P70280 (VAMP7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vesicle-associated membrane protein 7
Short name=VAMP-7

Alternative name(s):
Synaptobrevin-like protein 1

Gene names

Name:	Vamp7
Synonyms:	Sybl1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation. Ref.5
Subunit structure	Component of the SNARE complex composed of Stx4, Snap23 and Vamp7 that binds Syt7 during lysosomal exocytosis. Component of the SNARE complex composed of Stx7, Stx8, Vamp7 and Vti1b that is required for heterotypic fusion of late endosomes with lysosomes in liver cells By similarity.
Subcellular location	Cytoplasmic vesicle › secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus › trans-Golgi network membrane; Single-pass type IV membrane protein By similarity. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass type IV membrane protein By similarity. Cytoplasmic vesicle › phagosome membrane; Single-pass type IV membrane protein. Cell junction › synapse › synaptosome. Note: In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney By similarity. Ref.5 Ref.6
Miscellaneous	Loss-of-function mutant (antisense inhibition) displays impaired receptor-mediated phagocytosis.
Sequence similarities	Belongs to the synaptobrevin family. Contains 1 longin domain. Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
Biological process	Exocytosis Protein transport Transport
Cellular component	Cell junction Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Synapse Synaptosome
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from sequence or structural similarity PubMed 16495485. Source: UniProtKB Golgi to plasma membrane protein transport Inferred from mutant phenotype PubMed 20582536. Source: MGI calcium ion-dependent exocytosis Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB endosome to lysosome transport Inferred from sequence or structural similarity PubMed 10888671. Source: UniProtKB eosinophil degranulation Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB neutrophil degranulation Inferred from sequence or structural similarity PubMed 14993220. Source: UniProtKB phagocytosis, engulfment Inferred from sequence or structural similarity PubMed 15133481. Source: UniProtKB regulation of protein targeting to vacuolar membrane Inferred from mutant phenotype PubMed 18227281. Source: MGI triglyceride transport Inferred from electronic annotation. Source: Compara vesicle fusion Inferred from sequence or structural similarity PubMed 10888671. Source: UniProtKB vesicle fusion with Golgi apparatus Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 18321981. Source: MGI SNARE complex Inferred from sequence or structural similarity PubMed 15133481. Source: UniProtKB apical part of cell Inferred from direct assay PubMed 14758363. Source: MGI cell junction Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum membrane Inferred from sequence or structural similarity PubMed 16495485. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome membrane Inferred from sequence or structural similarity PubMed 10459012. Source: UniProtKB lysosomal membrane Inferred from sequence or structural similarity PubMed 10459012. Source: UniProtKB neuron projection Inferred from direct assay Ref.6. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 18321981. Source: MGI phagocytic vesicle Inferred from direct assay Ref.5. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW transport vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 220

219

Vesicle-associated membrane protein 7

PRO_0000316087

Regions

Topological domain

2 – 188

187

Cytoplasmic Potential

Transmembrane

189 – 209

21

Helical; Anchor for type IV membrane protein; Potential

Topological domain

210 – 220

11

Vesicular Potential

Domain

7 – 110

104

Longin

Domain

125 – 185

61

v-SNARE coiled-coil homology

Compositional bias

191 – 195

5

Poly-Ile

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Secondary structure

1

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220

Helix Strand Turn

Details...

