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DROME:ATLAS

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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 Evidence Code with/from Aspect Notes Status
GO:0016050

vesicle organization

PMID:19573020[1]

IDA: Inferred from Direct Assay

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]

IDA: Inferred from Direct Assay

P

Fig. 3. Atlastin induces formation of tubules characteristic of the ER.

complete
CACAO 9017

GO:0071787

PMID:19573020[1]

IMP: Inferred from Mutant Phenotype

Fig. 4. Vesicle formation from swollen tubules or ER.

complete
CACAO 9018

GO:0000139

Golgi membrane

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0134

C

Seeded From UniProt

complete

GO:0000166

nucleotide binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

GO:0003924

GTPase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003191
InterPro:IPR015894

F

Seeded From UniProt

complete

GO:0003924

GTPase activity

PMID:19633650[2]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0003924

GTPase activity

PMID:19633650[2]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0003924

GTPase activity

PMID:21368113[3]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:19341724[4]

IPI: Inferred from Physical Interaction

UniProtKB:Q8I0P1

F

Seeded From UniProt

complete

GO:0005525

GTP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003191
InterPro:IPR015894
InterPro:IPR030386

F

Seeded From UniProt

complete

GO:0005525

GTP binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0342

F

Seeded From UniProt

complete

GO:0005525

GTP binding

PMID:19633650[2]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

complete

GO:0005737

cytoplasm

PMID:17030474[5]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005783

endoplasmic reticulum

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

GO:0005783

endoplasmic reticulum

PMID:19341724[4]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005783

endoplasmic reticulum

PMID:19633650[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

GO:0005794

Golgi apparatus

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0333

C

Seeded From UniProt

complete

GO:0005794

Golgi apparatus

PMID:19341724[4]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005794

Golgi apparatus

PMID:19341724[4]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0007019

microtubule depolymerization

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007029

endoplasmic reticulum organization

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007029

endoplasmic reticulum organization

PMID:19633650[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007030

Golgi organization

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007517

muscle organ development

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007528

neuromuscular junction development

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003191
InterPro:IPR015894

P

Seeded From UniProt

complete

GO:0008152

metabolic process

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0378

P

Seeded From UniProt

complete

GO:0008582

regulation of synaptic growth at neuromuscular junction

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0012505

endomembrane system

PMID:19317464[6]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016020

membrane

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

GO:0016020

membrane

PMID:19633650[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016021

integral component of membrane

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

GO:0016320

endoplasmic reticulum membrane fusion

PMID:19633650[2]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0016320

endoplasmic reticulum membrane fusion

PMID:19633650[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0016320

endoplasmic reticulum membrane fusion

PMID:19633650[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0016787

hydrolase activity

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

GO:0031114

regulation of microtubule depolymerization

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0031227

intrinsic component of endoplasmic reticulum membrane

PMID:19633650[2]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0032561

guanyl ribonucleotide binding

PMID:21368113[3]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

complete

GO:0042802

identical protein binding

PMID:19633650[2]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0042803

protein homodimerization activity

PMID:21368113[3]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

complete

GO:0051124

synaptic growth at neuromuscular junction

PMID:19341724[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0051260

protein homooligomerization

PMID:19633650[2]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0061025

membrane fusion

PMID:19633650[2]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0061025

membrane fusion

PMID:21368113[3]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

colocalizes_with

GO:0005874

microtubule

PMID:19341724[4]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

Notes

References

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

  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
  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 Orso, G et al. (2009) Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 460 978-83 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 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
  4. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 4.12 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
  5. 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
  6. Tan, DJ et al. (2009) Mapping organelle proteins and protein complexes in Drosophila melanogaster. J. Proteome Res. 8 2667-78 PubMed GONUTS page