TNO1_ARATH
ID TNO1_ARATH Reviewed; 1767 AA.
AC F4I9A2; F1BCU1; Q8GXQ6; Q9FYL7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Trans-Golgi network-localized SYP41-interacting protein 1 {ECO:0000303|PubMed:21521696};
DE Short=TGN-localized SYP41-interacting protein 1 {ECO:0000303|PubMed:21521696};
GN Name=TNO1 {ECO:0000303|PubMed:21521696};
GN OrderedLocusNames=At1g24460 {ECO:0000312|Araport:AT1G24460};
GN ORFNames=F21J9.12 {ECO:0000312|EMBL:AAF97958.1};
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, INTERACTION WITH SYP41, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Silique;
RX PubMed=21521696; DOI=10.1104/pp.110.168963;
RA Kim S.-J., Bassham D.C.;
RT "TNO1 is involved in salt tolerance and vacuolar trafficking in
RT Arabidopsis.";
RL Plant Physiol. 156:514-526(2011).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1464-1767.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28399805; DOI=10.1186/s12870-017-1024-4;
RA Roy R., Bassham D.C.;
RT "TNO1, a TGN-localized SNARE-interacting protein, modulates root skewing in
RT Arabidopsis thaliana.";
RL BMC Plant Biol. 17:73-73(2017).
CC -!- FUNCTION: Tethering factor involved in vesicle fusion at the trans-
CC Golgi network (TGN) thus being required for efficient protein
CC trafficking to the vacuole (PubMed:21521696). Implicated in resistance
CC to salt and osmotic stresses (PubMed:21521696). Modulates the cell
CC morphology (e.g. epidermal cell file rotation (CFR) and cell expansion)
CC in mature regions of roots and the base of hypocotyls as well as root
CC skewing, a process leading to root movement within the soil in order to
CC maximize anchorage and nutrient acquisition, probably by regulating
CC microtubule stabilization independently of their orientation
CC (PubMed:28399805). {ECO:0000269|PubMed:21521696,
CC ECO:0000269|PubMed:28399805}.
CC -!- SUBUNIT: Interacts with SYP41. {ECO:0000269|PubMed:21521696}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:21521696}; Single-pass type IV membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in roots, leaves and
CC flowers, and, to a lower extent, in stems.
CC {ECO:0000269|PubMed:21521696}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during germination, flower
CC development, and silique maturation. {ECO:0000269|PubMed:21521696}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to high concentrations of
CC NaCl, KCl and LiCl, and also to mannitol-induced osmotic stress
CC (PubMed:21521696). Altered localization of SYP61 and abnormal partial
CC secretion of vacuolar proteins to the apoplast (PubMed:21521696).
CC Enhanced root skewing and epidermal cell file rotation (CFR) probably
CC due to microtubule destabilization, thus leading to abnormal cell
CC morphology in mature regions of roots and the base of hypocotyls
CC (PubMed:28399805). {ECO:0000269|PubMed:21521696,
CC ECO:0000269|PubMed:28399805}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE30533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HM776995; ADM94222.1; -; mRNA.
DR EMBL; AC000103; AAF97958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK118102; BAC42730.1; -; mRNA.
DR PIR; F86378; F86378.
DR RefSeq; NP_001185085.1; NM_001198156.2.
DR iPTMnet; F4I9A2; -.
DR PRIDE; F4I9A2; -.
DR ProteomicsDB; 218243; -.
DR EnsemblPlants; AT1G24460.2; AT1G24460.2; AT1G24460.
DR GeneID; 839062; -.
DR Gramene; AT1G24460.2; AT1G24460.2; AT1G24460.
DR KEGG; ath:AT1G24460; -.
DR Araport; AT1G24460; -.
DR HOGENOM; CLU_002578_0_0_1; -.
DR OMA; EKSNEHE; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I9A2; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IMP:UniProtKB.
DR GO; GO:0035864; P:response to potassium ion; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0010015; P:root morphogenesis; IMP:UniProtKB.
