ATL1
entrez
51062
canonical
uniprot
Q8WXF7
canonical
ensembl
ENSG00000198513
resolver
ensp
ENSP00000351155
resolver
ensp
ENSP00000413675
resolver
ensp
ENSP00000538245
resolver
genesymbol
ATL1
resolver
genesymbol_syn
GBP3
resolver
genesymbol_syn
SPG3
resolver
genesymbol_syn
SPG3A
resolver
hgnc
HGNC:11231
resolver
uniprot
A0A0S2Z5A2
resolver
uniprot
A0A0S2Z5B0
resolver
uniprot
A6NND5
resolver
uniprot
A8K2C0
resolver
uniprot
G5E9T1
resolver
uniprot
O95890
resolver
uniprot
Q53F53
resolver
uniprot
Q69YH7
resolver
uniprot
Q96FK0
resolver
uniprot_entry
A0A0S2Z5A2_HUMAN
resolver
uniprot_entry
A0A0S2Z5B0_HUMAN
resolver
uniprot_entry
ATLA1_HUMAN
resolver
uniprot_entry
Q53F53_HUMAN
resolver
uniprot_sec
A6NND5
resolver
uniprot_sec
A8K2C0
resolver
uniprot_sec
G5E9T1
resolver
uniprot_sec
O95890
resolver
uniprot_sec
Q69YH7
resolver
uniprot_sec
Q96FK0
resolver
amino_acid_sequence
MAKNRRDRNSWGGFSEKTYEWSSEEEEPVKKAGPVQVLIVKDDHSFELDETALNRILLSEAVRDKEVVAVSVAGAFRKGKSFLMDFMLRYMYNQESVDWVGDYNEPLTGFSWRGGSERETTGIQIWSEIFLINKPDGKKVAVLLMDTQGTFDSQSTLRDSATVFALSTMISSIQVYNLSQNVQEDDLQHLQLFTEYGRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLEKRLKVSGNQHEELQNVRKHIHSCFTNISCFLLPHPGLKVATNPNFDGKLKEIDDEFIKNLKILIPWLLSPESLDIKEINGNKITCRGLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVATAKDTYNKKMEEICGGDKPFLAPNDLQTKHLQLKEESVKLFRGVKKMGGEEFSRRYLQQLESEIDELYIQYIKHNDSKNIFHAARTPATLFVVIFITYVIAGVTGFIGLDIIASLCNMIMGLTLITLCTWAYIRYSGEYRELGAVIDQVAAALWDQGSTNEALYKLYSAAATHRHLYHQAFPTPKSESTEQSEKKKM
uniprot
proteins
disease_involvement
DISEASE: Spastic paraplegia 3, autosomal dominant (SPG3) [MIM:182600]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. {ECO:0000269|PubMed:11685207, ECO:0000269|PubMed:12112092, ECO:0000269|PubMed:12939451, ECO:0000269|PubMed:14695538, ECO:0000269|PubMed:15184642, ECO:0000269|PubMed:16533974, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:17427918, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283, ECO:0000269|PubMed:21336785, ECO:0000269|PubMed:23483706, ECO:0000269|PubMed:24473461, ECO:0000269|PubMed:24604904, ECO:0000269|PubMed:34817557}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuropathy, hereditary sensory, 1D (HSN1D) [MIM:613708]: A disease characterized by adult-onset distal axonal sensory neuropathy leading to mutilating ulcerations as well as hyporeflexia. Some patients may show features suggesting upper neuron involvement. {ECO:0000269|PubMed:21194679}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Atlastin-1 (ATL1) is a membrane-anchored GTPase that mediates the GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the continuous ER network. It facilitates the formation of three-way junctions where ER tubules intersect (PubMed:14506257, PubMed:18270207, PubMed:19665976, PubMed:27619977, PubMed:34817557, PubMed:38509071). Two atlastin-1 on neighboring ER tubules bind GTP and form loose homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon GTP hydrolysis, the 3HB regions tighten, pulling the membranes together to drive their fusion. After fusion, the homodimer disassembles upon release of inorganic phosphate (Pi). Subsequently, GDP dissociates, resetting the monomers to a conformation ready for a new fusion cycle (PubMed:14506257, PubMed:21220294, PubMed:21368113, PubMed:23334294, PubMed:38509071). May also regulate more or less directly Golgi biogenesis (PubMed:17321752). Indirectly regulates axonal development (By similarity). {ECO:0000250|UniProtKB:Q6PST4, ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:21368113, ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:34817557, ECO:0000269|PubMed:38509071}.
