VA714_ARATH
ID VA714_ARATH Reviewed; 221 AA.
AC Q9FMR5; Q93Z99;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Vesicle-associated membrane protein 714 {ECO:0000303|PubMed:11115874};
DE Short=AtVAMP714 {ECO:0000303|PubMed:11115874};
GN Name=VAMP714 {ECO:0000303|PubMed:11115874};
GN OrderedLocusNames=At5g22360 {ECO:0000312|Araport:AT5G22360};
GN ORFNames=MWD9.16 {ECO:0000312|EMBL:BAB08335.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11115874; DOI=10.1104/pp.124.4.1558;
RA Sanderfoot A.A., Assaad F.F., Raikhel N.V.;
RT "The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive
RT factor adaptor protein receptors.";
RL Plant Physiol. 124:1558-1569(2000).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane. {ECO:0000305|PubMed:11115874}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q12255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems and roots.
CC Detected in flowers. {ECO:0000269|PubMed:15342965}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL15329.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM51590.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB007651; BAB08335.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93017.1; -; Genomic_DNA.
DR EMBL; AY057699; AAL15329.1; ALT_SEQ; mRNA.
DR EMBL; AY116956; AAM51590.1; ALT_SEQ; mRNA.
DR RefSeq; NP_197628.1; NM_122141.5.
DR AlphaFoldDB; Q9FMR5; -.
DR SMR; Q9FMR5; -.
DR BioGRID; 17572; 6.
DR IntAct; Q9FMR5; 6.
DR STRING; 3702.AT5G22360.1; -.
DR iPTMnet; Q9FMR5; -.
DR PaxDb; Q9FMR5; -.
DR PRIDE; Q9FMR5; -.
DR ProteomicsDB; 243252; -.
DR EnsemblPlants; AT5G22360.1; AT5G22360.1; AT5G22360.
DR GeneID; 832297; -.
DR Gramene; AT5G22360.1; AT5G22360.1; AT5G22360.
DR KEGG; ath:AT5G22360; -.
DR Araport; AT5G22360; -.
DR TAIR; locus:2176342; AT5G22360.
DR eggNOG; KOG0859; Eukaryota.
DR HOGENOM; CLU_064620_1_1_1; -.
DR InParanoid; Q9FMR5; -.
DR OMA; NTKLMIM; -.
DR OrthoDB; 1211929at2759; -.
DR PhylomeDB; Q9FMR5; -.
DR PRO; PR:Q9FMR5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMR5; baseline and differential.
DR Genevisible; Q9FMR5; AT.
DR GO; GO:0005794; C:Golgi apparatus; TAS:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR042855; V_SNARE_CC.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..221
FT /note="Vesicle-associated membrane protein 714"
FT /id="PRO_0000206753"
FT TOPO_DOM 2..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..221
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 7..112
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 127..187
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 221 AA; 25317 MW; 48B59E2845FB1D03 CRC64;
MAIVYAVVAR GTVVLAEFSA VTGNTGAVVR RILEKLSPEI SDERLCFSQD RYIFHILRSD
GLTFLCMAND TFGRRVPFSY LEEIHMRFMK NYGKVAHNAP AYAMNDEFSR VLHQQMEFFS
SNPSVDTLNR VRGEVSEIRS VMVENIEKIM ERGDRIELLV DKTATMQDSS FHFRKQSKRL
RRALWMKNAK LLVLLTCLIV FLLYIIIASF CGGITLPSCR S
