRDVLAL SFAPKDEHEA QVQFALERGI PAMSNVMGTK
RLPFPGSVFD LIHCARCRVP WHIEGGKLLL ELNRALRPGG FFVWSATPVY RKTEEDVGIW
KAMSKLTKAM CWELMTIKKD ELNEVGAAIY QKPMSNKCYN ERSQNEPPLC KDSDDQNAAW
NVPLEACIHK VTEDSSKRGA VWPESWPERV ETVPQWLDSQ EGVYGKPAQE DFTADHERWK
TIVSKSYLNG MGIDWSYVRN VMDMRAVYGG FAAALKDLKL WVMNVVPIDS PDTLPIIYER
GLFGIYHDWC ESFSTYPRTY DLLHADHLFS SLKKRCNLVG VMAEVDRILR PQGTFIVRDD
METIGEIEKM VKSMKWNVRM THSKDGEGLL SVQKSWWRPT EAETIQSAIA
