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Actin, gamma-enteric smooth muscle (Alpha-actin-3) (Gamma-2-actin) (Smooth muscle gamma-actin) [Cleaved into: Actin, gamma-enteric smooth muscle, intermediate form]

 ACTH_HUMAN              Reviewed;         376 AA.
P63267; B2R7E7; B4E315; D6W5H8; E9PG30; P12718; Q504R1; Q6FI22;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
18-SEP-2019, entry version 142.
RecName: Full=Actin, gamma-enteric smooth muscle;
AltName: Full=Alpha-actin-3;
AltName: Full=Gamma-2-actin;
AltName: Full=Smooth muscle gamma-actin;
Contains:
RecName: Full=Actin, gamma-enteric smooth muscle, intermediate form;
Flags: Precursor;
Name=ACTG2; Synonyms=ACTA3, ACTL3, ACTSG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Stomach;
PubMed=2377475; DOI=10.1093/nar/18.14.4263;
Miwa T., Kamada S., Kakunaga T.;
"The nucleotide sequence of a human smooth muscle (enteric type)
gamma-actin cDNA.";
Nucleic Acids Res. 18:4263-4263(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1710027; DOI=10.1128/mcb.11.6.3296;
Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G.,
Ueyama H., Kakunaga T.;
"Structure, chromosome location, and expression of the human smooth
muscle (enteric type) gamma-actin gene: evolution of six human actin
genes.";
Mol. Cell. Biol. 11:3296-3306(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
PubMed=19015515; DOI=10.1073/pnas.0808082105;
Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J.,
Reisler E.;
"Connecting actin monomers by iso-peptide bond is a toxicity mechanism
of the Vibrio cholerae MARTX toxin.";
Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-3, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
PubMed=26228148; DOI=10.1126/science.aab4090;
Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C.,
Winkelman J.D., Birukov K.G., Kotha S.R., Parinandi N.L.,
Vavylonis D., Kovar D.R., Kudryashov D.S.;
"ACD toxin-produced actin oligomers poison formin-controlled actin
polymerization.";
Science 349:535-539(2015).
[11]
METHYLATION AT HIS-74.
PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
"SETD3 is an actin histidine methyltransferase that prevents primary
dystocia.";
Nature 565:372-376(2019).
[12]
VARIANT VSCM SER-148.
PubMed=22960657; DOI=10.1053/j.gastro.2012.08.045;
Lehtonen H.J., Sipponen T., Tojkander S., Karikoski R., Jarvinen H.,
Laing N.G., Lappalainen P., Aaltonen L.A., Tuupanen S.;
"Segregation of a missense variant in enteric smooth muscle actin
gamma-2 with autosomal dominant familial visceral myopathy.";
Gastroenterology 143:1482-1491(2012).
[13]
VARIANT VSCM SER-148.
PubMed=24777424; DOI=10.1055/s-0034-1365142;
Holla O.L., Bock G., Busk O.L., Isfoss B.L.;
"Familial visceral myopathy diagnosed by exome sequencing of a patient
with chronic intestinal pseudo-obstruction.";
Endoscopy 46:533-537(2014).
[14]
VARIANTS VSCM CYS-178 AND LEU-178, AND CHARACTERIZATION OF VARIANTS
VSCM CYS-178 AND LEU-178.
PubMed=24337657; DOI=10.1007/s00439-013-1406-0;
Thorson W., Diaz-Horta O., Foster J. II, Spiliopoulos M., Quintero R.,
Farooq A., Blanton S., Tekin M.;
"De novo ACTG2 mutations cause congenital distended bladder,
microcolon, and intestinal hypoperistalsis.";
Hum. Genet. 133:737-742(2014).
[15]
VARIANTS VSCM CYS-40; HIS-40; THR-45; GLY-63; LEU-110; ASN-134;
CYS-178; HIS-178; ASP-198 AND CYS-257.
PubMed=24676022; DOI=10.1371/journal.pgen.1004258;
Baylor-Hopkins Center for Mendelian Genomics;
Wangler M.F., Gonzaga-Jauregui C., Gambin T., Penney S., Moss T.,
Chopra A., Probst F.J., Xia F., Yang Y., Werlin S., Eglite I.,
Kornejeva L., Bacino C.A., Baldridge D., Neul J., Lehman E.L.,
Larson A., Beuten J., Muzny D.M., Jhangiani S., Gibbs R.A.,
Lupski J.R., Beaudet A.;
"Heterozygous de novo and inherited mutations in the smooth muscle
actin (ACTG2) gene underlie megacystis-microcolon-intestinal
hypoperistalsis syndrome.";
PLoS Genet. 10:E1004258-E1004258(2014).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells.
-!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
structural filament (F-actin) in the form of a two-stranded helix.
