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TOL6_ARATH
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   25-MAY-2022, entry version 139.
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}.
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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.AT2G38410.1; -.
DR   iPTMnet; O80910; -.
DR   PaxDb; O80910; -.
DR   PRIDE; O80910; -.
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; locus:2057140; AT2G38410.
DR   eggNOG; KOG1087; Eukaryota.
DR   HOGENOM; CLU_026748_2_1_1; -.
DR   InParanoid; O80910; -.
DR   OMA; CDKVTTN; -.
DR   OrthoDB; 660590at2759; -.
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   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; PTHR45898; 2.
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   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
 
 
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