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TOL1_ARATH
ID   TOL1_ARATH              Reviewed;         407 AA.
AC   Q9LFL3;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 146.
DE   RecName: Full=TOM1-like protein 1 {ECO:0000305};
GN   Name=TOL1 {ECO:0000303|PubMed:24316203};
GN   Synonyms=TOM_L {ECO:0000303|PubMed:22639582};
GN   OrderedLocusNames=At5g16880 {ECO:0000312|Araport:AT5G16880};
GN   ORFNames=F2K13_30 {ECO:0000312|EMBL:CAC01701.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, 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   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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   [9]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
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   [10]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=Additional isoforms seem to exist. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q9LFL3-1; Sequence=Displayed;
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; AL391141; CAC01701.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92353.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92354.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70041.1; -; Genomic_DNA.
DR   EMBL; AY056786; AAL10477.1; -; mRNA.
DR   EMBL; AY062640; AAL32718.1; -; mRNA.
DR   EMBL; BT002553; AAO00913.1; -; mRNA.
DR   EMBL; AY085140; AAM61693.1; -; mRNA.
DR   PIR; T51543; T51543.
DR   RefSeq; NP_001331679.1; NM_001343469.1. [Q9LFL3-1]
DR   RefSeq; NP_197190.1; NM_121694.4. [Q9LFL3-1]
DR   RefSeq; NP_850833.1; NM_180502.3. [Q9LFL3-1]
DR   AlphaFoldDB; Q9LFL3; -.
DR   SMR; Q9LFL3; -.
DR   IntAct; Q9LFL3; 3.
DR   STRING; 3702.AT5G16880.1; -.
DR   iPTMnet; Q9LFL3; -.
DR   PaxDb; Q9LFL3; -.
DR   PRIDE; Q9LFL3; -.
DR   ProteomicsDB; 234441; -. [Q9LFL3-1]
DR   EnsemblPlants; AT5G16880.1; AT5G16880.1; AT5G16880. [Q9LFL3-1]
DR   EnsemblPlants; AT5G16880.2; AT5G16880.2; AT5G16880. [Q9LFL3-1]
DR   EnsemblPlants; AT5G16880.4; AT5G16880.4; AT5G16880. [Q9LFL3-1]
DR   GeneID; 831551; -.
DR   Gramene; AT5G16880.1; AT5G16880.1; AT5G16880. [Q9LFL3-1]
DR   Gramene; AT5G16880.2; AT5G16880.2; AT5G16880. [Q9LFL3-1]
DR   Gramene; AT5G16880.4; AT5G16880.4; AT5G16880. [Q9LFL3-1]
DR   KEGG; ath:AT5G16880; -.
DR   Araport; AT5G16880; -.
DR   TAIR; locus:2148121; AT5G16880.
DR   eggNOG; KOG1087; Eukaryota.
DR   HOGENOM; CLU_038212_2_0_1; -.
DR   InParanoid; Q9LFL3; -.
DR   OMA; YKANAEP; -.
DR   PhylomeDB; Q9LFL3; -.
DR   PRO; PR:Q9LFL3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFL3; 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; IPR014645; TOM1.
DR   InterPro; IPR002014; VHS_dom.
DR   PANTHER; PTHR46646; PTHR46646; 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   Acetylation; Alternative splicing; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..407
FT                   /note="TOM1-like protein 1"
FT                   /id="PRO_0000440676"
FT   DOMAIN          55..183
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          228..315
FT                   /note="GAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT   REGION          315..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..407
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   407 AA;  45311 MW;  A3419556D696D8A2 CRC64;
     MGDNLMDKVT AFGERLKIGG SEVSNKISAG VSSMSFKVKE LFQGPNPTDK IVEDATTENL
     EEPDWDMNLE ICDMINQETI NSVELIRGIK KRIMMKQPRI QYLALVLLET CVKNCEKAFS
     EVAAERVLDE MVKLIDDPQT VVNNRNKALM LIEAWGESTS ELRYLPVFEE TYKSLKARGI
     RFPGRDNESL APIFTPARST PAPELNADLP QHVHEPAHIQ YDVPVRSFTA EQTKEAFDIA
     RNSIELLSTV LSSSPQHDAL QDDLTTTLVQ QCRQSQTTVQ RIIETAGENE ALLFEALNVN
     DELVKTLSKY EEMNKPSAPL TSHEPAMIPV AEEPDDSPIH GREESLVRKS SGVRGGFHGG
     GGSGDDMMDD LDEMIFGKKN GCDSSTNPDH DPKKEQSSSK NDDLIRF
 
 
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