TOL8_ARATH
ID TOL8_ARATH Reviewed; 607 AA.
AC Q9C9Y1;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=TOM1-like protein 8 {ECO:0000305};
GN Name=TOL8 {ECO:0000303|PubMed:24316203};
GN Synonyms=TOM1H {ECO:0000303|PubMed:22639582};
GN OrderedLocusNames=At3g08790 {ECO:0000312|Araport:AT3G08790};
GN ORFNames=F17O14.26 {ECO:0000312|EMBL:AAG51368.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [4]
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
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 [6]
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: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in siliques and flowers.
CC {ECO:0000269|PubMed:24699223}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AC012562; AAG51368.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74680.1; -; Genomic_DNA.
DR RefSeq; NP_187491.1; NM_111713.2.
DR AlphaFoldDB; Q9C9Y1; -.
DR SMR; Q9C9Y1; -.
DR STRING; 3702.AT3G08790.1; -.
DR PaxDb; Q9C9Y1; -.
DR PRIDE; Q9C9Y1; -.
DR ProteomicsDB; 232466; -.
DR EnsemblPlants; AT3G08790.1; AT3G08790.1; AT3G08790.
DR GeneID; 820026; -.
DR Gramene; AT3G08790.1; AT3G08790.1; AT3G08790.
DR KEGG; ath:AT3G08790; -.
DR Araport; AT3G08790; -.
DR TAIR; locus:2077808; AT3G08790.
DR eggNOG; KOG1087; Eukaryota.
DR HOGENOM; CLU_026748_2_0_1; -.
DR InParanoid; Q9C9Y1; -.
DR OMA; WNLQITQ; -.
DR OrthoDB; 521769at2759; -.
DR PhylomeDB; Q9C9Y1; -.
DR PRO; PR:Q9C9Y1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C9Y1; baseline and differential.
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; 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 2: Evidence at transcript level;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..607
FT /note="TOM1-like protein 8"
FT /id="PRO_0000440683"
FT DOMAIN 9..138
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 175..263
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 141..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NQK0"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPL6"
SQ SEQUENCE 607 AA; 66686 MW; BED892C2329899EA CRC64;
MVHPLVDRAT SDMLIGPDWA MNLEICDMLN HEPGQTREVV SGIKKRLTSR TSKVQLLALT
LLETIITNCG ELIHMQVAEK DILHKMVKMA KRKPNIQVKE KILILIDTWQ ESFSGPQGRH
PQYYAAYQEL LRAGIVFPQR PQITPSSGQN GPSTRYPQNS RNARQEAIDT STESEFPTLS
LTEIQNARGI MDVLAEMMNA IDGNNKEGLK QEVVVDLVSQ CRTYKQRVVH LVNSTSDESM
LCQGLALNDD LQRLLAKHEA IASGNSMIKK EEKSKKEVPK DTTQIIDVGS SETKNGSVVA
YTTNGPKIDL LSGDDFETPN ADNSLALVPL GPPQPSSPVA KPDNSIVLID MLSDNNCESS
TPTSNPHANH QKVQQNYSNG FGPGHQEQSY YGQGSSAPVW NLQITQQPSS PAYGNQPFSP
NFSPPASPHY GGQNNNVLAL PPPPWEAQSP SSSPQYSPTH PMQVTQVVIT THTHQPLGYN
PQGGSPHATN NNNNNMFGMF LPPMTGGHMP PPFGHNGHVT NNNYNPNMYG GYGGQAQPPQ
QYLVEQQMYG MSLQDNGNNN TNPYQVSSHQ PPPMMKPMNK KPEDKLFGDL VELSKFKKPT
SGRAGSM