Beta strand

2 – 10

9

Beta strand

13 – 23

11

Helix

25 – 33

9

Beta strand

38 – 47

10

Beta strand

50 – 57

8

Beta strand

60 – 67

8

Helix

72 – 90

19

Helix

91 – 95

5

Turn

99 – 102

4

Helix

103 – 118

16

Helix

130 – 134

5

Turn

135 – 138

4

Beta strand

151 – 153

3

Sequences

	Sequence		Length	Mass (Da)
	P70280 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 109DBA4BE5772B0C	FASTA	220	24,967
	10 20 30 40 50 60 MAILFAVVAR GTTILAKHAW CGGNFLEVTE QILAKIPSEN NKLTYSHGNY LFHYICQDRI 70 80 90 100 110 120 VYLCITDDDF ERSRAFSFLN EVKKRFQTTY GSRAQTALPY AMNSEFSSVL AAQLKHHSEN 130 140 150 160 170 180 KSLDKVMETQ AQVDELKGIM VRNIDLVAQR GERLELLIDK TENLVDSSVT FKTTSRNLAR 190 200 210 220 AMCMKNIKLT IIIIIVSIVF IYIIVSLLCG GFTWPNCVKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential expression pattern of XqPAR-linked genes SYBL1 and IL9R correlates with the structure and evolution of the region." D'Esposito M., Matarazzo M.R., Ciccodicola A., Strazzullo M., Mazzarella R., Quaderi N.A., Fujiwara H., Ko M.S., Rowe L.B., Ricco A., Archidiacono N., Rocchi M., Schlessinger D., D'Urso M. Hum. Mol. Genet. 6:1917-1923(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human and mouse SYBL1 gene structure and expression." Matarazzo M.R., Cuccurese M., Strazzullo M., Vacca M., Curci A., Miano M.G., Cocchia M., Mercadante G., Torino A., D'Urso M., Ciccodicola A., D'Esposito M. Gene 240:233-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[3]	"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 and NOD. Tissue: Embryo, Kidney, Spleen and Thymus.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[5]	"TI-VAMP/VAMP7 is required for optimal phagocytosis of opsonised particles in macrophages." Braun V., Fraisier V., Raposo G., Hurbain I., Sibarita J.-B., Chavrier P., Galli T., Niedergang F. EMBO J. 23:4166-4176(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse." Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V. Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X96737 mRNA. Translation: CAA65509.1.
AJ133536 , AJ133537, AJ133538, AJ133539, AJ133540, AJ133541, AJ133542 Genomic DNA. Translation: CAB94231.1.
AK002825 mRNA. Translation: BAB22386.1.
AK011510 mRNA. Translation: BAB27667.1.
AK089035 mRNA. Translation: BAC40712.1.
AK165299 mRNA. Translation: BAE38126.1.
BC003764 mRNA. Translation: AAH03764.1.

IPI

IPI00137647.

RefSeq

NP_035645.1. NM_011515.4.

UniGene

Mm.1517.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AFI	X-ray	2.80	A/B	1-120	[»]
4B93	X-ray	2.00	A	1-188	[»]

ProteinModelPortal

P70280.

SMR

P70280. Positions 1-193.

ModBase

Search...

Protein-protein interaction databases

STRING

10090.ENSMUSP00000052262.

PTM databases

PhosphoSite

P70280.

Proteomic databases

PaxDb

P70280.

PRIDE

P70280.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000051100; ENSMUSP00000052262; ENSMUSG00000051412.

GeneID

20955.

KEGG

mmu:20955.

UCSC

uc009uym.1. mouse.

Organism-specific databases

CTD

6845.

MGI

MGI:1096399. Vamp7.

Phylogenomic databases

eggNOG

COG5143.

GeneTree

ENSGT00510000047733.

HOGENOM

HOG000042711.

HOVERGEN

HBG006675.

InParanoid

P70280.

KO

K08515.

OrthoDB

EOG49079V.

Gene expression databases

ArrayExpress

P70280.

Bgee

P70280.

CleanEx

MM_VAMP7.

Genevestigator

P70280.

Family and domain databases

Gene3D

3.30.450.50. 1 hit.

InterPro

IPR011012. Longin-like_dom.
IPR010908. Longin_dom.
IPR001388. Synaptobrevin.
[Graphical view]

Pfam

PF13774. Longin. 1 hit.
PF00957. Synaptobrevin. 1 hit.
[Graphical view]

PRINTS

PR00219. SYNAPTOBREVN.

SUPFAM

SSF64356. Longin_like. 1 hit.

PROSITE

PS50859. LONGIN. 1 hit.
PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

299904.

SOURCE

Search...

Entry information

Entry name

VAMP7_MOUSE

Accession

Primary (citable) accession number: P70280

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program