TOL2_ARATH
ID TOL2_ARATH Reviewed; 383 AA.
AC Q9LNC6; F4IC14;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=TOM1-like protein 2 {ECO:0000305};
GN Name=TOL2 {ECO:0000303|PubMed:24316203};
GN Synonyms=TOM1E {ECO:0000303|PubMed:22639582};
GN OrderedLocusNames=At1g06210 {ECO:0000312|Araport:AT1G06210};
GN ORFNames=F9P14.7 {ECO:0000312|EMBL:AAF80218.1};
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP GENE FAMILY, AND REVIEW.
RX PubMed=16488176; DOI=10.1016/j.tplants.2006.01.008;
RA Winter V., Hauser M.-T.;
RT "Exploring the ESCRTing machinery in eukaryotes.";
RL Trends Plant Sci. 11:115-123(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-378, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-378, 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).
RN [9]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
RX PubMed=22639582; DOI=10.3389/fpls.2011.00020;
RA Richardson L.G., Howard A.S., Khuu N., Gidda S.K., McCartney A.,
RA Morphy B.J., Mullen R.T.;
RT "Protein-protein interaction network and subcellular localization of the
RT Arabidopsis thaliana ESCRT machinery.";
RL Front. Plant Sci. 2:20-20(2011).
RN [10]
RP GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX PubMed=24316203; DOI=10.1016/j.cub.2013.10.036;
RA Korbei B., Moulinier-Anzola J., De-Araujo L., Lucyshyn D., Retzer K.,
RA Khan M.A., Luschnig C.;
RT "Arabidopsis TOL proteins act as gatekeepers for vacuolar sorting of PIN2
RT plasma membrane protein.";
RL Curr. Biol. 23:2500-2505(2013).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=24699223; DOI=10.4161/psb.28667;
RA Moulinier-Anzola J., De-Araujo L., Korbei B.;
RT "Expression of Arabidopsis TOL genes.";
RL Plant Signal. Behav. 9:E28667-E28667(2014).
CC -!- FUNCTION: Binds ubiquitin in vitro (PubMed:24316203). Might contribute
CC to the loading of the ESCRT machinery (Probable).
CC {ECO:0000269|PubMed:24316203, ECO:0000305|PubMed:16488176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22639582}. Membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LNC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LNC6-2; Sequence=VSP_058983, VSP_058984;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:24699223}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC025290; AAF80218.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27960.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27959.1; -; Genomic_DNA.
DR EMBL; AY052723; AAK96627.1; -; mRNA.
DR EMBL; BT000578; AAN18147.1; -; mRNA.
DR EMBL; BX816443; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; G86197; G86197.
DR RefSeq; NP_563762.1; NM_100502.4. [Q9LNC6-1]
DR RefSeq; NP_973770.1; NM_202041.2. [Q9LNC6-2]
DR AlphaFoldDB; Q9LNC6; -.
DR SMR; Q9LNC6; -.
DR STRING; 3702.AT1G06210.1; -.
DR iPTMnet; Q9LNC6; -.
DR PaxDb; Q9LNC6; -.
DR PRIDE; Q9LNC6; -.
DR ProteomicsDB; 232432; -. [Q9LNC6-1]
DR EnsemblPlants; AT1G06210.1; AT1G06210.1; AT1G06210. [Q9LNC6-1]
DR EnsemblPlants; AT1G06210.2; AT1G06210.2; AT1G06210. [Q9LNC6-2]
DR GeneID; 837130; -.
DR Gramene; AT1G06210.1; AT1G06210.1; AT1G06210. [Q9LNC6-1]
DR Gramene; AT1G06210.2; AT1G06210.2; AT1G06210. [Q9LNC6-2]
DR KEGG; ath:AT1G06210; -.
DR Araport; AT1G06210; -.
DR TAIR; locus:2038545; AT1G06210.
DR eggNOG; KOG1087; Eukaryota.
DR InParanoid; Q9LNC6; -.
DR OMA; NWSLNLR; -.
DR OrthoDB; 1213216at2759; -.
DR PhylomeDB; Q9LNC6; -.
DR PRO; PR:Q9LNC6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNC6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:InterPro.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR044836; TOL_plant.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR46646; PTHR46646; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..383
FT /note="TOM1-like protein 2"
FT /id="PRO_0000440677"
FT DOMAIN 45..178
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 223..310
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 305..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 257..279
FT /note="DDLTVSLMEKCKQSQPLIQMIIE -> VVATLSAHLTFVIFLNKCLWNMD
FT (in isoform 2)"
FT /id="VSP_058983"
FT VAR_SEQ 280..383
FT /note="Missing (in isoform 2)"
FT /id="VSP_058984"
SQ SEQUENCE 383 AA; 42797 MW; 26BE6EB7B897F887 CRC64;
MDKLKIAEWG EKLKTGGAQM SRMVSEKVKD MLQAPTLESK MVDEATLETL EEPNWGMNMR
ICAQINNDEF NGTEIVRAIK RKISGKSPVS QRLSLELLEA CAMNCEKVFS EVASEKVLDE
MVWLIKNGEA DSENRKRAFQ LIRAWGQSQD LTYLPVFHQT YMSLEGENGL HARGEENSMP
GQSSLESLMQ RPVPVPPPGS YPVPNQEQAL GDDDGLDYNF GNLSIKDKKE QIEITRNSLE
LLSSMLNTEG KPNHTEDDLT VSLMEKCKQS QPLIQMIIES TTDDEGVLFE ALHLNDELQQ
VLSSYKKPDE TEKKASIVEQ ESSGSKDTGP KPTEQEEQEP VKKTGADDDK KHSEASGSSN
KTVKEEKQAV KIELGLSSDE DEK
