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Protein

Vesicle-associated membrane protein 4

Gene

Vamp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule (By similarity).By similarity

GO - Biological processi

  • Golgi ribbon formation Source: MGI
  • Golgi to plasma membrane protein transport Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • regulation of Golgi to plasma membrane protein transport Source: MGI
  • SNARE complex assembly Source: MGI
  • toxin transport Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 4
Short name:
VAMP-4
Gene namesi
Name:Vamp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1858730. Vamp4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 118118CytoplasmicSequence analysisAdd
BLAST
Transmembranei119 – 13921Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini140 – 1412VesicularSequence analysis

GO - Cellular componenti

  • cell surface Source: MGI
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • SNARE complex Source: MGI
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 141141Vesicle-associated membrane protein 4PRO_0000206732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei30 – 301PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO70480.
MaxQBiO70480.
PaxDbiO70480.
PRIDEiO70480.

PTM databases

iPTMnetiO70480.
PhosphoSiteiO70480.
SwissPalmiO70480.

Expressioni

Gene expression databases

BgeeiO70480.
CleanExiMM_VAMP4.
ExpressionAtlasiO70480. baseline and differential.
GenevisibleiO70480. MM.

Interactioni

Subunit structurei

Identified in a complex containing STX6, STX12, VAMP4 and VTI1A.1 Publication

Protein-protein interaction databases

IntActiO70480. 3 interactions.
MINTiMINT-4139753.
STRINGi10090.ENSMUSP00000051544.

Structurei

Secondary structure

1
141
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533Combined sources
Helixi54 – 574Combined sources
Helixi60 – 10950Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPSX-ray2.50A47-117[»]
ProteinModelPortaliO70480.
SMRiO70480. Positions 49-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 11261v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG061695.
InParanoidiO70480.
OMAiWRGCKMK.
OrthoDBiEOG7J182W.
PhylomeDBiO70480.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN
60 70 80 90 100
DKIKHVQNQV DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN
110 120 130 140
RSKQLRRQMW WRGCKIKAIM ALAAAILLLM IIILIVVKFR T
Length:141
Mass (Da):16,353
Last modified:August 1, 1998 - v1
Checksum:i556CCCB8213CF91E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131G → V in BAB27774 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061516 mRNA. Translation: AAC15776.1.
AK011678 mRNA. Translation: BAB27774.1.
AK018344 mRNA. Translation: BAB31171.1.
RefSeqiXP_006496997.1. XM_006496934.1.
XP_006496998.1. XM_006496935.1.
UniGeneiMm.10699.

Genome annotation databases

EnsembliENSMUST00000135241; ENSMUSP00000116376; ENSMUSG00000026696.
ENSMUST00000150040; ENSMUSP00000115133; ENSMUSG00000026696.
ENSMUST00000155003; ENSMUSP00000114172; ENSMUSG00000026696.
GeneIDi53330.
UCSCiuc007dgk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061516 mRNA. Translation: AAC15776.1.
AK011678 mRNA. Translation: BAB27774.1.
AK018344 mRNA. Translation: BAB31171.1.
RefSeqiXP_006496997.1. XM_006496934.1.
XP_006496998.1. XM_006496935.1.
UniGeneiMm.10699.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPSX-ray2.50A47-117[»]
ProteinModelPortaliO70480.
SMRiO70480. Positions 49-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70480. 3 interactions.
MINTiMINT-4139753.
STRINGi10090.ENSMUSP00000051544.

PTM databases

iPTMnetiO70480.
PhosphoSiteiO70480.
SwissPalmiO70480.

Proteomic databases

EPDiO70480.
MaxQBiO70480.
PaxDbiO70480.
PRIDEiO70480.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000135241; ENSMUSP00000116376; ENSMUSG00000026696.
ENSMUST00000150040; ENSMUSP00000115133; ENSMUSG00000026696.
ENSMUST00000155003; ENSMUSP00000114172; ENSMUSG00000026696.
GeneIDi53330.
UCSCiuc007dgk.1. mouse.

Organism-specific databases

CTDi8674.
MGIiMGI:1858730. Vamp4.

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG061695.
InParanoidiO70480.
OMAiWRGCKMK.
OrthoDBiEOG7J182W.
PhylomeDBiO70480.

Enzyme and pathway databases

ReactomeiR-MMU-6811440. Retrograde transport at the Trans-Golgi-Network.

Miscellaneous databases

EvolutionaryTraceiO70480.
PROiO70480.
SOURCEiSearch...

Gene expression databases

BgeeiO70480.
CleanExiMM_VAMP4.
ExpressionAtlasiO70480. baseline and differential.
GenevisibleiO70480. MM.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zhang T., Wong S.H., Xu Y., Hong W.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum and Embryo.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies."
    Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C., Jahn R.
    EMBO J. 26:9-18(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH STX12; VTI1A AND STX6, SUBUNIT.

Entry informationi

Entry nameiVAMP4_MOUSE
AccessioniPrimary (citable) accession number: O70480
Secondary accession number(s): Q9D095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.