PMT7_ARATH
ID PMT7_ARATH Reviewed; 600 AA.
AC Q9LZA4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable methyltransferase PMT7;
DE EC=2.1.1.-;
GN OrderedLocusNames=At5g04060; ORFNames=F21E1.1, F8F6.270;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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; AL162873; CAB85526.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90692.1; -; Genomic_DNA.
DR EMBL; AY072008; AAL57703.1; -; mRNA.
DR PIR; T48433; T48433.
DR RefSeq; NP_196026.1; NM_120488.4.
DR AlphaFoldDB; Q9LZA4; -.
DR STRING; 3702.AT5G04060.1; -.
DR PaxDb; Q9LZA4; -.
DR PRIDE; Q9LZA4; -.
DR ProteomicsDB; 226152; -.
DR EnsemblPlants; AT5G04060.1; AT5G04060.1; AT5G04060.
DR GeneID; 830285; -.
DR Gramene; AT5G04060.1; AT5G04060.1; AT5G04060.
DR KEGG; ath:AT5G04060; -.
DR Araport; AT5G04060; -.
DR TAIR; locus:2150670; AT5G04060.
DR eggNOG; ENOG502QTJJ; Eukaryota.
DR HOGENOM; CLU_010485_2_3_1; -.
DR InParanoid; Q9LZA4; -.
DR OMA; AMSSYPV; -.
DR OrthoDB; 362552at2759; -.
DR PhylomeDB; Q9LZA4; -.
DR PRO; PR:Q9LZA4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZA4; baseline and differential.
DR Genevisible; Q9LZA4; 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: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..600
FT /note="Probable methyltransferase PMT7"
FT /id="PRO_0000393247"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..600
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 600 AA; 68357 MW; 39E0CAC1FA7B201D CRC64;
MGGGYVLFGS ARSGQMIMVA LVLMVGSFYA GSIFGNNSPI YISQPSSSNS SSSSPSQSGP
SNFANKIELT YRRTSVSIPE SGVNVCPLKF NEYIPCHNVT YVQQLLPSLN LSRREELERH
CPPLEQRLFC LVPPPKDYKI PIRWPTSRDY VWRSNVNHTH LAEVKGGQNW VHEQGQLWWF
PGGGTHFKHG APEYIQRLGN MTTNETGDLL SAGVEQVLDV GCGVASFAAY LLPLGIKTMS
FAPKDGHENQ IQFALERGIR AMISAIATKQ MPYPAASFDM VHCSRCRVDW HENDGVLMKE
VNRLLRPNGY FVYSAPPAYR KDKDFPVIWD KLVNLTSAMC WKLISRKVQT AIWVKEDDEA
CLRKNAELEL ITICGVEDVS KASWKVPLRD CVDISENRQQ KPSSLTDRLS SYPTSLREKG
ISEDEFTLDT NFWREQVNQY WELMNVNKTE VRNVMDTNAF IGGFAAAMNS YPLWVMNVVP
ATMNDTLSGI YQRGLTGAYH DWCEPFSTYP RTYDLLHADH LFTHYKIYGE GCLLEDIMLE
MDRIIRPQGF IIIRDEESIV SRVRDLAPKF LWEVEAHELQ DKYKKTETVL FCRKKFWAIL
