TOL5_ARATH
ID TOL5_ARATH Reviewed; 447 AA.
AC Q9FFQ0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=TOM1-like protein 5 {ECO:0000305};
GN Name=TOL5 {ECO:0000303|PubMed:24316203};
GN Synonyms=TOM1G {ECO:0000303|PubMed:22639582};
GN OrderedLocusNames=At5g63640 {ECO:0000312|Araport:AT5G63640};
GN ORFNames=MBK5.12 {ECO:0000312|EMBL:BAB10457.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
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 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 GENE FAMILY, AND NOMENCLATURE.
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 [6]
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 [7]
RP GENE FAMILY, NOMENCLATURE, 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 [8]
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: Might contribute to the loading of the ESCRT machinery.
CC {ECO:0000305|PubMed:16488176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24316203}. Membrane
CC {ECO:0000269|PubMed:24316203}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in siliques and cauline
CC leaves. {ECO:0000269|PubMed:24699223}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AB005234; BAB10457.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97780.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70205.1; -; Genomic_DNA.
DR EMBL; AY062583; AAL32661.1; -; mRNA.
DR EMBL; AY114647; AAM47966.1; -; mRNA.
DR RefSeq; NP_001331835.1; NM_001345600.1.
DR RefSeq; NP_201169.1; NM_125759.6.
DR AlphaFoldDB; Q9FFQ0; -.
DR SMR; Q9FFQ0; -.
DR STRING; 3702.AT5G63640.1; -.
DR iPTMnet; Q9FFQ0; -.
DR PaxDb; Q9FFQ0; -.
DR PRIDE; Q9FFQ0; -.
DR ProteomicsDB; 234454; -.
DR EnsemblPlants; AT5G63640.1; AT5G63640.1; AT5G63640.
DR EnsemblPlants; AT5G63640.2; AT5G63640.2; AT5G63640.
DR GeneID; 836484; -.
DR Gramene; AT5G63640.1; AT5G63640.1; AT5G63640.
DR Gramene; AT5G63640.2; AT5G63640.2; AT5G63640.
DR KEGG; ath:AT5G63640; -.
DR Araport; AT5G63640; -.
DR TAIR; locus:2160654; AT5G63640.
DR eggNOG; KOG1087; Eukaryota.
DR HOGENOM; CLU_026748_0_0_1; -.
DR InParanoid; Q9FFQ0; -.
DR OMA; TVINREP; -.
DR OrthoDB; 852075at2759; -.
DR PhylomeDB; Q9FFQ0; -.
DR PRO; PR:Q9FFQ0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFQ0; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
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; PTHR45898; PTHR45898; 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 Acetylation; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..447
FT /note="TOM1-like protein 5"
FT /id="PRO_0000440680"
FT DOMAIN 9..138
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 178..266
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 164..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
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"
SQ SEQUENCE 447 AA; 49423 MW; CCF9F64366A1D338 CRC64;
MAAELVSSAT SEKLADVDWA KNIEICELAA RDERQAKDVI KAIKKRLGSK NPNTQLYAVQ
LLEMLMNNIG ENIHKQVIDT GVLPTLVKIV KKKSDLPVRE RIFLLLDATQ TSLGGASGKF
PQYYTAYYEL VNAGVKFTQR PNATPVVVTA QAVPRNTLNE QLASARNEGP ATTQQRESQS
VSPSSILQKA STALEILKEV LDAVDSQNPE GAKDEFTLDL VEQCSFQKER VMHLVMTSRD
EKAVSKAIEL NEQLQRILNR HEDLLSGRIT VPSRSTTSNG YHSNLEPVRP ISNGDQKREL
KASNANTESS SFISNRAHLK LEEEDEEEEP EQLFRRLRKG KARARPEDEE EPSPPQGLPG
SAIHNERLNR PLIRPLPSEE ASRGGDSHSQ SPPVVIPPPP AKHVEREKFF KENKGDGALG
LPGHMRGLSL HSRDGSSSRS GSVDFSD
