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Information on EC 3.6.5.2 - small monomeric GTPase

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EC Tree
IUBMB Comments
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
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This record set is specific for:
UNIPROT: P36404
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
k-ras, cdc42, h-ras, small gtpase, ef-tu, rho gtpase, rab11, rab3a, rab27a, rap1a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-ribosylation factor-like protein 2
UniProt
small GTPase
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GTP-phosphohydrolase
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GTPase
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guanine triphosphatase
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guanosine 5'-triphosphatase
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guanosine triphosphatase
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ribosomal GTPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (cell-regulating)
A family of about 50 enzymes with a molecular mass of 21 kDa that are distantly related to the alpha-subunit of heterotrimeric G-protein GTPase (EC 3.6.5.1). They are involved in cell-growth regulation (Ras subfamily), membrane vesicle traffic and uncoating (Rab and ARF subfamilies), nuclear protein import (Ran subfamily) and organization of the cytoskeleton (Rho and Rac subfamilies).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-32-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
ARL2 plays an essential role in the cellular actions of tubulin binding cofactor B (TBCD) but, rather than competing with the binding of beta-tubulin, facilitates it. The ARL2-TBCD interaction is critical for proper maintenance of microtubule densities in cells. The TBCD-ARL2-beta-tubulin trimer represents a functional complex whose activity is fundamental to microtubule dynamics. Correlation between the ability of ARL2 and ARL2 mutants to bind TBCD and to alter microtubule dynamics in a cell-based assay
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ARL2_HUMAN
184
0
20878
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
recombinant Arl2, gel filtration
200000
Arl2-TBCD-tubulin complex, gel filtration
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F50A
site-directed mutagenesis, the mutation disrupts the interaction with TBCD, increased expression levels compared to wild-type
F50A/Q70L
site-directed mutagenesis, cells expressing mutant L3A/F50A show a reversal of the microtubule loss phenotype, with about 20% of transfected cells showing only intermediate loss in microtubule densities
I6R
site-directed mutagenesis, the mutation disrupts the interaction with TBCD
I6R/Q70L
site-directed mutagenesis, the addition of the I6R mutation to Q70L does not reverse the effects of the dominant mutant on microtubule densities
L3A
site-directed mutagenesis, the mutation disrupts the interaction with TBCD
L3A/Q70L
site-directed mutagenesis, cells expressing mutant L3A/Q70L show a reversal of the microtubule loss phenotype, with about 10% of transfected cells showing only intermediate loss in microtubule densities
Q70L
site-directed mutagenesis, ARL2 dominant activating mutation. Expression of ARL2 Q70L mutant causes the loss of polymerized microtubules in cultured cells
T30N
site-directed mutagenesis, ARL2 dominant inactivating mutation, shows decreased expression levels compared to wild-type
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant enzymes from HEK cells by glutathione affinity chromatography. Purification GST-TBCD with or withoout ARL2 from HEK cells results in the co-purification of different combinations of tubulins in novel complexes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of HA- and GST-tagged wild-type and mutant enzymes in HEK cells, recombinant optimized expression of Arl2 in HeLa cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Francis, J.W.; Newman, L.E.; Cunningham, L.A.; Kahn, R.A.
A trimer consisting of the tubulin-specific chaperone D (TBCD), regulatory GTPase ARL2, and beta-tubulin is required for maintaining the microtubule network
J. Biol. Chem.
292
4336-4349
2017
Homo sapiens (P36404), Homo sapiens
Manually annotated by BRENDA team