VTI13_ARATH
ID VTI13_ARATH Reviewed; 221 AA.
AC Q9LVP9; A0A1I9LSM6; Q8GXG5;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Vesicle transport v-SNARE 13 {ECO:0000303|PubMed:24737717};
DE Short=AtVTI13 {ECO:0000303|PubMed:24737717};
DE AltName: Full=Vesicle soluble NSF attachment protein receptor 13 {ECO:0000303|PubMed:24737717};
DE AltName: Full=Vesicle transport v-SNARE protein VTI13 {ECO:0000303|PubMed:24737717};
GN Name=VTI13 {ECO:0000303|PubMed:24737717};
GN OrderedLocusNames=At3g29100 {ECO:0000312|Araport:AT3G29100};
GN ORFNames=MXE2.7 {ECO:0000312|EMBL:BAB01986.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 2).
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=24737717; DOI=10.1093/aob/mcu041;
RA Larson E.R., Domozych D.S., Tierney M.L.;
RT "SNARE VTI13 plays a unique role in endosomal trafficking pathways
RT associated with the vacuole and is essential for cell wall organization and
RT root hair growth in arabidopsis.";
RL Ann. Bot. 114:1147-1159(2014).
CC -!- FUNCTION: May function as a v-SNARE responsible for targeting vesicles
CC involved in the secretory pathway (By similarity). Involved in actin-
CC dependent endosomal trafficking pathways associated with the vacuole
CC within root hairs and root tip epidermal cells (PubMed:24737717).
CC Essential for cell wall organization and polarized root hair growth
CC (PubMed:24737717). Also required for the localization of SYP41 to the
CC trans-Golgi network in root hair cells (PubMed:24737717).
CC {ECO:0000250|UniProtKB:Q9SEL5, ECO:0000269|PubMed:24737717}.
CC -!- SUBUNIT: Forms SNARE complexes with t-SNAREs.
CC {ECO:0000250|UniProtKB:Q9SEL5}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:24737717}; Single-pass type IV membrane protein
CC {ECO:0000255}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:24737717}; Single-
CC pass type IV membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:24737717}; Single-pass type IV membrane protein
CC {ECO:0000255}. Note=Present in a mobile endosomal compartment as well
CC as in vacuolar 'bulb'-like structures. {ECO:0000269|PubMed:24737717}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LVP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LVP9-2; Sequence=VSP_013658;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, flowers
CC and leaves. {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:24737717}.
CC -!- DISRUPTION PHENOTYPE: Abnormal cell wall organization in root hair and
CC root epidermal cells, probably due to altered endosomal trafficking,
CC and leading to short and branched root hairs (PubMed:24737717).
CC Mislocalization of SYP41 in root hair cells (PubMed:24737717).
CC {ECO:0000269|PubMed:24737717}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the VTI1 family. {ECO:0000305}.
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DR EMBL; AB018121; BAB01986.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77536.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65584.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65585.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65586.1; -; Genomic_DNA.
DR EMBL; AK118255; BAC42873.1; -; mRNA.
DR RefSeq; NP_001189997.1; NM_001203068.2. [Q9LVP9-2]
DR RefSeq; NP_001327542.1; NM_001339005.1. [Q9LVP9-2]
DR RefSeq; NP_001327543.1; NM_001339006.1. [Q9LVP9-2]
DR RefSeq; NP_001327544.1; NM_001339004.1. [Q9LVP9-1]
DR AlphaFoldDB; Q9LVP9; -.
DR SMR; Q9LVP9; -.
DR BioGRID; 7886; 1.
DR STRING; 3702.AT3G29100.1; -.
DR iPTMnet; Q9LVP9; -.
DR PaxDb; Q9LVP9; -.
DR PRIDE; Q9LVP9; -.
DR ProteomicsDB; 242543; -. [Q9LVP9-1]
DR EnsemblPlants; AT3G29100.2; AT3G29100.2; AT3G29100. [Q9LVP9-2]
DR EnsemblPlants; AT3G29100.3; AT3G29100.3; AT3G29100. [Q9LVP9-1]
DR EnsemblPlants; AT3G29100.4; AT3G29100.4; AT3G29100. [Q9LVP9-2]
DR EnsemblPlants; AT3G29100.5; AT3G29100.5; AT3G29100. [Q9LVP9-2]
DR GeneID; 822557; -.
DR Gramene; AT3G29100.2; AT3G29100.2; AT3G29100. [Q9LVP9-2]
DR Gramene; AT3G29100.3; AT3G29100.3; AT3G29100. [Q9LVP9-1]
DR Gramene; AT3G29100.4; AT3G29100.4; AT3G29100. [Q9LVP9-2]
DR Gramene; AT3G29100.5; AT3G29100.5; AT3G29100. [Q9LVP9-2]
DR KEGG; ath:AT3G29100; -.
DR Araport; AT3G29100; -.
DR eggNOG; KOG1666; Eukaryota.
DR InParanoid; Q9LVP9; -.
DR OMA; RGRVESH; -.
DR OrthoDB; 1195966at2759; -.
DR PhylomeDB; Q9LVP9; -.
DR PRO; PR:Q9LVP9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVP9; baseline and differential.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
DR GO; GO:0051222; P:positive regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0080147; P:root hair cell development; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Endosome; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..221
FT /note="Vesicle transport v-SNARE 13"
FT /id="PRO_0000218235"
FT TOPO_DOM 1..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 VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_013658"
SQ SEQUENCE 221 AA; 25026 MW; 0D8867595EE3EB81 CRC64;
MSQGFERYER QYCEISANLS KKCTSAIALD GEQKKQNLSE IKSGVEEAEA LVKKMDLEAR
NLPPNVKSSL LVKLREYKSD LNNFKTEVKR ITSGNLNATA RDELLEAGMA DTLTASADQR
SRLMMSTDHL GRTTDRIKDS RRTILETEEL GVSILQDLHG QRQSLLRAHE TLHGVDDNVG
KSKKILTTMT RRMNRNKWTI GAIITVLVLA IIFILYFKLT R
