VA711_ARATH
ID VA711_ARATH Reviewed; 219 AA.
AC O49377;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Vesicle-associated membrane protein 711 {ECO:0000303|PubMed:11115874};
DE Short=AtVAMP711 {ECO:0000303|PubMed:11115874};
DE AltName: Full=v-SNARE synaptobrevin 7C {ECO:0000303|Ref.1};
DE Short=AtVAMP7C {ECO:0000303|Ref.1};
GN Name=VAMP711 {ECO:0000303|PubMed:11115874};
GN Synonyms=VAMP7C {ECO:0000303|Ref.1};
GN OrderedLocusNames=At4g32150 {ECO:0000312|Araport:AT4G32150};
GN ORFNames=F10N7.40 {ECO:0000312|EMBL:CAA16574.1};
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 TISSUE=Flower, Rosette leaf, Seedling, Silique, and Stem;
RA Nikoloff D.M., Somerville C.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP DOMAIN.
RX PubMed=15876431; DOI=10.1016/j.febslet.2005.04.022;
RA Uemura T., Sato M.H., Takeyasu K.;
RT "The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis
RT thaliana.";
RL FEBS Lett. 579:2842-2846(2005).
RN [9]
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: Vacuole membrane {ECO:0000269|PubMed:15342965};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
CC Prevacuolar compartment membrane {ECO:0000269|PubMed:15342965}; Single-
CC pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, stems and roots.
CC {ECO:0000269|PubMed:15342965}.
CC -!- DOMAIN: The longin domain is essential for the vacuolar and subcellular
CC targeting. {ECO:0000269|PubMed:15876431}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; AF025332; AAD01748.1; -; mRNA.
DR EMBL; AL021636; CAA16574.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79933.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86011.1; -; Genomic_DNA.
DR EMBL; AF439840; AAL27509.1; -; mRNA.
DR EMBL; AY125553; AAM78063.1; -; mRNA.
DR EMBL; AY088128; AAM65673.1; -; mRNA.
DR PIR; T04630; T04630.
DR RefSeq; NP_194942.1; NM_119367.3.
DR AlphaFoldDB; O49377; -.
DR SMR; O49377; -.
DR BioGRID; 14633; 7.
DR IntAct; O49377; 4.
DR STRING; 3702.AT4G32150.1; -.
DR iPTMnet; O49377; -.
DR SwissPalm; O49377; -.
DR PaxDb; O49377; -.
DR PRIDE; O49377; -.
DR ProteomicsDB; 242304; -.
DR EnsemblPlants; AT4G32150.1; AT4G32150.1; AT4G32150.
DR GeneID; 829347; -.
DR Gramene; AT4G32150.1; AT4G32150.1; AT4G32150.
DR KEGG; ath:AT4G32150; -.
DR Araport; AT4G32150; -.
DR TAIR; locus:2116672; AT4G32150.
DR eggNOG; KOG0859; Eukaryota.
DR HOGENOM; CLU_064620_1_2_1; -.
DR InParanoid; O49377; -.
DR OMA; AFTMNDE; -.
DR OrthoDB; 1211929at2759; -.
DR PhylomeDB; O49377; -.
DR PRO; PR:O49377; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49377; baseline and differential.
DR Genevisible; O49377; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0061025; P:membrane fusion; TAS:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; 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; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..219
FT /note="Vesicle-associated membrane protein 711"
FT /id="PRO_0000206750"
FT TOPO_DOM 2..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..219
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 7..111
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 126..186
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 219 AA; 25039 MW; 54C3ECF5C7A3D39E CRC64;
MAILYALVAR GTVVLSEFTA TSTNASTIAK QILEKVPGDN DSNVSYSQDR YVFHVKRTDG
LTVLCMAEET AGRRIPFAFL EDIHQRFVRT YGRAVHTALA YAMNEEFSRV LSQQIDYYSN
DPNADRINRI KGEMNQVRGV MIENIDKVLD RGERLELLVD KTANMQGNTF RFRKQARRFR
SNVWWRNCKL TVLLILLLLV IIYIAVAFLC HGPTLPSCI
