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Protein

Vesicle-associated membrane protein 711

Gene

VAMP711

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the targeting and/or fusion of transport vesicles to their target membrane.1 Publication

GO - Molecular functioni

GO - Biological processi

  • exocytosis Source: GO_Central
  • intermembrane transport Source: TAIR
  • membrane fusion Source: TAIR
  • protein transport Source: UniProtKB-KW
  • response to abscisic acid Source: TAIR
  • response to salt stress Source: TAIR
  • stomatal movement Source: TAIR
  • vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 7111 Publication
Short name:
AtVAMP7111 Publication
Alternative name(s):
v-SNARE synaptobrevin 7C1 Publication
Short name:
AtVAMP7C1 Publication
Gene namesi
Name:VAMP7111 Publication
Synonyms:VAMP7C1 Publication
Ordered Locus Names:At4g32150Imported
ORF Names:F10N7.40Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G32150.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 189188CytoplasmicSequence analysisAdd
BLAST
Transmembranei190 – 21021Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini211 – 2199VesicularSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: UniProtKB-SubCell
  • plasma membrane Source: TAIR
  • SNARE complex Source: GO_Central
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 219218Vesicle-associated membrane protein 711PRO_0000206750Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO49377.
PRIDEiO49377.

PTM databases

SwissPalmiO49377.

Expressioni

Tissue specificityi

Expressed in flowers, leaves, stems and roots.1 Publication

Gene expression databases

ExpressionAtlasiO49377. baseline and differential.
GenevisibleiO49377. AT.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi14633. 7 interactions.
IntActiO49377. 3 interactions.
STRINGi3702.AT4G32150.1.

Structurei

3D structure databases

ProteinModelPortaliO49377.
SMRiO49377. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 111105LonginPROSITE-ProRule annotationAdd
BLAST
Domaini126 – 18661v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Domaini

The longin domain is essential for the vacuolar and subcellular targeting.1 Publication

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated
Contains 1 longin domain.PROSITE-ProRule annotation
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0859. Eukaryota.
COG5143. LUCA.
HOGENOMiHOG000042711.
InParanoidiO49377.
KOiK08515.
OMAiNDDINQV.
PhylomeDBiO49377.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O49377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILYALVAR GTVVLSEFTA TSTNASTIAK QILEKVPGDN DSNVSYSQDR
60 70 80 90 100
YVFHVKRTDG LTVLCMAEET AGRRIPFAFL EDIHQRFVRT YGRAVHTALA
110 120 130 140 150
YAMNEEFSRV LSQQIDYYSN DPNADRINRI KGEMNQVRGV MIENIDKVLD
160 170 180 190 200
RGERLELLVD KTANMQGNTF RFRKQARRFR SNVWWRNCKL TVLLILLLLV
210
IIYIAVAFLC HGPTLPSCI
Length:219
Mass (Da):25,039
Last modified:January 1, 1999 - v2
Checksum:i54C3ECF5C7A3D39E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025332 mRNA. Translation: AAD01748.1.
AL021636 Genomic DNA. Translation: CAA16574.1.
AL161580 Genomic DNA. Translation: CAB79933.1.
CP002687 Genomic DNA. Translation: AEE86011.1.
AF439840 mRNA. Translation: AAL27509.1.
AY125553 mRNA. Translation: AAM78063.1.
AY088128 mRNA. Translation: AAM65673.1.
PIRiT04630.
RefSeqiNP_194942.1. NM_119367.2.
UniGeneiAt.25445.

Genome annotation databases

EnsemblPlantsiAT4G32150.1; AT4G32150.1; AT4G32150.
GeneIDi829347.
GrameneiAT4G32150.1; AT4G32150.1; AT4G32150.
KEGGiath:AT4G32150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025332 mRNA. Translation: AAD01748.1.
AL021636 Genomic DNA. Translation: CAA16574.1.
AL161580 Genomic DNA. Translation: CAB79933.1.
CP002687 Genomic DNA. Translation: AEE86011.1.
AF439840 mRNA. Translation: AAL27509.1.
AY125553 mRNA. Translation: AAM78063.1.
AY088128 mRNA. Translation: AAM65673.1.
PIRiT04630.
RefSeqiNP_194942.1. NM_119367.2.
UniGeneiAt.25445.

3D structure databases

ProteinModelPortaliO49377.
SMRiO49377. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14633. 7 interactions.
IntActiO49377. 3 interactions.
STRINGi3702.AT4G32150.1.

PTM databases

SwissPalmiO49377.

Proteomic databases

PaxDbiO49377.
PRIDEiO49377.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G32150.1; AT4G32150.1; AT4G32150.
GeneIDi829347.
GrameneiAT4G32150.1; AT4G32150.1; AT4G32150.
KEGGiath:AT4G32150.

Organism-specific databases

TAIRiAT4G32150.

Phylogenomic databases

eggNOGiKOG0859. Eukaryota.
COG5143. LUCA.
HOGENOMiHOG000042711.
InParanoidiO49377.
KOiK08515.
OMAiNDDINQV.
PhylomeDBiO49377.

Miscellaneous databases

PROiO49377.

Gene expression databases

ExpressionAtlasiO49377. baseline and differential.
GenevisibleiO49377. AT.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
3.30.450.50. 1 hit.
InterProiIPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]
PfamiPF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
SMARTiSM01270. Longin. 1 hit.
[Graphical view]
SUPFAMiSSF64356. SSF64356. 1 hit.
PROSITEiPS50859. LONGIN. 1 hit.
PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Nikoloff D.M., Somerville C.R.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Flower, Rosette leaf, Seedling, Silique and Stem.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors."
    Sanderfoot A.A., Assaad F.F., Raikhel N.V.
    Plant Physiol. 124:1558-1569(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  7. "Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells."
    Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., Sato M.H.
    Cell Struct. Funct. 29:49-65(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "The longin domain regulates subcellular targeting of VAMP7 in Arabidopsis thaliana."
    Uemura T., Sato M.H., Takeyasu K.
    FEBS Lett. 579:2842-2846(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiVA711_ARATH
AccessioniPrimary (citable) accession number: O49377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 1, 1999
Last modified: June 8, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.