VTI11_ARATH
ID VTI11_ARATH Reviewed; 221 AA.
AC Q9SEL6; Q9FLY4;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Vesicle transport v-SNARE 11 {ECO:0000303|PubMed:11739776};
DE Short=AtVTI11 {ECO:0000303|PubMed:11739776};
DE AltName: Full=Protein SHOOT GRAVITROPISM 4 {ECO:0000303|PubMed:9210330};
DE AltName: Full=Vesicle soluble NSF attachment protein receptor VTI1a {ECO:0000303|PubMed:10397763};
DE Short=AtVTI1a {ECO:0000303|PubMed:10397763};
DE AltName: Full=Vesicle transport v-SNARE protein VTI1a {ECO:0000303|PubMed:10397763};
GN Name=VTI11 {ECO:0000303|PubMed:11739776};
GN Synonyms=SGR4 {ECO:0000303|PubMed:9210330},
GN VTI1A {ECO:0000303|PubMed:10397763}, ZIG {ECO:0000303|PubMed:11826297},
GN ZIG1 {ECO:0000303|PubMed:11826297};
GN OrderedLocusNames=At5g39510 {ECO:0000312|Araport:AT5G39510};
GN ORFNames=MUL8.21 {ECO:0000312|EMBL:BAB11026.1};
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], INTERACTION WITH SYP21, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10397763; DOI=10.1091/mbc.10.7.2251;
RA Zheng H., von Mollard G.F., Kovaleva V., Stevens T.H., Raikhel N.V.;
RT "The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle
RT transport from the trans-Golgi network to the prevacuolar compartment.";
RL Mol. Biol. Cell 10:2251-2264(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9210330; DOI=10.1093/oxfordjournals.pcp.a029201;
RA Yamauchi Y., Fukaki H., Fujisawa H., Tasaka M.;
RT "Mutations in the SGR4, SGR5 and SGR6 loci of Arabidopsis thaliana alter
RT the shoot gravitropism.";
RL Plant Cell Physiol. 38:530-535(1997).
RN [6]
RP INTERACTION WITH SYP21; SYP22; SYP51 AND SYP61.
RX PubMed=11739776; DOI=10.1091/mbc.12.12.3733;
RA Sanderfoot A.A., Kovaleva V., Bassham D.C., Raikhel N.V.;
RT "Interactions between syntaxins identify at least five SNARE complexes
RT within the Golgi/prevacuolar system of the Arabidopsis cell.";
RL Mol. Biol. Cell 12:3733-3743(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-151.
RC STRAIN=cv. Columbia;
RX PubMed=11826297; DOI=10.1105/tpc.010215;
RA Kato T., Morita M.T., Fukaki H., Yamauchi Y., Uehara M., Niihama M.,
RA Tasaka M.;
RT "SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are involved in
RT the shoot gravitropism of Arabidopsis.";
RL Plant Cell 14:33-46(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11826298; DOI=10.1105/tpc.010216;
RA Morita M.T., Kato T., Nagafusa K., Saito C., Ueda T., Nakano A., Tasaka M.;
RT "Involvement of the vacuoles of the endodermis in the early process of
RT shoot gravitropism in Arabidopsis.";
RL Plant Cell 14:47-56(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15342965; DOI=10.1247/csf.29.49;
RA Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., Sato M.H.;
RT "Systematic analysis of SNARE molecules in Arabidopsis: dissection of the
RT post-Golgi network in plant cells.";
RL Cell Struct. Funct. 29:49-65(2004).
RN [10]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15797025; DOI=10.1016/j.cub.2005.02.021;
RA Niihama M., Uemura T., Saito C., Nakano A., Sato M.H., Tasaka M.,
RA Morita M.T.;
RT "Conversion of functional specificity in Qb-SNARE VTI1 homologues of
RT Arabidopsis.";
RL Curr. Biol. 15:555-560(2005).
RN [11]
RP INTERACTION WITH EPSIN1.
