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Vesicle transport v-SNARE 11 (AtVTI11) (Protein SHOOT GRAVITROPISM 4) (Vesicle soluble NSF attachment protein receptor VTI1a) (AtVTI1a) (Vesicle transport v-SNARE protein VTI1a)

 VTI11_ARATH             Reviewed;         221 AA.
Q9SEL6; Q9FLY4;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
17-JAN-2003, sequence version 2.
23-MAY-2018, entry version 129.
RecName: Full=Vesicle transport v-SNARE 11;
Short=AtVTI11;
AltName: Full=Protein SHOOT GRAVITROPISM 4;
AltName: Full=Vesicle soluble NSF attachment protein receptor VTI1a;
Short=AtVTI1a;
AltName: Full=Vesicle transport v-SNARE protein VTI1a;
Name=VTI11; Synonyms=SGR4, VTI1A, ZIG, ZIG1;
OrderedLocusNames=At5g39510; ORFNames=MUL8_190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SYP21.
STRAIN=cv. Columbia;
PubMed=10397763; DOI=10.1091/mbc.10.7.2251;
Zheng H., von Mollard G.F., Kovaleva V., Stevens T.H., Raikhel N.V.;
"The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle
transport from the trans-Golgi network to the prevacuolar
compartment.";
Mol. Biol. Cell 10:2251-2264(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
INTERACTION WITH SYP21; SYP22; SYP51 AND SYP61.
PubMed=11739776; DOI=10.1091/mbc.12.12.3733;
Sanderfoot A.A., Kovaleva V., Bassham D.C., Raikhel N.V.;
"Interactions between syntaxins identify at least five SNARE complexes
within the Golgi/prevacuolar system of the Arabidopsis cell.";
Mol. Biol. Cell 12:3733-3743(2001).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=9210330; DOI=10.1093/oxfordjournals.pcp.a029201;
Yamauchi Y., Fukaki H., Fujisawa H., Tasaka M.;
"Mutations in the SGR4, SGR5 and SGR6 loci of Arabidopsis thaliana
alter the shoot gravitropism.";
Plant Cell Physiol. 38:530-535(1997).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-151.
STRAIN=cv. Columbia;
PubMed=11826297; DOI=10.1105/tpc.010215;
Kato T., Morita M.T., Fukaki H., Yamauchi Y., Uehara M., Niihama M.,
Tasaka M.;
"SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are
involved in the shoot gravitropism of Arabidopsis.";
Plant Cell 14:33-46(2002).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11826298; DOI=10.1105/tpc.010216;
Morita M.T., Kato T., Nagafusa K., Saito C., Ueda T., Nakano A.,
Tasaka M.;
"Involvement of the vacuoles of the endodermis in the early process of
shoot gravitropism in Arabidopsis.";
Plant Cell 14:47-56(2002).
[9]
INTERACTION WITH EPSIN1.
PubMed=16905657; DOI=10.1105/tpc.105.039123;
Song J., Lee M.H., Lee G.-J., Yoo C.M., Hwang I.;
"Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of
soluble cargo proteins in plant cells via interactions with clathrin,
AP-1, VTI11, and VSR1.";
Plant Cell 18:2258-2274(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=17151019; DOI=10.1074/mcp.M600250-MCP200;
Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V.,
Bruley C., Garin J., Bourguignon J.;
"A proteomics dissection of Arabidopsis thaliana vacuoles isolated
from cell culture.";
Mol. Cell. Proteomics 6:394-412(2007).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=21645145; DOI=10.1111/j.1365-313X.2011.04665.x;
Saito C., Uemura T., Awai C., Tominaga M., Ebine K., Ito J., Ueda T.,
Abe H., Morita M.T., Tasaka M., Nakano A.;
"The occurrence of 'bulbs', a complex configuration of the vacuolar
membrane, is affected by mutations of vacuolar SNARE and phospholipase
in Arabidopsis.";
Plant J. 68:64-73(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: May function as a v-SNARE responsible for targeting
AtELP-containing vesicles from the trans-Golgi network (TGN) to
the prevacuolar compartment (PVC). May be also involved in
retrograde traffic to the cis-Golgi (By similarity). Promotes the
formation of vacuolar membrane 'bulbs'. Required for amyloplast
sedimentation in the endodermis during shoot gravitropism, which
are thus acting as statoliths. Expression in the endodermis is
essential for the shoot gravitropic response, whereas expression
in other tissues may be responsible for the correct stem and leaf
shape. {ECO:0000250, ECO:0000269|PubMed:11826297,
ECO:0000269|PubMed:11826298, ECO:0000269|PubMed:21645145,
ECO:0000269|PubMed:9210330}.
