ATL2
entrez
64225
canonical
uniprot
Q8NHH9
canonical
ensembl
ENSG00000119787
resolver
ensp
ENSP00000368237
resolver
ensp
ENSP00000385446
resolver
ensp
ENSP00000390743
resolver
ensp
ENSP00000415336
resolver
ensp
ENSP00000498813
resolver
ensp
ENSP00000610253
resolver
ensp
ENSP00000644331
resolver
enst
ENST00000406122
resolver
genesymbol
ATL2
resolver
genesymbol_syn
ARL6IP2
resolver
hgnc
HGNC:24047
resolver
uniprot
B5MCN0
resolver
uniprot
B7Z1X2
resolver
uniprot
B7Z2H0
resolver
uniprot
B7Z7X8
resolver
uniprot
Q4ZG30
resolver
uniprot
Q7Z630
resolver
uniprot
Q8NHH8
resolver
uniprot
Q9H5M7
resolver
uniprot_entry
ATLA2_HUMAN
resolver
uniprot_entry
B5MCN0_HUMAN
resolver
uniprot_entry
B7Z2H0_HUMAN
resolver
uniprot_sec
B7Z1X2
resolver
uniprot_sec
B7Z7X8
resolver
uniprot_sec
Q4ZG30
resolver
uniprot_sec
Q7Z630
resolver
uniprot_sec
Q8NHH8
resolver
uniprot_sec
Q9H5M7
resolver
activity_regulation
ACTIVITY REGULATION: [Isoform 2]: With its alternative C-terminus disrupting the autoinhibitory domain, this brain-specific isoform is probably more active at fusing ER membranes. {ECO:0000269|PubMed:34817557}.
uniprot
proteins
amino_acid_sequence
MAEGDEAARGQQPHQGLWRRRRTSDPSAAVNHVSSTTSLGENYEDDDLVNSDEVMKKPCPVQIVLAHEDDHNFELDEEALEQILLQEHIRDLNIVVVSVAGAFRKGKSFLLDFMLRYMYNKDSQSWIGGNNEPLTGFTWRGGCERETTGIQVWNEVFVIDRPNGTKVAVLLMDTQGAFDSQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTEYGRLAMEEIYQKPFQTLMFLIRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSFDGRLKDIDEDFKRELRNLVPLLLAPENLVEKEISGSKVTCRDLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVAGARDTYCKSMEQVCGGDKPYIAPSDLERKHLDLKEVAIKQFRSVKKMGGDEFCRRYQDQLEAEIEETYANFIKHNDGKNIFYAARTPATLFAVMFAMYIISGLTGFIGLNSIAVLCNLVMGLALIFLCTWAYVKYSGEFREIGTVIDQIAETLWEQVLKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Atlastin-2 (ATL2) 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:18270207, PubMed:19665976, PubMed:22065636, PubMed:27619977, PubMed:34817557). Two atlastin-2 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 (By similarity). {ECO:0000250|UniProtKB:Q8WXF7, ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:22065636, ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:34817557}.
uniprot
proteins
mass_dalton
66229
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="K->A: Alters endoplasmic reticulum morphology."; /evidence="ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:27619977"; MUTAGEN 244; /note="R->Q: Alters endoplasmic reticulum morphogenesis."; /evidence="ECO:0000269|PubMed:18270207"; MUTAGEN 372; /note="K->E: No effect on GTP-binding or GTPase activity. Loss of function in endoplasmic reticulum tubular network membrane organization. No effect on function in endoplasmic reticulum tubular network membrane organization; when associated with R-380."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 380; /note="E->A: Loss of function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 380; /note="E->R: No effect on GTP-binding or GTPase activity. Loss of function in endoplasmic reticulum tubular network membrane organization. No effect on function in endoplasmic reticulum tubular network membrane organization; when associated with E-372."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 384; /note="L->D: Loss of function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 431; /note="S->A: No effect on function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 435; /note="M->A: Loss of function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 440; /note="F->A: Decreased function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 444; /note="Y->A: No effect on function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 447; /note="Q->A: No effect on function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 454; /note="E->A: Loss of function in endoplasmic reticulum tubular network membrane organization."; /evidence="ECO:0000269|PubMed:22065636"; MUTAGEN 555; /note="E->K: Increased GTPase-dependent fusogenic activity."; /evidence="ECO:0000269|PubMed:34817557"; MUTAGEN 556; /note="E->K: Increased GTPase-dependent fusogenic activity."; /evidence="ECO:0000269|PubMed:34817557"; MUTAGEN 559; /note="R->E: Increased GTPase-dependent fusogenic activity."; /evidence="ECO:0000269|PubMed:34817557
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
14506257
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18270207
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19665976
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22065636
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23969831
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27619977
uniprot
proteins
pubmed
34817557
uniprot
proteins
sequence_length
583
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18270207, ECO:0000269|PubMed:22065636, ECO:0000269|PubMed:27619977}; Multi-pass membrane protein {ECO:0000269|PubMed:18270207}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions (PubMed:27619977). {ECO:0000269|PubMed:27619977}.
uniprot
proteins
transmembrane_region
TRANSMEM 477..497; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 500..520; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins