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TOL3_ARATH
ID   TOL3_ARATH              Reviewed;         506 AA.
AC   Q9LPL6;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=TOM1-like protein 3 {ECO:0000305};
GN   Name=TOL3 {ECO:0000303|PubMed:24316203};
GN   Synonyms=TOM1F {ECO:0000303|PubMed:22639582};
GN   OrderedLocusNames=At1g21380 {ECO:0000312|Araport:AT1G21380};
GN   ORFNames=F24J8.3 {ECO:0000312|EMBL:AAF87893.1};
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].
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP   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, 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   [7]
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   [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: Membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in cauline leaves.
CC       {ECO:0000269|PubMed:24699223}.
CC   -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR   EMBL; AC015447; AAF87893.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30096.1; -; Genomic_DNA.
DR   EMBL; AY034974; AAK59479.1; -; mRNA.
DR   EMBL; AY062980; AAL34154.1; -; mRNA.
DR   PIR; H86346; H86346.
DR   RefSeq; NP_564138.1; NM_101990.4.
DR   AlphaFoldDB; Q9LPL6; -.
DR   SMR; Q9LPL6; -.
DR   STRING; 3702.AT1G21380.1; -.
DR   iPTMnet; Q9LPL6; -.
DR   PaxDb; Q9LPL6; -.
DR   PRIDE; Q9LPL6; -.
DR   ProteomicsDB; 234619; -.
DR   EnsemblPlants; AT1G21380.1; AT1G21380.1; AT1G21380.
DR   GeneID; 838737; -.
DR   Gramene; AT1G21380.1; AT1G21380.1; AT1G21380.
DR   KEGG; ath:AT1G21380; -.
DR   Araport; AT1G21380; -.
DR   TAIR; locus:2027037; AT1G21380.
DR   eggNOG; KOG1087; Eukaryota.
DR   HOGENOM; CLU_026748_2_1_1; -.
DR   InParanoid; Q9LPL6; -.
DR   OMA; INMEPSQ; -.
DR   OrthoDB; 508632at2759; -.
DR   PhylomeDB; Q9LPL6; -.
DR   PRO; PR:Q9LPL6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPL6; 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; IPR014645; TOM1.
DR   InterPro; IPR002014; VHS_dom.
DR   PANTHER; PTHR45898; PTHR45898; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036948; TOM1; 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   Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..506
FT                   /note="TOM1-like protein 3"
FT                   /id="PRO_0000440678"
FT   DOMAIN          12..141
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          180..268
FT                   /note="GAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT   REGION          266..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..370
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NQK0"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   506 AA;  55791 MW;  8D48F15FC714605C CRC64;
     MANNAAACAE RATNDMLIGP DWAINIELCD IINMEPSQAK EAVKVLKKRL GSKNSKVQIL
     ALYALETLSK NCGESVYQLI VDRDILPDMV KIVKKKPDLT VREKILSLLD TWQEAFGGSG
     GRFPQYYNAY NELRSAGIEF PPRTESSVPF FTPPQTQPIV AQATASDEDA AIQASLQSDD
     ASALSMEEIQ SAQGSVDVLT DMLGALDPSH PEGLKEELIV DLVEQCRTYQ RRVMALVNTT
     SDEELMCQGL ALNDNLQRVL QHHDDKAKGN SVPATAPTPI PLVSINHDDD DDESDDDFLQ
     LAHRSKRESA RGTGQGNFNP ILPPPPSSMR PVHVDSGAMD FLSGDVYKPQ ETFENVKPPS
     TSQSSNHDYS APIFDEPVPQ SKSPEHALFT KPVYDQTEQL PPAPWETQEP RKYPPSMSAR
     TNKRPEYFQH NVPQHSSSAS ESSYDDLLGQ SRNLSLNPTA SAAPVTPPKK DDKPEDILFK
     DLMDFAKTRT SSSSSSKPNN QNNKPF
 
 
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