From Wikipedia, the free encyclopedia
VAMP7
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases VAMP7, SYBL1, TI-VAMP, TIVAMP, VAMP-7, vesicle associated membrane protein 7
External IDs OMIM: 300053; MGI: 1096399; HomoloGene: 4121; GeneCards: VAMP7; OMA: VAMP7 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001145149
NM_001185183
NM_005638

NM_001302138
NM_011515
NM_001359151

RefSeq (protein)

NP_001138621
NP_001172112
NP_005629

NP_001289067
NP_035645
NP_001346080

Location (UCSC) Chr X: 155.88 – 155.94 Mbn/a
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Vesicle-associated membrane protein 7 (VAMP-7), is a protein that in humans is encoded by the VAMP7 gene also known as the or SYBL1 gene. [4] [5] [6]

Function

VAMP-7 is a transmembrane protein that is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor ( SNARE) family. VAMP-7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. [6]

Interactions

VAMP-7 has been shown to interact with SNAP23 [7] [8] and AP3D1. [7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000124333Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ D'Esposito M, Ciccodicola A, Gianfrancesco F, Esposito T, Flagiello L, Mazzarella R, Schlessinger D, D'Urso M (Jul 1996). "A synaptobrevin-like gene in the Xq28 pseudoautosomal region undergoes X inactivation". Nat. Genet. 13 (2): 227–9. doi: 10.1038/ng0696-227. PMID  8640232. S2CID  8466678.
  5. ^ Filippini F, Rossi V, Galli T, Budillon A, D'Urso M, D'Esposito M (Jul 2001). "Longins: a new evolutionary conserved VAMP family sharing a novel SNARE domain". Trends Biochem. Sci. 26 (7): 407–9. doi: 10.1016/S0968-0004(01)01861-8. PMID  11440841.
  6. ^ a b "Entrez Gene: SYBL1 synaptobrevin-like 1".
  7. ^ a b Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (Jul 2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9011–6. Bibcode: 2003PNAS..100.9011M. doi: 10.1073/pnas.1431910100. PMC  166429. PMID  12853575.
  8. ^ Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D (Jun 1998). "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells". Mol. Biol. Cell. 9 (6): 1437–48. doi: 10.1091/mbc.9.6.1437. PMC  25366. PMID  9614185.

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: P51809 (Vesicle-associated membrane protein 7) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


From Wikipedia, the free encyclopedia
VAMP7
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases VAMP7, SYBL1, TI-VAMP, TIVAMP, VAMP-7, vesicle associated membrane protein 7
External IDs OMIM: 300053; MGI: 1096399; HomoloGene: 4121; GeneCards: VAMP7; OMA: VAMP7 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001145149
NM_001185183
NM_005638

NM_001302138
NM_011515
NM_001359151

RefSeq (protein)

NP_001138621
NP_001172112
NP_005629

NP_001289067
NP_035645
NP_001346080

Location (UCSC) Chr X: 155.88 – 155.94 Mbn/a
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Vesicle-associated membrane protein 7 (VAMP-7), is a protein that in humans is encoded by the VAMP7 gene also known as the or SYBL1 gene. [4] [5] [6]

Function

VAMP-7 is a transmembrane protein that is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor ( SNARE) family. VAMP-7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. [6]

Interactions

VAMP-7 has been shown to interact with SNAP23 [7] [8] and AP3D1. [7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000124333Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ D'Esposito M, Ciccodicola A, Gianfrancesco F, Esposito T, Flagiello L, Mazzarella R, Schlessinger D, D'Urso M (Jul 1996). "A synaptobrevin-like gene in the Xq28 pseudoautosomal region undergoes X inactivation". Nat. Genet. 13 (2): 227–9. doi: 10.1038/ng0696-227. PMID  8640232. S2CID  8466678.
  5. ^ Filippini F, Rossi V, Galli T, Budillon A, D'Urso M, D'Esposito M (Jul 2001). "Longins: a new evolutionary conserved VAMP family sharing a novel SNARE domain". Trends Biochem. Sci. 26 (7): 407–9. doi: 10.1016/S0968-0004(01)01861-8. PMID  11440841.
  6. ^ a b "Entrez Gene: SYBL1 synaptobrevin-like 1".
  7. ^ a b Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (Jul 2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9011–6. Bibcode: 2003PNAS..100.9011M. doi: 10.1073/pnas.1431910100. PMC  166429. PMID  12853575.
  8. ^ Galli T, Zahraoui A, Vaidyanathan VV, Raposo G, Tian JM, Karin M, Niemann H, Louvard D (Jun 1998). "A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells". Mol. Biol. Cell. 9 (6): 1437–48. doi: 10.1091/mbc.9.6.1437. PMC  25366. PMID  9614185.

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: P51809 (Vesicle-associated membrane protein 7) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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