Each actin can bind to 4 others.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63267-1; Sequence=Displayed;
Name=2;
IsoId=P63267-2; Sequence=VSP_045861;
Note=No experimental confirmation available.;
-!- 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: 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}.
-!- 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}.
-!- DISEASE: Visceral myopathy (VSCM) [MIM:155310]: A rare inherited
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:24337657,
ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:24777424}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
alpha, beta and gamma have been identified. The alpha actins are
found in muscle tissues and are a major constituent of the
contractile apparatus. The beta and gamma actins coexist in most
cell types as components of the cytoskeleton and as mediators of
internal cell motility.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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EMBL; X16940; CAA34814.1; -; mRNA.
EMBL; D00654; BAA00546.1; -; Genomic_DNA.
EMBL; AK304523; BAG65327.1; -; mRNA.
EMBL; AK312955; BAG35794.1; -; mRNA.
EMBL; CR536515; CAG38753.1; -; mRNA.
EMBL; CR541794; CAG46593.1; -; mRNA.
EMBL; AC073046; AAX88909.1; -; Genomic_DNA.
EMBL; CH471053; EAW99713.1; -; Genomic_DNA.
EMBL; BC012617; AAH12617.1; -; mRNA.
EMBL; BC094877; AAH94877.1; -; mRNA.
CCDS; CCDS1930.1; -. [P63267-1]
CCDS; CCDS56124.1; -. [P63267-2]
PIR; A40261; A40261.
RefSeq; NP_001186822.1; NM_001199893.1. [P63267-2]
RefSeq; NP_001606.1; NM_001615.3. [P63267-1]
SMR; P63267; -.
BioGrid; 106587; 20.
CORUM; P63267; -.
IntAct; P63267; 12.
MINT; P63267; -.
STRING; 9606.ENSP00000386857; -.
iPTMnet; P63267; -.
PhosphoSitePlus; P63267; -.
SwissPalm; P63267; -.
BioMuta; ACTG2; -.
DMDM; 54036679; -.
OGP; P12718; -.
jPOST; P63267; -.
MassIVE; P63267; -.
MaxQB; P63267; -.
PaxDb; P63267; -.
PeptideAtlas; P63267; -.
PRIDE; P63267; -.
ProteomicsDB; 20231; -.
ProteomicsDB; 57515; -. [P63267-1]
DNASU; 72; -.
Ensembl; ENST00000345517; ENSP00000295137; ENSG00000163017. [P63267-1]
Ensembl; ENST00000409624; ENSP00000386857; ENSG00000163017. [P63267-1]
Ensembl; ENST00000409731; ENSP00000386929; ENSG00000163017. [P63267-2]
GeneID; 72; -.
KEGG; hsa:72; -.
UCSC; uc002sjw.4; human. [P63267-1]
CTD; 72; -.
DisGeNET; 72; -.
GeneCards; ACTG2; -.
GeneReviews; ACTG2; -.
HGNC; HGNC:145; ACTG2.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTG2; -.
MIM; 102545; gene.
MIM; 155310; phenotype.
neXtProt; NX_P63267; -.
OpenTargets; ENSG00000163017; -.
Orphanet; 2604; Familial visceral myopathy.
Orphanet; 2241; Megacystis-microcolon-intestinal hypoperistalsis syndrome.
Orphanet; 104077; Myopathic intestinal pseudoobstruction.
PharmGKB; PA24469; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00940000154148; -.
HOGENOM; HOG000233340; -.
InParanoid; P63267; -.
KO; K12315; -.
OMA; IXMESAG; -.
OrthoDB; 649708at2759; -.
PhylomeDB; P63267; -.
TreeFam; TF354237; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
SignaLink; P63267; -.
SIGNOR; P63267; -.
ChiTaRS; ACTG2; human.
GeneWiki; ACTG2; -.
GenomeRNAi; 72; -.
Pharos; P63267; -.
PMAP-CutDB; P63267; -.
PRO; PR:P63267; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163017; Expressed in 195 organ(s), highest expression level in myometrium.
ExpressionAtlas; P63267; baseline and differential.
Genevisible; P63267; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0032982; C:myosin filament; ISS:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0006936; P:muscle contraction; TAS:Reactome.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR004001; Actin_CS.
PANTHER; PTHR11937; PTHR11937; 1.
Pfam; PF00022; Actin; 1.
PRINTS; PR00190; ACTIN.
SMART; SM00268; ACTIN; 1.
PROSITE; PS00406; ACTINS_1; 1.
PROSITE; PS00432; ACTINS_2; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Isopeptide bond;
Methylation; Muscle protein; Nucleotide-binding; Oxidation;
Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 376 Actin, gamma-enteric smooth muscle,
intermediate form.
{ECO:0000250|UniProtKB:P62737}.
/FTId=PRO_0000442949.
CHAIN 3 376 Actin, gamma-enteric smooth muscle.
/FTId=PRO_0000442950.
