ACTG2
entrez
72
canonical
uniprot
P63267
canonical
ensembl
ENSG00000163017
resolver
ensp
ENSP00000295137
resolver
ensp
ENSP00000386929
resolver
genesymbol
ACTG2
resolver
genesymbol_syn
ACTA3
resolver
genesymbol_syn
ACTL3
resolver
genesymbol_syn
ACTSG
resolver
hgnc
HGNC:145
resolver
uniprot
B2R7E7
resolver
uniprot
B4E315
resolver
uniprot
D6W5H8
resolver
uniprot
E9PG30
resolver
uniprot
P12718
resolver
uniprot
Q504R1
resolver
uniprot
Q6FI22
resolver
uniprot_entry
ACTH_HUMAN
resolver
uniprot_sec
B2R7E7
resolver
uniprot_sec
B4E315
resolver
uniprot_sec
D6W5H8
resolver
uniprot_sec
E9PG30
resolver
uniprot_sec
P12718
resolver
uniprot_sec
Q504R1
resolver
uniprot_sec
Q6FI22
resolver
amino_acid_sequence
MCEEETTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKPEYDEAGPSIVHRKCF
uniprot
proteins
disease_involvement
DISEASE: Visceral myopathy 1 (VSCM1) [MIM:155310]: An autosomal dominant form of myopathic pseudo-obstruction characterized by impaired function of enteric smooth muscle cells, resulting in abnormal intestinal motility, severe abdominal pain, malnutrition, and even death. The disease shows inter- and intrafamilial variability. Most severely affected patients exhibit prenatal bladder enlargement, intestinal malrotation, neonatal functional gastrointestinal obstruction, and dependence on total parenteral nutrition and urinary catheterization. {ECO:0000269|PubMed:22960657, ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:24777424, ECO:0000269|PubMed:26647307, ECO:0000269|PubMed:27481187, ECO:0000269|PubMed:29781137, ECO:0000269|PubMed:33294969, ECO:0000269|PubMed:33880338}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome 5 (MMIHS5) [MIM:619431]: A form of megacystis-microcolon-intestinal hypoperistalsis syndrome, a congenital visceral myopathy primarily affecting females, and characterized by loss of smooth muscle contraction in the bladder and intestine. Affected individuals present at birth with functional obstruction of intestine, microcolon, dilation of bladder, and secondary hydronephrosis. The majority of cases have a fatal outcome due to malnutrition and sepsis, followed by multiorgan failure. MMIHS5 is an autosomal dominant form with significant inter- and intrafamilial variability. {ECO:0000269|PubMed:24337657, ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:26647307, ECO:0000269|PubMed:27481187, ECO:0000269|PubMed:28422808, ECO:0000269|PubMed:29781137, ECO:0000269|PubMed:33294969}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
uniprot
proteins
mass_dalton
41877
uniprot
proteins
mutagenesis
MUTAGEN 72; /note="I->A,D,K: Abolished methylation by SETD3."; /evidence="ECO:0000269|PubMed:31993215"; MUTAGEN 72; /note="I->L,M: Slightly decreased methylation by SETD3."; /evidence="ECO:0000269|PubMed:31993215
uniprot
proteins
post_translational_modification
PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin repolymerization. {ECO:0000250|UniProtKB:P63268}.; PTM: [Actin, gamma-enteric smooth muscle, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. {ECO:0000250|UniProtKB:P62737}.; PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P68133}.; PTM: Methylated at His-74 by SETD3. {ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:31993215}.; PTM: (Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-51 of one monomer and Glu-271 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148). {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}.
uniprot
proteins
protein_family
Actin family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
1710027
uniprot
proteins
pubmed
19015515
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22960657
uniprot
proteins
pubmed
2377475
uniprot
proteins
pubmed
24337657
uniprot
proteins
pubmed
24676022
uniprot
proteins
pubmed
24777424
uniprot
proteins
pubmed
26228148
uniprot
proteins
pubmed
26647307
uniprot
proteins
pubmed
27481187
uniprot
proteins
pubmed
28422808
uniprot
proteins
pubmed
29781137
uniprot
proteins
pubmed
30626964
uniprot
proteins
pubmed
31993215
uniprot
proteins
pubmed
33294969
uniprot
proteins
pubmed
33880338
uniprot
proteins
sequence_length
376
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
uniprot
proteins