DROME:ATLAS

Species (Taxon ID)	Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s)	atl
Protein Name(s)	Atlastin
External Links
UniProt	Q9VC57
EMBL	AE014297 AE014297 AY069079 BT004893
RefSeq	NP_001287506.1 NP_651274.1 NP_733020.1
UniGene	Dm.31277
ProteinModelPortal	Q9VC57
SMR	Q9VC57
BioGrid	67860
DIP	DIP-59281N
IntAct	Q9VC57
MINT	MINT-316814
STRING	7227.FBpp0084037
PaxDb	Q9VC57
PRIDE	Q9VC57
EnsemblMetazoa	FBtr0084656 FBtr0084657
GeneID	42934
KEGG	dme:Dmel_CG6668
UCSC	CG6668-RA
CTD	42934
FlyBase	FBgn0039213
eggNOG	NOG325148
GeneTree	ENSGT00390000008959
InParanoid	Q9VC57
KO	K17339
OMA	GILMWSD
OrthoDB	EOG7H4DTH
PhylomeDB	Q9VC57
GenomeRNAi	42934
NextBio	831354
Proteomes	UP000000803
Bgee	Q9VC57
GO	GO:0005737 GO:0012505 GO:0005783 GO:0005794 GO:0000139 GO:0016021 GO:0031227 GO:0016020 GO:0005525 GO:0003924 GO:0032561 GO:0042802 GO:0042803 GO:0016320 GO:0007029 GO:0007030 GO:0006184 GO:0061025 GO:0007019 GO:0007517 GO:0007528 GO:0051260 GO:0031114 GO:0008582 GO:0051124
Gene3D	3.40.50.300
InterPro	IPR030386 IPR003191 IPR015894 IPR027417
Pfam	PF02263
SUPFAM	SSF48340 SSF52540
PROSITE	PS51715

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0016050	vesicle organization	PMID:19573020^[1]	ECO:0000314			P	Fig. 2. Atlastin helps form vesicles with VSV-G and increases sensitivity to VSV-G.	complete CACAO 9016
	GO:0071787	endoplasmic reticulum tubular network assembly	PMID:19573020^[1]	ECO:0000314			P	Fig. 3. Atlastin induces formation of tubules characteristic of the ER.	complete CACAO 9017
	GO:0071787		PMID:19573020^[1]	ECO:0000315				Fig. 4. Vesicle formation from swollen tubules or ER.	complete CACAO 9018
involved_in	GO:0061025	membrane fusion	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051124	synaptic growth at neuromuscular junction	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016320	endoplasmic reticulum membrane fusion	PMID:19633650^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007517	muscle organ development	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007030	Golgi organization	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007029	endoplasmic reticulum organization	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007029	endoplasmic reticulum organization	PMID:19633650^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007019	microtubule depolymerization	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
colocalizes_with	GO:0005874	microtubule	PMID:19341724^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:19341724^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:19633650^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22802620^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9VC57	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21930898^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9VC57	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19633650^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9VC57	F	Seeded From UniProt	complete
involved_in	GO:0048691	positive regulation of axon extension involved in regeneration	PMID:27605706^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007029	endoplasmic reticulum organization	PMID:26906425^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0012505	endomembrane system	PMID:19317464^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21368113^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0032561	guanyl ribonucleotide binding	PMID:21368113^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21368113^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0061025	membrane fusion	PMID:21368113^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0031227	intrinsic component of endoplasmic reticulum membrane	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016320	endoplasmic reticulum membrane fusion	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016320	endoplasmic reticulum membrane fusion	PMID:19633650^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:19633650^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:19341724^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:19341724^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007528	neuromuscular junction development	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031114	regulation of microtubule depolymerization	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0008582	regulation of synaptic growth at neuromuscular junction	PMID:19341724^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17030474^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0061025	membrane fusion	PMID:23684613^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015894 InterPro:IPR036543	F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015894 InterPro:IPR030386 InterPro:IPR036543	F	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256	C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F	Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0134	C	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0097	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Muriel, MP et al. (2009) Atlastin-1, the dynamin-like GTPase responsible for spastic paraplegia SPG3A, remodels lipid membranes and may form tubules and vesicles in the endoplasmic reticulum. J. Neurochem. 110 1607-16 PubMed GONUTS page
↑ ^2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 ^2.13 Orso, G et al. (2009) Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 460 978-83 PubMed GONUTS page
↑ ^3.00 ^3.01 ^3.02 ^3.03 ^3.04 ^3.05 ^3.06 ^3.07 ^3.08 ^3.09 ^3.10 ^3.11 Lee, M et al. (2009) Drosophila Atlastin regulates the stability of muscle microtubules and is required for synapse development. Dev. Biol. 330 250-62 PubMed GONUTS page
↑ Liu, TY et al. (2012) Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion. Proc. Natl. Acad. Sci. U.S.A. 109 E2146-54 PubMed GONUTS page
↑ Pendin, D et al. (2011) GTP-dependent packing of a three-helix bundle is required for atlastin-mediated fusion. Proc. Natl. Acad. Sci. U.S.A. 108 16283-8 PubMed GONUTS page
↑ Rao, K et al. (2016) Spastin, atlastin, and ER relocalization are involved in axon but not dendrite regeneration. Mol. Biol. Cell 27 3245-3256 PubMed GONUTS page
↑ Summerville, JB et al. (2016) The effects of ER morphology on synaptic structure and function in Drosophila melanogaster. J. Cell. Sci. 129 1635-48 PubMed GONUTS page
↑ Tan, DJ et al. (2009) Mapping organelle proteins and protein complexes in Drosophila melanogaster. J. Proteome Res. 8 2667-78 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Bian, X et al. (2011) Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes. Proc. Natl. Acad. Sci. U.S.A. 108 3976-81 PubMed GONUTS page
↑ Lee, Y et al. (2008) Loss of spastic paraplegia gene atlastin induces age-dependent death of dopaminergic neurons in Drosophila. Neurobiol. Aging 29 84-94 PubMed GONUTS page
↑ Klemm, RW et al. (2013) A conserved role for atlastin GTPases in regulating lipid droplet size. Cell Rep 3 1465-75 PubMed GONUTS page

