VTI12_ARATH
ID VTI12_ARATH Reviewed; 222 AA.
AC Q9SEL5; Q9LQY5;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Vesicle transport v-SNARE 12 {ECO:0000303|PubMed:11739776, ECO:0000303|PubMed:17277094};
DE Short=AtVTI12 {ECO:0000303|PubMed:11739776, ECO:0000303|PubMed:17277094};
DE AltName: Full=Protein ZIG SUPPRESSOR 1 {ECO:0000303|PubMed:15797025};
DE AltName: Full=Vesicle soluble NSF attachment protein receptor VTI1b {ECO:0000303|PubMed:10397763, ECO:0000303|PubMed:10888666};
DE Short=AtVTI1b {ECO:0000303|PubMed:10397763, ECO:0000303|PubMed:10888666};
DE AltName: Full=Vesicle transport v-SNARE protein VTI1b {ECO:0000303|PubMed:10397763, ECO:0000303|PubMed:10888666};
GN Name=VTI12 {ECO:0000303|PubMed:11739776, ECO:0000303|PubMed:17277094};
GN Synonyms=VTI1B {ECO:0000303|PubMed:10397763, ECO:0000303|PubMed:10888666},
GN ZIP1 {ECO:0000303|PubMed:15797025};
GN OrderedLocusNames=At1g26670 {ECO:0000312|Araport:AT1G26670};
GN ORFNames=T24P13.5 {ECO:0000312|EMBL:AAF87026.1};
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].
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=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 INTERACTION WITH VPS45.
RX PubMed=10888666; DOI=10.1091/mbc.11.7.2251;
RA Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT "AtVPS45 complex formation at the trans-Golgi network.";
RL Mol. Biol. Cell 11:2251-2265(2000).
RN [5]
RP INTERACTION WITH SYP41; SYP42; 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 [6]
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 [7]
RP FUNCTION, MUTAGENESIS OF GLU-129, 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 [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SYP41.
RX PubMed=15919093; DOI=10.1016/j.jmb.2005.04.061;
RA Chen Y., Shin Y.-K., Bassham D.C.;
RT "YKT6 is a core constituent of membrane fusion machineries at the
RT Arabidopsis trans-Golgi network.";
RL J. Mol. Biol. 350:92-101(2005).
RN [9]
RP INTERACTION WITH EPSIN2, AND SUBCELLULAR LOCATION.
RX PubMed=17277094; DOI=10.1104/pp.106.095349;
RA Lee G.-J., Kim H., Kang H., Jang M., Lee D.W., Lee S., Hwang I.;
RT "EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and
RT phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in
RT protein trafficking in plant cells.";
RL Plant Physiol. 143:1561-1575(2007).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20841426; DOI=10.1105/tpc.109.069880;
RA Ovecka M., Berson T., Beck M., Derksen J., Samaj J., Baluska F.,
RA Lichtscheidl I.K.;
RT "Structural sterols are involved in both the initiation and tip growth of
RT root hairs in Arabidopsis thaliana.";
RL Plant Cell 22:2999-3019(2010).
RN [12]
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 [13]
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 [14]
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: Together with either SYP41 or SYP61, required for membrane
CC fusion; the fusion of phospholipid vesicles containing SYP41 or SYP61
CC and VTI12 is triggered by YKT61 and YKT62 (PubMed:15919093). Functions
CC as a v-SNARE responsible for the docking or fusion of transport
CC vesicles within the trans-Golgi network (TGN) and mediates liposome
CC fusion (PubMed:24021022, PubMed:15797025). Necessary to deliver
CC proteins to the protein storage vacuole (PSV) (PubMed:17360696). May be
CC also involved in retrograde traffic to the cis-Golgi (By similarity).
CC {ECO:0000250|UniProtKB:Q04338, ECO:0000269|PubMed:15797025,
CC ECO:0000269|PubMed:15919093, ECO:0000269|PubMed:17360696,
CC ECO:0000269|PubMed:24021022}.
