TOM1_ARATH
ID TOM1_ARATH Reviewed; 291 AA.
AC Q9FEG2; Q9SVR8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Tobamovirus multiplication protein 1;
DE Short=AtTOM1;
GN Name=TOM1; Synonyms=PD114; OrderedLocusNames=At4g21790;
GN ORFNames=F17L22.250;
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, SUBUNIT, AND TOPOLOGY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=10944200; DOI=10.1073/pnas.170295097;
RA Yamanaka T., Ohta T., Takahashi M., Meshi T., Schmidt R., Dean C.,
RA Naito S., Ishikawa M.;
RT "TOM1, an Arabidopsis gene required for efficient multiplication of a
RT tobamovirus, encodes a putative transmembrane protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10107-10112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8350399; DOI=10.1128/jvi.67.9.5328-5338.1993;
RA Ishikawa M., Naito S., Ohno T.;
RT "Effects of the tom1 mutation of Arabidopsis thaliana on the multiplication
RT of tobacco mosaic virus RNA in protoplasts.";
RL J. Virol. 67:5328-5338(1993).
RN [6]
RP INTERACTION WITH TOM2A.
RX PubMed=12514139; DOI=10.1093/emboj/cdg034;
RA Tsujimoto Y., Numaga T., Ohshima K., Yano M.A., Ohsawa R., Goto D.B.,
RA Naito S., Ishikawa M.;
RT "Arabidopsis TOBAMOVIRUS MULTIPLICATION (TOM) 2 locus encodes a
RT transmembrane protein that interacts with TOM1.";
RL EMBO J. 22:335-343(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12514140; DOI=10.1093/emboj/cdg033;
RA Hagiwara Y., Komoda K., Yamanaka T., Tamai A., Meshi T., Funada R.,
RA Tsuchiya T., Naito S., Ishikawa M.;
RT "Subcellular localization of host and viral proteins associated with
RT tobamovirus RNA replication.";
RL EMBO J. 22:344-353(2003).
CC -!- FUNCTION: Necessary for the efficient intracellular multiplication of
CC tobamoviruses, probably being a membrane anchor promoting the formation
CC of the replication complex. {ECO:0000269|PubMed:10944200,
CC ECO:0000269|PubMed:8350399}.
CC -!- SUBUNIT: Constituent of tobamovirus replication complex. Interacts with
CC TOM2A and with the helicase domain of tobamovirus-encoded replication
CC proteins. {ECO:0000269|PubMed:10944200, ECO:0000269|PubMed:12514139}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10944200,
CC ECO:0000269|PubMed:12514140}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10944200, ECO:0000269|PubMed:12514140}.
CC -!- DISRUPTION PHENOTYPE: Reduced efficiency of intracellular
CC multiplication of tobamoviruses (e.g. crucifer strain TMV-Cg),
CC characterized by a reduced accumulation of viral coat protein (CP) and
CC reduced amplification of TMV-related RNAs.
CC {ECO:0000269|PubMed:10944200, ECO:0000269|PubMed:8350399}.
CC -!- SIMILARITY: Belongs to the plant tobamovirus multiplication TOM1
CC protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81286.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016924; BAB12401.1; -; Genomic_DNA.
DR EMBL; AB016925; BAB12402.1; -; mRNA.
DR EMBL; AL035527; CAB36823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81286.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84503.1; -; Genomic_DNA.
DR EMBL; AY046049; AAK76723.1; -; mRNA.
DR EMBL; AY079319; AAL85050.1; -; mRNA.
DR PIR; T05854; T05854.
DR RefSeq; NP_567636.1; NM_118299.4.
DR AlphaFoldDB; Q9FEG2; -.
DR SMR; Q9FEG2; -.
DR BioGRID; 13556; 1.
DR IntAct; Q9FEG2; 1.
DR STRING; 3702.AT4G21790.1; -.
DR PaxDb; Q9FEG2; -.
DR PRIDE; Q9FEG2; -.
DR ProteomicsDB; 234336; -.
DR EnsemblPlants; AT4G21790.1; AT4G21790.1; AT4G21790.
DR GeneID; 828267; -.
DR Gramene; AT4G21790.1; AT4G21790.1; AT4G21790.
DR KEGG; ath:AT4G21790; -.
DR Araport; AT4G21790; -.
DR TAIR; locus:2119088; AT4G21790.
DR eggNOG; ENOG502QQMF; Eukaryota.
DR HOGENOM; CLU_059685_0_0_1; -.
DR InParanoid; Q9FEG2; -.
DR OMA; WSQVYYA; -.
DR OrthoDB; 1107947at2759; -.
DR PhylomeDB; Q9FEG2; -.
DR PRO; PR:Q9FEG2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FEG2; baseline and differential.
DR Genevisible; Q9FEG2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0046786; P:viral replication complex formation and maintenance; IMP:TAIR.
DR InterPro; IPR040226; THH1/TOM1/TOM3.
DR InterPro; IPR009457; THH1/TOM1/TOM3_dom.
DR PANTHER; PTHR31142; PTHR31142; 1.
DR Pfam; PF06454; DUF1084; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host-virus interaction; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..291
FT /note="Tobamovirus multiplication protein 1"
FT /id="PRO_0000423669"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..253
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 291 AA; 33009 MW; 0D82BE9E29A54FE7 CRC64;
MTDSGLMMPA EIAGILTTAI TSWWDDVNES TQWQDGIFFA LCGAYALVSA VALVQLIRIQ
MRVPEYGWTT QKVFHLMNFV VNGVRAVLFG FHMQVFLVHP KALCWVLLDL PGLLFFSAYT
LLVLFWAEIY HQARSLPTDK LRITYISVNV AVYLAQIGIW AYIWVHDNST VELVGKIFIA
VVSFIAALGF LLYGGRLFFM LRRFPIESKG RRKKLHEVGS VTAICFTCFL IRCVVVAVSA
FDKDLTLDVL DHPVLNLIYY MVVEVLPSAL VLFILRKLPP KRVSAQYHPI Q