uniprot
proteins
mass_dalton
63544
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="S->A: No effect on GTPase-dependent fusogenic activity. No effect on the membrane tethering step."; /evidence="ECO:0000305|PubMed:34546351"; MUTAGEN 10; /note="S->E: Decreased GTPase-dependent fusogenic activity. Specifically alters the membrane tethering step."; /evidence="ECO:0000305|PubMed:34546351"; MUTAGEN 22; /note="S->A: No effect on GTPase-dependent fusogenic activity; when associated with A-23."; /evidence="ECO:0000269|PubMed:34817557"; MUTAGEN 22; /note="S->E: No effect on GTPase-dependent fusogenic activity. No effect on the membrane tethering step; when associated with E-23."; /evidence="ECO:0000305|PubMed:34546351"; MUTAGEN 23; /note="S->A: No effect on GTPase-dependent fusogenic activity; when associated with A-22."; /evidence="ECO:0000269|PubMed:34817557"; MUTAGEN 23; /note="S->E: No effect on GTPase-dependent fusogenic activity. No effect on the membrane tethering step; when associated with E-22."; /evidence="ECO:0000305|PubMed:34546351"; MUTAGEN 77; /note="R->A: Abolishes GTPase activity and impairs homodimerization."; /evidence="ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:23334294"; MUTAGEN 77; /note="R->E: Abolishes homodimerization. Loss of GTPase-dependent fusogenic activity."; /evidence="ECO:0000269|PubMed:21220294, ECO:0000269|PubMed:23334294, ECO:0000269|PubMed:34817557"; MUTAGEN 80; /note="K->A: Changed endoplasmic reticulum tubular network organization. Alters endoplasmic reticulum morphogenesis."; /evidence="ECO:0000269|PubMed:27619977, ECO:0000305|PubMed:18270207"; MUTAGEN 151; /note="F->S: Changed endoplasmic reticulum tubular network organization. Endoplasmic reticulum and Golgi morphology are affected."; /evidence="ECO:0000305|PubMed:17321752"; MUTAGEN 162; /note="T->P: Changed endoplasmic reticulum tubular network organization. Endoplasmic reticulum and Golgi morphology are affected."; /evidence="ECO:0000269|PubMed:17321752"; MUTAGEN 191; /note="Q->R: Abolishes homodimerization."; /evidence="ECO:0000269|PubMed:21220294"; MUTAGEN 247; /note="H->R: Impairs homodimerization and GTPase activity."; /evidence="ECO:0000269|PubMed:21220294"; MUTAGEN 398; /note="S->Y: Changed endoplasmic reticulum tubular network organization. Alters homodimerization. Endoplasmic reticulum and Golgi morphology are affected."; /evidence="ECO:0000269|PubMed:38509071, ECO:0000305|PubMed:17321752"; MUTAGEN 443; /note="H->P: Changed endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:38509071"; MUTAGEN 507; /note="I->D: Loss of GTPase-dependent fusogenic activity."; /evidence="ECO:0000269|PubMed:34817557
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation, by different kinases, of the N-terminal hypervariable region (HVR) regulates the ATL1-mediated membrane tethering step. {ECO:0000269|PubMed:34546351}.
uniprot
proteins
protein_family
GB1 subfamily
uniprot
proteins
protein_family
GB1/RHD3 GTPase family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
11685207
uniprot
proteins
pubmed
12112092
uniprot
proteins
pubmed
12387898
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12939451
uniprot
proteins
pubmed
14506257
uniprot
proteins
pubmed
14695538
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15184642
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16339213
uniprot
proteins
pubmed
16533974
uniprot
proteins
pubmed
16815977
uniprot
proteins
pubmed
17321752
uniprot
proteins
pubmed
17427918
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18270207
uniprot
proteins
pubmed
19665976
uniprot
proteins
pubmed
20200447
uniprot
proteins
pubmed
20718791
uniprot
proteins
pubmed
20932283
uniprot
proteins
pubmed
21194679
uniprot
proteins
pubmed
21220294
uniprot
proteins
pubmed
21336785
uniprot
proteins
pubmed
21368113
uniprot
proteins
pubmed
23334294
uniprot
proteins
pubmed
23483706
uniprot
proteins
pubmed
23969831
uniprot
proteins
pubmed
24473461
uniprot
proteins
pubmed
24604904
uniprot
proteins
pubmed
25751282
uniprot
proteins
pubmed
27619977
uniprot
proteins
pubmed
34546351
uniprot
proteins
pubmed
34817557
uniprot
proteins
pubmed
38509071
uniprot
proteins
sequence_length
558
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:16339213, ECO:0000269|PubMed:17321752, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257}. Golgi apparatus membrane {ECO:0000269|PubMed:14506257, ECO:0000269|PubMed:17321752}; Multi-pass membrane protein {ECO:0000269|PubMed:14506257}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PST4}. Note=Localizes to endoplasmic reticulum tubular network (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
uniprot
proteins
transmembrane_region
TRANSMEM 450..470; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 472..492; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins