TOM1_TOBAC
ID TOM1_TOBAC Reviewed; 288 AA.
AC Q402F4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Tobamovirus multiplication protein 1;
DE Short=NtTOM1;
GN Name=TOM1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP BIOTECHNOLOGY.
RC STRAIN=cv. Samsun;
RX PubMed=16081069; DOI=10.1016/j.febslet.2005.07.021;
RA Asano M., Satoh R., Mochizuki A., Tsuda S., Yamanaka T., Nishiguchi M.,
RA Hirai K., Meshi T., Naito S., Ishikawa M.;
RT "Tobamovirus-resistant tobacco generated by RNA interference directed
RT against host genes.";
RL FEBS Lett. 579:4479-4484(2005).
RN [2]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=cv. Bright Yellow 2;
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:16081069}.
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:12514140}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12514140};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12514140}.
CC -!- DISRUPTION PHENOTYPE: Reduced efficiency of intracellular
CC multiplication of tobamoviruses (e.g. TMV-L, ToMV, PMMoV, and TMGMV),
CC characterized by a reduced accumulation of viral coat protein (CP) and
CC reduced amplification of TMV-related RNAs.
CC {ECO:0000269|PubMed:16081069}.
CC -!- BIOTECHNOLOGY: TOM1 inhibition via RNA interference constitutes a
CC useful method for generating tobamovirus-resistant plants.
CC {ECO:0000269|PubMed:16081069}.
CC -!- SIMILARITY: Belongs to the plant tobamovirus multiplication TOM1
CC protein family. {ECO:0000305}.
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DR EMBL; AB193039; BAE43836.1; -; mRNA.
DR AlphaFoldDB; Q402F4; -.
DR SMR; Q402F4; -.
DR STRING; 4097.Q402F4; -.
DR PhylomeDB; Q402F4; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0046786; P:viral replication complex formation and maintenance; IDA:UniProtKB.
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..288
FT /note="Tobamovirus multiplication protein 1"
FT /id="PRO_0000423672"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 288 AA; 32748 MW; 0FCDBEEABBF114BC CRC64;
MTRLPLGSSS IDIAGPTTNW WDQINESVQW QDGIFYSLCA SYALVSAVAL IQLIRIELRV
PEYGWTTQKV FHLMNFVVNG VRAIVFGFHK QVFLFHPKVL SLAILDLPGL LFFSTFTLLV
LFWAEIYHQA RSLPTDKLRI SYISINGAIY FIQACIWVYL WSNDNSTVEF IGKIFIAVVS
FIAALGFLLY GGRLFLMLRR FPIESKGRRK KLHEVGSVTA ICFTCFLISC FVVVLSAFDP
DASLDVLDHP VLNLIYYLLV EILPSALVLY ILRKLPPKRV SAQYHPIS