[PMID:19573020-1] 1.0 ^1.1 ^1.2 Muriel, MP et al. (2009) Atlastin-1, the dynamin-like GTPase responsible for spastic paraplegia SPG3A, remodels lipid membranes and may form tubules and vesicles in the endoplasmic reticulum. J. Neurochem. 110 1607-16 PubMed GONUTS page

[PMID:19633650-2] 2.00 ^2.01 ^2.02 ^2.03 ^2.04 ^2.05 ^2.06 ^2.07 ^2.08 ^2.09 ^2.10 ^2.11 ^2.12 ^2.13 Orso, G et al. (2009) Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 460 978-83 PubMed GONUTS page

[PMID:19341724-3] 3.00 ^3.01 ^3.02 ^3.03 ^3.04 ^3.05 ^3.06 ^3.07 ^3.08 ^3.09 ^3.10 ^3.11 Lee, M et al. (2009) Drosophila Atlastin regulates the stability of muscle microtubules and is required for synapse development. Dev. Biol. 330 250-62 PubMed GONUTS page

[PMID:22802620-4] Liu, TY et al. (2012) Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion. Proc. Natl. Acad. Sci. U.S.A. 109 E2146-54 PubMed GONUTS page

[PMID:21930898-5] Pendin, D et al. (2011) GTP-dependent packing of a three-helix bundle is required for atlastin-mediated fusion. Proc. Natl. Acad. Sci. U.S.A. 108 16283-8 PubMed GONUTS page

[PMID:27605706-6] Rao, K et al. (2016) Spastin, atlastin, and ER relocalization are involved in axon but not dendrite regeneration. Mol. Biol. Cell 27 3245-3256 PubMed GONUTS page

[PMID:26906425-7] Summerville, JB et al. (2016) The effects of ER morphology on synaptic structure and function in Drosophila melanogaster. J. Cell. Sci. 129 1635-48 PubMed GONUTS page

[PMID:19317464-8] Tan, DJ et al. (2009) Mapping organelle proteins and protein complexes in Drosophila melanogaster. J. Proteome Res. 8 2667-78 PubMed GONUTS page

[PMID:21368113-9] 9.0 ^9.1 ^9.2 ^9.3 Bian, X et al. (2011) Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes. Proc. Natl. Acad. Sci. U.S.A. 108 3976-81 PubMed GONUTS page

[PMID:17030474-10] Lee, Y et al. (2008) Loss of spastic paraplegia gene atlastin induces age-dependent death of dopaminergic neurons in Drosophila. Neurobiol. Aging 29 84-94 PubMed GONUTS page

[PMID:23684613-11] Klemm, RW et al. (2013) A conserved role for atlastin GTPases in regulating lipid droplet size. Cell Rep 3 1465-75 PubMed GONUTS page

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DROME:ATLAS

Contents

Annotations

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References

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