T112A_ARATH
ID T112A_ARATH Reviewed; 124 AA.
AC Q8LFJ5; Q67ZR1; Q681G4; Q9LME3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Multifunctional methyltransferase subunit TRM112 homolog A {ECO:0000305};
DE AltName: Full=Multifunctional methyltransferase subunit TRM112-like protein At1g22270 {ECO:0000305};
DE AltName: Full=Protein SMALL ORGAN 2 {ECO:0000303|PubMed:19929876};
DE AltName: Full=tRNA methyltransferase 112 homolog A {ECO:0000305};
DE Short=AtTRM112a {ECO:0000303|PubMed:21653555};
GN Name=TRM112A {ECO:0000303|PubMed:21653555};
GN Synonyms=SMO2 {ECO:0000303|PubMed:19929876};
GN OrderedLocusNames=At1g22270 {ECO:0000312|Araport:AT1G22270};
GN ORFNames=T16E15.11 {ECO:0000312|EMBL:AAF87264.1};
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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19929876; DOI=10.1111/j.1365-313x.2009.04085.x;
RA Hu Z., Qin Z., Wang M., Xu C., Feng G., Liu J., Meng Z., Hu Y.;
RT "The Arabidopsis SMO2, a homologue of yeast TRM112, modulates progression
RT of cell division during organ growth.";
RL Plant J. 61:600-610(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH TRM9.
RX PubMed=21653555; DOI=10.1093/nar/gkr406;
RA Leihne V., Kirpekar F., Vaagboe C.B., van den Born E., Krokan H.E.,
RA Grini P.E., Meza T.J., Falnes P.O.;
RT "Roles of Trm9- and ALKBH8-like proteins in the formation of modified
RT wobble uridines in Arabidopsis tRNA.";
RL Nucleic Acids Res. 39:7688-7701(2011).
CC -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein
CC methyltransferases (By similarity). Required for TRM9 tRNA
CC methyltransferase activity (PubMed:21653555). Involved in the
CC regulation of cell division progression during organ growth. Required
CC for the expression of cell cycle-related genes, and the G2-M phase
CC progression during organogenesis (PubMed:19929876).
CC {ECO:0000250|UniProtKB:P53738, ECO:0000269|PubMed:19929876,
CC ECO:0000269|PubMed:21653555}.
CC -!- SUBUNIT: Interacts with TRM9. {ECO:0000269|PubMed:21653555}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf phenotype. Reduced organ growth due to
CC inhibition of cell proliferation. {ECO:0000269|PubMed:19929876}.
CC -!- SIMILARITY: Belongs to the TRM112 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87264.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g22270 has been split into 2 genes: At1g22270 and At1g22275.; Evidence={ECO:0000305};
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DR EMBL; AC068562; AAF87264.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30218.1; -; Genomic_DNA.
DR EMBL; BT006386; AAP21194.1; -; mRNA.
DR EMBL; AK227723; BAE99709.1; -; mRNA.
DR EMBL; AK175143; BAD42906.1; -; mRNA.
DR EMBL; AK175653; BAD43416.1; -; mRNA.
DR EMBL; AK175662; BAD43425.1; -; mRNA.
DR EMBL; AK175824; BAD43587.1; -; mRNA.
DR EMBL; AK176029; BAD43792.1; -; mRNA.
DR EMBL; AK176056; BAD43819.1; -; mRNA.
DR EMBL; AK176229; BAD43992.1; -; mRNA.
DR EMBL; AK176275; BAD44038.1; -; mRNA.
DR EMBL; AY084809; AAM61375.1; -; mRNA.
DR PIR; E86355; E86355.
DR RefSeq; NP_564163.1; NM_102077.5.
DR AlphaFoldDB; Q8LFJ5; -.
DR SMR; Q8LFJ5; -.
DR BioGRID; 24072; 1.
DR IntAct; Q8LFJ5; 1.
DR STRING; 3702.AT1G22270.1; -.
DR PaxDb; Q8LFJ5; -.
DR PRIDE; Q8LFJ5; -.
DR ProteomicsDB; 245268; -.
DR DNASU; 838833; -.
DR EnsemblPlants; AT1G22270.1; AT1G22270.1; AT1G22270.
DR GeneID; 838833; -.
DR Gramene; AT1G22270.1; AT1G22270.1; AT1G22270.
DR KEGG; ath:AT1G22270; -.
DR Araport; AT1G22270; -.
DR TAIR; locus:2196536; AT1G22270.
DR eggNOG; KOG1088; Eukaryota.
DR HOGENOM; CLU_086140_2_0_1; -.
DR InParanoid; Q8LFJ5; -.
DR OMA; NMLTSKC; -.
DR OrthoDB; 1465773at2759; -.
DR PhylomeDB; Q8LFJ5; -.
DR PRO; PR:Q8LFJ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LFJ5; baseline and differential.
DR Genevisible; Q8LFJ5; AT.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0035265; P:organ growth; IMP:TAIR.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:TAIR.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR InterPro; IPR039127; Trm112.
DR InterPro; IPR005651; Trm112-like.
DR PANTHER; PTHR12773; PTHR12773; 1.
DR Pfam; PF03966; Trm112p; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..124
FT /note="Multifunctional methyltransferase subunit TRM112
FT homolog A"
FT /id="PRO_0000215801"
FT DOMAIN 2..120
FT /note="TRM112"
FT CONFLICT 28
FT /note="N -> S (in Ref. 4; BAD43792/BAD43819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13961 MW; 1AB5F7AC8FC55961 CRC64;
MRLITHNMLS CNIKGVTSGF PLRIEAGNVI EKEVDFNPDF IRHMFAKIEW KALVEGARSM
GYAELPEESP DAAVLKSDEP FLKKLHHALL ELHLEEGALV CPETGRKFPV NKGIPNMLLH
EDEV
