ID TOL6_ARATH Reviewed; 671 AA.
AC O80910;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=TOM1-like protein 6 {ECO:0000305};
GN Name=TOL6 {ECO:0000303|PubMed:24316203};
GN Synonyms=TOM1A {ECO:0000303|PubMed:22639582};
GN OrderedLocusNames=At2g38410 {ECO:0000312|Araport:AT2G38410};
GN ORFNames=T19C21.10 {ECO:0000312|EMBL:AAC28763.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-596, 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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
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: Acts as a gatekeeper for degradative protein sorting to the
CC vacuole. Plays a role in recognition of ubiquitinated PIN2 auxin
CC carrier at the plasma membrane and further to its endocytic sorting.
CC Binds ubiquitin in vitro (PubMed:24316203). Might contribute to the
CC loading of the ESCRT machinery (Probable).
CC {ECO:0000269|PubMed:24316203, ECO:0000305|PubMed:16488176}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body
CC {ECO:0000269|PubMed:22639582}. Cytoplasm {ECO:0000269|PubMed:22639582}.
CC Early endosome membrane {ECO:0000269|PubMed:24316203}; Peripheral
CC membrane protein {ECO:0000305}.
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; AC004683; AAC28763.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09534.1; -; Genomic_DNA.
DR EMBL; BT046195; ACI49794.1; -; mRNA.
DR PIR; T02504; T02504.
DR RefSeq; NP_181375.1; NM_129397.3.
DR AlphaFoldDB; O80910; -.
DR SMR; O80910; -.
DR STRING; 3702.O80910; -.
DR iPTMnet; O80910; -.
DR PaxDb; 3702-AT2G38410-1; -.
DR ProteomicsDB; 234442; -.
DR EnsemblPlants; AT2G38410.1; AT2G38410.1; AT2G38410.
DR GeneID; 818422; -.
DR Gramene; AT2G38410.1; AT2G38410.1; AT2G38410.
DR KEGG; ath:AT2G38410; -.
DR Araport; AT2G38410; -.
DR TAIR; AT2G38410; -.
DR eggNOG; KOG1087; Eukaryota.
DR HOGENOM; CLU_026748_2_1_1; -.
DR InParanoid; O80910; -.
DR OMA; CDKVTTN; -.
DR OrthoDB; 620063at2759; -.
DR PhylomeDB; O80910; -.
DR PRO; PR:O80910; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80910; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; 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; IDA:UniProtKB.
DR CDD; cd14231; GAT_GGA-like_plant; 1.
DR CDD; cd03561; VHS; 1.
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; PTHR45898:SF2; TARGET OF MYB PROTEIN 1; 1.
DR PANTHER; PTHR45898; TOM1-LIKE PROTEIN; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..671
FT /note="TOM1-like protein 6"
FT /id="PRO_0000440681"
FT DOMAIN 15..144
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 229..317
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 320..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 671 AA; 72318 MW; 7096EE64AB916B14 CRC64;
MASSSASATV AVDKATSDLL LGPDWTTNME ICDSVNSLHW QAKDVVKAVK KRLQHKSSRV
QLLALTLLET LVKNCGDYLH HQVAEKNILG EMVKIVKKKA DMQVRDKILV MVDSWQQAFG
GPEGKYPQYY WAYDELRRSG VEFPRRSPDA SPIITPPVSH PPLRQPQGGY GVPPAGYGVH
QAGYGVPQAG YGIPQAGYGV PQAGYGIPQV GYGMPSGSSR RLDEAMATEV EGLSLSSIES
MRDVMDLLGD MLQAVDPSDR EAVKDEVIVD LVERCRSNQK KLMQMLTSTG DDELLGRGLD
LNDSLQILLA KHDAIASGSP LPVQASGSPL SVQASKPADS SPKSSEAKDS SSIAGSSSPI
PATVSTGKSP IDEEYEEEED EFAQLARRHS KPPASVTTDP TSLESHNAAS NALALALPDP
PPPVNTTKEQ DMIDLLSITL CTPSTPPAPS SQPSPPPPAG SDQNTHIYPQ PQPRFDSYVA
PWAQQQQPQQ PQAQQGYSQH QQHQQQQGYS QPQHSQQQQG YSQLQQPQPQ QGYSQSQPQA
QVQMQPSTRP QNPYEYPPPP WASTSANAYY TPRANASASY TDTSALAGRS LQQSNSFPTR
AGDPQATSTA SNSGVSVGQK PFVPSYRLFE DLDVFGSADG KHNKPANSSN GSQNLSGSQT
QQSMIGGRKM I
//
