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InterPro: IPR010908 Longin

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714 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
Matches in BioMart

Accession

IPR010908 Longin

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.30.450.50	Longin	484
PROSITE profile	PS50859	LONGIN	695
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011012 Longin-like

GO Term annotation Help

Process

GO:0016192 vesicle-mediated transport

Component

GO:0016021 integral to membrane

InterPro annotation

Entry Details in BioMart

Abstract

VAMPs (and its homologue synaptobrevins) define a group of SNARE proteins that contain a C-terminal coiled-coil/SNARE domain, in combination with variable N-terminal domains that are used to classify VAMPs: those containing longin N-terminal domains (~150 aa) are referred to as longins, while those with shorter N-termini are referred to as brevins [1]. Longins are the only type of VAMP protein found in all eukaryotes, suggesting that their longin domain is essential. The longin domain is thought to exert a regulatory function. Longin domains have been shown to share the same structural fold, a profilin-like globular domain consisting of a five-stranded antiparallel beta-sheet that is sandwiched by an alpha-helix on one side, and two alpha-helices on the other (beta(2)-alpha-beta(3)-alpha(2)).

Structural links Help

PDB - click here

SCOP: d.110.4.1

CATH: 3.30.450.50

Database links Help

PROSITE doc: PDOC50859

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010908

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O08547 Vesicle-trafficking protein SEC22b

O08595 Vesicle-trafficking protein SEC22b

O23429 Vesicle-associated membrane protein 724

O75396 Vesicle-trafficking protein SEC22b

P36015 Synaptobrevin homolog YKT6

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010908	Longin
IPR001388	Synaptobrevin
IPR011012	Longin-like
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Dietrich LE, Boeddinghaus C, LaGrassa TJ, Ungermann C. Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins. Biochim. Biophys. Acta 1641 111-9 2003 [PubMed: 12914952] http://dx.doi.org/10.1016/S0167-4889(03)00094-6

Additional Reading Open in usermanual
	Pryor PR, Jackson L, Gray SR, Edeling MA, Thompson A, Sanderson CM, Evans PR, Owen DJ, Luzio JP. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb. Cell 134 2008 817-27 [PubMed: 18775314] http://dx.doi.org/10.1016/j.cell.2008.07.023
	Gonzalez LC Jr, Weis WI, Scheller RH. A novel snare N-terminal domain revealed by the crystal structure of Sec22b. J. Biol. Chem. 276 2001 24203-11 [PubMed: 11309394] http://dx.doi.org/10.1074/jbc.M101584200
	Filippini F, Rossi V, Galli T, Budillon A, D'Urso M, D'Esposito M. Longins: a new evolutionary conserved VAMP family sharing a novel SNARE domain. Trends Biochem. Sci. 26 2001 407-9 [PubMed: 11440841] http://dx.doi.org/10.1016/S0968-0004(01)01861-8
	Tochio H, Tsui MM, Banfield DK, Zhang M. An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p. Science 293 2001 698-702 [PubMed: 11474112] http://dx.doi.org/10.1126/science.1062950
	Pylypenko O, Schonichen A, Ludwig D, Ungermann C, Goody RS, Rak A, Geyer M. Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding. J. Mol. Biol. 377 2008 1334-45 [PubMed: 18329045] http://dx.doi.org/10.1016/j.jmb.2008.01.099

InterPro 23.1