DR GO; GO:0007034; P:vacuolar transport; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1767
FT /note="Trans-Golgi network-localized SYP41-interacting
FT protein 1"
FT /id="PRO_0000454396"
FT TOPO_DOM 1..1748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1749..1766
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1767
FT /note="Vesicular"
FT /evidence="ECO:0000305"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..436
FT /evidence="ECO:0000255"
FT COILED 493..516
FT /evidence="ECO:0000255"
FT COILED 570..590
FT /evidence="ECO:0000255"
FT COILED 684..805
FT /evidence="ECO:0000255"
FT COILED 845..1082
FT /evidence="ECO:0000255"
FT COILED 1251..1310
FT /evidence="ECO:0000255"
FT COILED 1362..1424
FT /evidence="ECO:0000255"
FT COILED 1522..1542
FT /evidence="ECO:0000255"
FT COILED 1603..1630
FT /evidence="ECO:0000255"
FT COMPBIAS 12..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 275
FT /note="R -> G (in Ref. 1; ADM94222)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="Q -> H (in Ref. 1; ADM94222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1404
FT /note="C -> R (in Ref. 1; ADM94222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1425
FT /note="E -> K (in Ref. 1; ADM94222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1445
FT /note="N -> H (in Ref. 1; ADM94222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1554
FT /note="L -> M (in Ref. 4; BAC42730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1767 AA; 197632 MW; 742C04559462C43F CRC64;
MHEKDDLPQD SIADGIENDD ESNGQEEEEL DPDQGTAFVD SKEDMFVDAP EELNFDTPSK
EALTTDDDDN DDLGTHFNIE KGDWEKELAG LQEQFKLLTG ENDLTGEDGN TTVDIVSRFS
KFLKTAKEER IQHEVALKEL HGVISGRDDE IADLTTKISE LSSSQPVSEM GDQAQNLEHL
EAATDRIMVS LSNVFGEGEL QYGSSISEKL AHLENRVSFL GAKYTEFYYG ADQLRKCLAS
DVLDLSFQED FGSALGAACS ELFELKQKEA AFFERLSHLE DENRNFVEQV NREKEMCESM
RTEFEKLKAE LELEKTKCTN TKEKLSMAVT KGKALVQNRD ALKHQLSEKT TELANRLTEL
QEKEIALESS EVMKGQLEQS LTEKTDELEK CYAELNDRSV SLEAYELTKK ELEQSLAEKT
KELEECLTKL QEMSTALDQS ELDKGELAKS DAMVASYQEM LSVRNSIIEN IETILSNIYT
PEEGHSFDIV EKVRSLAEER KELTNVSQEY NRLKDLIVSI DLPEEMSQSS LESRLAWLRE
SFLQGKDEVN ALQNRIESVS MSLSAEMEEK SNIRKELDDL SFSLKKMEET AERGSLEREE
IVRRLVETSG LMTEGVEDHT SSDINLLVDR SFDKIEKQIR DSSDSSYGNE EIFEAFQSLL
YVRDLEFSLC KEMLGEGELI SFQVSNLSDE LKIASQELAF VKEEKIALEK DLERSEEKSA
LLRDKLSMAI KKGKGLVQDR EKFKTQLDEK KSEIEKLMLE LQQLGGTVDG YKNQIDMLSR
DLERTKELET ELVATKEERD QLQQSLSLID TLLQKVMKSV EIIALPVDLA SEDPSEKIDR
LAGYIQEVQL ARVEEQEEIE KVKSEVDALT SKLAETQTAL KLVEDALSTA EDNISRLTEE
NRNVQAAKEN AELELQKAVA DASSVASELD EVLATKSTLE AALMQAERNI SDIISEKEEA
QGRTATAEME QEMLQKEASI QKNKLTEAHS TINSLEETLA QTESNMDSLS KQIEDDKVLT
TSLKNELEKL KIEAEFERNK MAEASLTIVS HEEALMKAEN SLSALQGEMV KAEGEISTLS
SKLNVCMEEL AGSSGNSQSK SLEIITHLDN LQMLLKDGGL ISKVNEFLQR KFKSLRDVDV
IARDITRNIG ENGLLAGEMG NAEDDSTEAK SLLSDLDNSV NTEPENSQGS AADEDEISSS
LRKMAEGVRL RNKTLENNFE GFSTSIDTLI ATLMQNMTAA RADVLNIVGH NSSLEEQVRS
VENIVREQEN TISALQKDLS SLISACGAAA RELQLEVKNN LLELVQFQEN ENGGEMESTE
DPQELHVSEC AQRIKELSSA AEKACATLKL FETTNNAAAT VIRDMENRLT EASVALEKAV
LERDLNQTKV SSSEAKVESL EELCQDLKLQ LENLRVKEEK WHEKEVELST LYDKLLVQEQ
EAKENLIPAS DMRTLFDKIN GIEVPSVDLV NGLDPQSPYD VKKLFAIVDS VTEMQHQIDI
LSYGQKELNS TLAEKDLEIQ GLKKATEAES TTELELVKAK NELSKLISGL EKLLGILASN
NPVVDPNFSE SWTLVQALEK KITSLLLESE SSKSRAQELG LKLAGSEKLV DKLSLRVKEF
EEKLQTKAIQ PDIVQERSIF ETPRAPSTSE ISEIEDKGAL GIKSISPVPT AAQVRTVRKG
STDHLSINID SESEHLMNNN ETDEDKGHVF KSLNMSGLIP TQGKIIADRV DGIWVSGGRV
LMSRPQARLG VMVYSLLLHL WLLASIL