MOD_RES 2 2 N-acetylcysteine; in intermediate form.
{ECO:0000250|UniProtKB:P62737}.
MOD_RES 3 3 N-acetylglutamate; in Actin, gamma-
enteric smooth muscle.
{ECO:0000244|PubMed:22223895}.
MOD_RES 45 45 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P63268}.
MOD_RES 48 48 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P63268}.
MOD_RES 74 74 Tele-methylhistidine.
{ECO:0000269|PubMed:30626964}.
CROSSLNK 51 51 Isoglutamyl lysine isopeptide (Lys-Glu)
(interchain with E-271); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
CROSSLNK 271 271 Isoglutamyl lysine isopeptide (Glu-Lys)
(interchain with K-51); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
VAR_SEQ 43 85 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045861.
VARIANT 40 40 R -> C (in VSCM; dbSNP:rs587777385).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071279.
VARIANT 40 40 R -> H (in VSCM; dbSNP:rs587777386).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071280.
VARIANT 45 45 M -> T (in VSCM; dbSNP:rs864309490).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071281.
VARIANT 63 63 R -> G (in VSCM; dbSNP:rs864309491).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071282.
VARIANT 110 110 P -> L (in VSCM).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071283.
VARIANT 134 134 Y -> N (in VSCM; dbSNP:rs587777388).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071284.
VARIANT 148 148 R -> S (in VSCM; dbSNP:rs587777383).
{ECO:0000269|PubMed:22960657,
ECO:0000269|PubMed:24777424}.
/FTId=VAR_071285.
VARIANT 178 178 R -> C (in VSCM; interferes with proper
polymerization into thin filaments
leading to impaired contractility of the
smooth muscle; dbSNP:rs78001248).
{ECO:0000269|PubMed:24337657,
ECO:0000269|PubMed:24676022}.
/FTId=VAR_071286.
VARIANT 178 178 R -> H (in VSCM; dbSNP:rs587777384).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071287.
VARIANT 178 178 R -> L (in VSCM; interferes with proper
polymerization into thin filaments
leading to impaired contractility of the
smooth muscle; dbSNP:rs587777384).
{ECO:0000269|PubMed:24337657}.
/FTId=VAR_071288.
VARIANT 198 198 G -> D (in VSCM; dbSNP:rs864309492).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071289.
VARIANT 257 257 R -> C (in VSCM; dbSNP:rs587777387).
{ECO:0000269|PubMed:24676022}.
/FTId=VAR_071290.
CONFLICT 130 130 V -> F (in Ref. 4; CAG38753).
{ECO:0000305}.
CONFLICT 157 157 G -> C (in Ref. 3; BAG65327).
{ECO:0000305}.
SEQUENCE 376 AA; 41877 MW; 6EC08CD5EEAD445E CRC64;
MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM
TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD
LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
PEYDEAGPSI VHRKCF


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WP1380: Regulation of Actin Cytoskeleton
WP351: Regulation of Actin Cytoskeleton
WP824: Regulation of Actin Cytoskeleton
WP1178: Regulation of Actin Cytoskeleton
WP511: FAS pathway and Stress induction of HSP regulation
WP1225: estrogen signalling
WP902: FAS pathway and Stress induction of HSP regulation
WP314: FAS pathway and Stress induction of HSP regulation
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Related Genes :
[psbX] Photosystem II reaction center X protein
[ndhA] NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1)
[KK1_045969] 40S ribosomal protein SA
[KK1_006657] Uncharacterized protein
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[KK1_031928] Tyrosine N-monooxygenase
[] UDP-glycosyltransferase homolog (Fragment)
[ndhA] NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1)
[KK1_005898] Secologanin synthase
[ndhD] NAD(P)H-quinone oxidoreductase chain 4, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, chain 4) (NADH-plastoquinone oxidoreductase chain 4)
[psbH] Photosystem II reaction center protein H (PSII-H)
[KK1_044146] Uncharacterized protein
[petB] Cytochrome b6
[ARD1] 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (EC 1.13.11.54) (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD) (Fe-ARD)
[COB] Cytochrome b (Fragment)
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5)
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[atpF] ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I)
[malate dehydrogenase] Malate dehydrogenase
[ndhE] NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 4L) (NADH-plastoquinone oxidoreductase subunit 4L)
[g.33360] 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (Fragment)
[ndhI] NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I)
[ndhK] NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit K) (NADH-plastoquinone oxidoreductase subunit K)
[psbA] Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein)
[LOC101502735] Lipoxygenase (EC 1.13.11.-)
[AM588_10001736] Uncharacterized protein
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[LOC101491357] cytochrome P450 734A1-like isoform X1
[psbI] Photosystem II reaction center protein I (PSII-I) (PSII 4.8 kDa protein)
[petB] Cytochrome b6

Bibliography :