CC -!- SUBUNIT: Forms SNARE complexes with the t-SNAREs SYP61 and either SYP41
CC or SYP42, and with a much lower affinity with SYP51 in the TGN
CC (PubMed:11739776, PubMed:15919093). Interacts also with VPS45, a Sec1
CC protein, but not with SYP21 or SYP22 (PubMed:10888666). Binds to EPSIN2
CC (PubMed:17277094). Core constituent of the SNARE complex required for
CC membrane fusion at the trans-Golgi network (PubMed:15919093). Interacts
CC with SCYL2B (PubMed:28751315). {ECO:0000269|PubMed:10888666,
CC ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15919093,
CC ECO:0000269|PubMed:17277094, ECO:0000269|PubMed:28751315}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:15797025,
CC ECO:0000269|PubMed:17277094}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:17277094}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:15797025, ECO:0000269|PubMed:17277094}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:17277094}. Cell membrane
CC {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein
CC {ECO:0000255}. Note=Accumulates in structural sterols-containing apical
CC and subapical compartments of developing root hairs tips.
CC {ECO:0000269|PubMed:20841426}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and leaves.
CC {ECO:0000269|PubMed:15342965}.
CC -!- DISRUPTION PHENOTYPE: Altered transport of storage proteins to the
CC protein storage vacuole (PSV). {ECO:0000269|PubMed:17360696}.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AF114751; AAF24062.1; -; mRNA.
DR EMBL; AC006535; AAF87026.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30719.1; -; Genomic_DNA.
DR RefSeq; NP_564255.1; NM_102430.5.
DR AlphaFoldDB; Q9SEL5; -.
DR SMR; Q9SEL5; -.
DR BioGRID; 24444; 10.
DR IntAct; Q9SEL5; 2.
DR STRING; 3702.AT1G26670.1; -.
DR iPTMnet; Q9SEL5; -.
DR PaxDb; Q9SEL5; -.
DR PRIDE; Q9SEL5; -.
DR ProteomicsDB; 242672; -.
DR EnsemblPlants; AT1G26670.1; AT1G26670.1; AT1G26670.
DR GeneID; 839208; -.
DR Gramene; AT1G26670.1; AT1G26670.1; AT1G26670.
DR KEGG; ath:AT1G26670; -.
DR Araport; AT1G26670; -.
DR TAIR; locus:2200595; AT1G26670.
DR eggNOG; KOG1666; Eukaryota.
DR HOGENOM; CLU_075474_3_0_1; -.
DR InParanoid; Q9SEL5; -.
DR OMA; KLRMYRR; -.
DR OrthoDB; 1195966at2759; -.
DR PhylomeDB; Q9SEL5; -.
DR PRO; PR:Q9SEL5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SEL5; baseline and differential.
DR Genevisible; Q9SEL5; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; TAS:TAIR.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; 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:0005483; F:soluble NSF attachment protein activity; TAS:TAIR.
DR GO; GO:0046907; P:intracellular transport; TAS:TAIR.
DR GO; GO:1990019; P:protein storage vacuole organization; IDA: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; Cell membrane; Coiled coil; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..222
FT /note="Vesicle transport v-SNARE 12"
FT /id="PRO_0000218234"
FT TOPO_DOM 2..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..222
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT COILED 68..95
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 129
FT /note="E->K: In zip1; dominant suppressor of the zip1
FT mutation (plants lacking VTI11) by changing both the
FT specificity of SNARE complex formation and its
FT intracellular localization."
FT /evidence="ECO:0000269|PubMed:15797025"
FT CONFLICT 41
FT /note="E -> Q (in Ref. 1; AAF24062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25057 MW; CA9AA9B1C9B59880 CRC64;
MSDVFEGYER QYCELSTNLS RKCHSASVLS NGEEKKGKIA EIKSGIDEAD VLIRKMDLEA
RSLQPSAKAV CLSKLREYKS DLNQLKKEFK RVSSADAKPS SREELMESGM ADLHAVSADQ
RGRLAMSVER LDQSSDRIRE SRRLMLETEE VGISIVQDLS QQRQTLLHAH NKLHGVDDAI
DKSKKVLTAM SRRMTRNKWI ITSVIVALVL AIILIISYKL SH
