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TOM2A_ARATH
ID   TOM2A_ARATH             Reviewed;         280 AA.
AC   Q9C5W7; Q56Z79; Q9LQL8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Tobamovirus multiplication protein 2A;
DE            Short=AtTOM2A;
GN   Name=TOM2A; OrderedLocusNames=At1g32400; ORFNames=F5D14.22;
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, INTERACTION
RP   WITH TOM1, SUBUNIT, AND TOPOLOGY.
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   [2]
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   [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   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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-280.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9568044; DOI=10.1006/viro.1998.9078;
RA   Ohshima K., Taniyama T., Yamanaka T., Ishikawa M., Naito S.;
RT   "Isolation of a mutant of Arabidopsis thaliana carrying two simultaneous
RT   mutations affecting tobacco mosaic virus multiplication within a single
RT   cell.";
RL   Virology 243:472-481(1998).
RN   [8]
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).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18474569; DOI=10.1099/vir.0.2008/000539-0;
RA   Fujisaki K., Kobayashi S., Tsujimoto Y., Naito S., Ishikawa M.;
RT   "Analysis of tobamovirus multiplication in Arabidopsis thaliana mutants
RT   defective in TOM2A homologues.";
RL   J. Gen. Virol. 89:1519-1524(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 AND SER-233, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: Necessary for the efficient intracellular multiplication of
CC       tobamoviruses, being a component of the replication complex.
CC       {ECO:0000269|PubMed:12514139, ECO:0000269|PubMed:18474569,
CC       ECO:0000269|PubMed:9568044}.
CC   -!- SUBUNIT: Homodimer. Constituent of tobamovirus replication complex.
CC       Interacts with TOM1. {ECO:0000269|PubMed:12514139}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12514140};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in rosette leaves.
CC       {ECO:0000269|PubMed:18474569}.
CC   -!- DISRUPTION PHENOTYPE: Reduced efficiency of intracellular
CC       multiplication of tobamoviruses (e.g. crucifer strain TMV-Cg),
CC       characterized by a reduced amplification of TMV-related RNAs.
CC       {ECO:0000269|PubMed:12514139, ECO:0000269|PubMed:18474569,
CC       ECO:0000269|PubMed:9568044}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF81337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB085684; BAC24019.1; -; mRNA.
DR   EMBL; AC007767; AAF81337.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31476.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31477.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31478.1; -; Genomic_DNA.
DR   EMBL; AF334723; AAG50101.1; -; mRNA.
DR   EMBL; AF385687; AAK60280.1; -; mRNA.
DR   EMBL; AY088560; AAM66092.1; -; mRNA.
DR   EMBL; AK221090; BAD94952.1; -; mRNA.
DR   PIR; A86449; A86449.
DR   RefSeq; NP_001031127.1; NM_001036050.2.
DR   RefSeq; NP_564399.1; NM_102974.5.
DR   RefSeq; NP_973952.1; NM_202223.3.
DR   AlphaFoldDB; Q9C5W7; -.
DR   BioGRID; 25367; 3.
DR   IntAct; Q9C5W7; 1.
DR   STRING; 3702.AT1G32400.3; -.
DR   iPTMnet; Q9C5W7; -.
DR   SwissPalm; Q9C5W7; -.
DR   PaxDb; Q9C5W7; -.
DR   PRIDE; Q9C5W7; -.
DR   ProMEX; Q9C5W7; -.
DR   ProteomicsDB; 234322; -.
DR   EnsemblPlants; AT1G32400.1; AT1G32400.1; AT1G32400.
DR   EnsemblPlants; AT1G32400.2; AT1G32400.2; AT1G32400.
DR   EnsemblPlants; AT1G32400.3; AT1G32400.3; AT1G32400.
DR   GeneID; 840133; -.
DR   Gramene; AT1G32400.1; AT1G32400.1; AT1G32400.
DR   Gramene; AT1G32400.2; AT1G32400.2; AT1G32400.
DR   Gramene; AT1G32400.3; AT1G32400.3; AT1G32400.
DR   KEGG; ath:AT1G32400; -.
DR   Araport; AT1G32400; -.
DR   TAIR; locus:2033718; AT1G32400.
DR   eggNOG; ENOG502QRDH; Eukaryota.
DR   HOGENOM; CLU_055730_0_0_1; -.
DR   InParanoid; Q9C5W7; -.
DR   OMA; NICCLSC; -.
DR   OrthoDB; 1180379at2759; -.
DR   PhylomeDB; Q9C5W7; -.
DR   PRO; PR:Q9C5W7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C5W7; baseline and differential.
DR   Genevisible; Q9C5W7; AT.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISS:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0046786; P:viral replication complex formation and maintenance; IMP:TAIR.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   PANTHER; PTHR19282; PTHR19282; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..280
FT                   /note="Tobamovirus multiplication protein 2A"
FT                   /id="PRO_0000423674"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..280
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          258..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   280 AA;  31556 MW;  227C8FE0658A8C0C CRC64;
     MACRGCLECL LKLLNFLLAV AGLGMIGYGI YLFVEYKRVT DNSVTFDLTN GDQSYVSFGR
     PILMAVSLSS NIFDNLPKAW FIYLFIGIGV ALFVISCCGC VGTCSRSVCC LSCYSLLLIL
     LILVELGFAA FIFFDNSWRD ELPSDRTGNF DTIYNFLREN WKIVRWVALG AVVFEALLFL
     LALMVRAANT PAEYDSDDEY LAPRQQIRQP FINRQAAPVT GVPVAPTLDQ RPSRSDPWSA
     RMREKYGLDT SEFTYNPSES HRFQQMPAQP NEEKGRCTIM
 
 
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