RX PubMed=16905657; DOI=10.1105/tpc.105.039123;
RA Song J., Lee M.H., Lee G.-J., Yoo C.M., Hwang I.;
RT "Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of
RT soluble cargo proteins in plant cells via interactions with clathrin, AP-1,
RT VTI11, and VSR1.";
RL Plant Cell 18:2258-2274(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA Garin J., Bourguignon J.;
RT "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT cell culture.";
RL Mol. Cell. Proteomics 6:394-412(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17360696; DOI=10.1073/pnas.0611147104;
RA Sanmartin M., Ordonez A., Sohn E.J., Robert S., Sanchez-Serrano J.J.,
RA Surpin M.A., Raikhel N.V., Rojo E.;
RT "Divergent functions of VTI12 and VTI11 in trafficking to storage and lytic
RT vacuoles in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3645-3650(2007).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21645145; DOI=10.1111/j.1365-313x.2011.04665.x;
RA Saito C., Uemura T., Awai C., Tominaga M., Ebine K., Ito J., Ueda T.,
RA Abe H., Morita M.T., Tasaka M., Nakano A.;
RT "The occurrence of 'bulbs', a complex configuration of the vacuolar
RT membrane, is affected by mutations of vacuolar SNARE and phospholipase in
RT Arabidopsis.";
RL Plant J. 68:64-73(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [16]
RP FUNCTION.
RX PubMed=24021022; DOI=10.1186/1471-2091-14-22;
RA Kim S.-J., Bassham D.C.;
RT "Functional redundancy between trans-Golgi network SNARE family members in
RT Arabidopsis thaliana.";
RL BMC Biochem. 14:22-22(2013).
RN [17]
RP INTERACTION WITH SCYL2B.
RC STRAIN=cv. Columbia;
RX PubMed=28751315; DOI=10.1104/pp.17.00824;
RA Jung J.-Y., Lee D.W., Ryu S.B., Hwang I., Schachtman D.P.;
RT "SCYL2 genes are involved in clathrin-mediated vesicle trafficking and
RT essential for plant growth.";
RL Plant Physiol. 175:194-209(2017).
CC -!- FUNCTION: Functions as a v-SNARE responsible for targeting AtELP-
CC containing vesicles from the trans-Golgi network (TGN) to the
CC prevacuolar compartment (PVC) and mediates liposome fusion
CC (PubMed:10397763, PubMed:24021022). May be also involved in retrograde
CC traffic to the cis-Golgi (By similarity). Promotes the formation of
CC vacuolar membrane 'bulbs' (PubMed:21645145). Necessary to deliver
CC proteins to the lytic vacuole, but seems not involved in storage
CC proteins transport (PubMed:17360696). Required for amyloplast
CC sedimentation in the endodermis during shoot gravitropism, which are
CC thus acting as statoliths (PubMed:11826298, PubMed:15797025).
CC Expression in the endodermis is essential for the shoot gravitropic
CC response, whereas expression in other tissues may be responsible for
CC the correct stem and leaf shape (PubMed:9210330, PubMed:11826297,
CC PubMed:15797025). {ECO:0000250, ECO:0000269|PubMed:10397763,
CC ECO:0000269|PubMed:11826297, ECO:0000269|PubMed:11826298,
CC ECO:0000269|PubMed:15797025, ECO:0000269|PubMed:17360696,
CC ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:24021022,
CC ECO:0000269|PubMed:9210330}.
CC -!- SUBUNIT: Forms SNARE complexes with the t-SNAREs SYP51 and either SYP21
CC or SYP22 in the PVC, and with a much lower affinity with SYP61 in the
CC TGN (PubMed:15797025). Does not interact with SYP41, SYP42 or VPS45.
CC Binds to EPSIN1. Interacts with SCYL2B (PubMed:28751315).
CC {ECO:0000269|PubMed:15797025, ECO:0000269|PubMed:28751315}.
CC -!- INTERACTION:
CC Q9SEL6; Q8VY07: EPSIN1; NbExp=3; IntAct=EBI-1162795, EBI-1162785;
CC Q9SEL6; Q39233: SYP21; NbExp=4; IntAct=EBI-1162795, EBI-2352544;
CC Q9SEL6; P93654: SYP22; NbExp=3; IntAct=EBI-1162795, EBI-2352632;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:10397763, ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:15797025}; Single-pass type IV membrane protein
CC {ECO:0000255}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:10397763, ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:15797025}; Single-pass type IV membrane protein
CC {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:15797025, ECO:0000269|PubMed:17151019}; Single-pass
CC type IV membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
CC {ECO:0000269|PubMed:10397763, ECO:0000269|PubMed:15342965}.