-!- SUBUNIT: Forms SNARE complexes with the t-SNAREs SYP51 and either
SYP21 or SYP22 in the PVC, and with a much lower affinity with
SYP61 in the TGN. Does not interact with SYP41, SYP42 or VPS45.
Binds to EPSIN1.
-!- INTERACTION:
Q8VY07:EPSIN1; NbExp=3; IntAct=EBI-1162795, EBI-1162785;
Q39233:SYP21; NbExp=4; IntAct=EBI-1162795, EBI-2352544;
P93654:SYP22; NbExp=3; IntAct=EBI-1162795, EBI-2352632;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane; Single-pass type IV membrane protein. Prevacuolar
compartment membrane; Single-pass type IV membrane protein.
Vacuole membrane {ECO:0000269|PubMed:17151019}; Single-pass type
IV membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
-!- DISRUPTION PHENOTYPE: Abnormal amyloplast sedimentation and
gravitropism in both inflorescence stems and hypocotyls with
elongated stems in a zigzag fashion, due to narrower angles in
internodes mediated by aberrant cell shapes. Reduced formation of
vacuolar membrane 'bulbs'. Small and wrinkled rosette leaves.
Fragmentation and vesiculation of vacuoles mostly in cortex cells
of the inflorescence stem in comparison to endodermal cells.
{ECO:0000269|PubMed:11826297, ECO:0000269|PubMed:11826298,
ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:9210330}.
-!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF114750; AAF24061.1; -; mRNA.
EMBL; AB009054; BAB11026.1; -; Genomic_DNA.
EMBL; CP002688; AED94442.1; -; Genomic_DNA.
EMBL; AY070486; AAL49951.1; -; mRNA.
EMBL; AY091707; AAM10306.1; -; mRNA.
RefSeq; NP_198767.1; NM_123313.5.
UniGene; At.30339; -.
UniGene; At.71131; -.
ProteinModelPortal; Q9SEL6; -.
SMR; Q9SEL6; -.
BioGrid; 19198; 11.
IntAct; Q9SEL6; 12.
STRING; 3702.AT5G39510.1; -.
iPTMnet; Q9SEL6; -.
PaxDb; Q9SEL6; -.
EnsemblPlants; AT5G39510.1; AT5G39510.1; AT5G39510.
GeneID; 833947; -.
Gramene; AT5G39510.1; AT5G39510.1; AT5G39510.
KEGG; ath:AT5G39510; -.
Araport; AT5G39510; -.
TAIR; locus:2175733; AT5G39510.
eggNOG; KOG1666; Eukaryota.
eggNOG; ENOG4111J90; LUCA.
HOGENOM; HOG000116573; -.
InParanoid; Q9SEL6; -.
KO; K08493; -.
OMA; KNKWTIG; -.
OrthoDB; EOG09360PI6; -.
PhylomeDB; Q9SEL6; -.
Reactome; R-ATH-114608; Platelet degranulation.
Reactome; R-ATH-6811438; Intra-Golgi traffic.
Reactome; R-ATH-6811440; Retrograde transport at the Trans-Golgi-Network.
PRO; PR:Q9SEL6; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9SEL6; baseline and differential.
Genevisible; Q9SEL6; AT.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:TAIR.
GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0009630; P:gravitropism; IMP:TAIR.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
Gene3D; 1.20.58.400; -; 1.
InterPro; IPR027027; GOSR2/Membrin/Bos1.
InterPro; IPR010989; SNARE.
InterPro; IPR038407; v-SNARE_N_sf.
InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
Pfam; PF05008; V-SNARE; 1.
PIRSF; PIRSF028865; Membrin-2; 1.
SUPFAM; SSF47661; SSF47661; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Golgi apparatus;
Membrane; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Vacuole.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 221 Vesicle transport v-SNARE 11.
/FTId=PRO_0000218233.
TOPO_DOM 2 198 Cytoplasmic. {ECO:0000255}.
TRANSMEM 199 219 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 220 221 Vesicular. {ECO:0000255}.
COILED 32 93 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 151 151 G->D: In zig-3; retarded response to
gravity. {ECO:0000269|PubMed:11826297}.
CONFLICT 4 4 V -> A (in Ref. 1; AAF24061).
{ECO:0000305}.
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


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