CC -!- DISRUPTION PHENOTYPE: Abnormal amyloplast sedimentation and
CC gravitropism in both inflorescence stems and hypocotyls with elongated
CC stems in a zigzag fashion, due to narrower angles in internodes
CC mediated by aberrant cell shapes (PubMed:9210330, PubMed:11826297,
CC PubMed:11826298, PubMed:15797025). Reduced formation of vacuolar
CC membrane 'bulbs' (PubMed:21645145). Altered transport of proteins to
CC the lytic vacuole (PubMed:17360696). Small and wrinkled rosette leaves.
CC Fragmentation and vesiculation of vacuoles mostly in cortex cells of
CC the inflorescence stem in comparison to endodermal cells.
CC {ECO:0000269|PubMed:11826297, ECO:0000269|PubMed:11826298,
CC ECO:0000269|PubMed:15797025, ECO:0000269|PubMed:17360696,
CC ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:9210330}.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AF114750; AAF24061.1; -; mRNA.
DR EMBL; AB009054; BAB11026.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94442.1; -; Genomic_DNA.
DR EMBL; AY070486; AAL49951.1; -; mRNA.
DR EMBL; AY091707; AAM10306.1; -; mRNA.
DR RefSeq; NP_198767.1; NM_123313.5.
DR AlphaFoldDB; Q9SEL6; -.
DR SMR; Q9SEL6; -.
DR BioGRID; 19198; 11.
DR IntAct; Q9SEL6; 12.
DR STRING; 3702.AT5G39510.1; -.
DR iPTMnet; Q9SEL6; -.
DR PaxDb; Q9SEL6; -.
DR PRIDE; Q9SEL6; -.
DR ProteomicsDB; 242762; -.
DR EnsemblPlants; AT5G39510.1; AT5G39510.1; AT5G39510.
DR GeneID; 833947; -.
DR Gramene; AT5G39510.1; AT5G39510.1; AT5G39510.
DR KEGG; ath:AT5G39510; -.
DR Araport; AT5G39510; -.
DR TAIR; locus:2175733; AT5G39510.
DR eggNOG; KOG1666; Eukaryota.
DR HOGENOM; CLU_075474_3_0_1; -.
DR InParanoid; Q9SEL6; -.
DR OMA; EHSHQIA; -.
DR OrthoDB; 1195966at2759; -.
DR PhylomeDB; Q9SEL6; -.
DR PRO; PR:Q9SEL6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SEL6; baseline and differential.
DR Genevisible; Q9SEL6; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0075733; P:intracellular transport of virus; IMP:TAIR.
DR GO; GO:0080171; P:lytic vacuole organization; IMP:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR Gene3D; 1.20.58.400; -; 1.
DR InterPro; IPR027027; GOSR2/Membrin/Bos1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR038407; v-SNARE_N_sf.
DR InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR Pfam; PF05008; V-SNARE; 1.
DR PIRSF; PIRSF028865; Membrin-2; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..221
FT /note="Vesicle transport v-SNARE 11"
FT /id="PRO_0000218233"
FT TOPO_DOM 2..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..221
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT COILED 32..93
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 151
FT /note="G->D: In zig-3; retarded response to gravity."
FT /evidence="ECO:0000269|PubMed:11826297"
FT CONFLICT 4
FT /note="V -> A (in Ref. 1; AAF24061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 24951 MW; AFC1E86167981ED0 CRC64;
MSDVFDGYER QYCELSASLS KKCSSAISLD GEQKKQKLSE IKSGLENAEV LIRKMDLEAR
TLPPNLKSSL LVKLREFKSD LNNFKTEVKR ITSGQLNAAA RDELLEAGMA DTKTASADQR
ARLMMSTERL GRTTDRVKDS RRTMMETEEI GVSILQDLHG QRQSLLRAHE TLHGVDDNIG
KSKKILTDMT RRMNKNKWTI GAIIIALIAA IFIILYFKLT K
