ACTH_HUMAN
ID ACTH_HUMAN Reviewed; 376 AA.
AC P63267; B2R7E7; B4E315; D6W5H8; E9PG30; P12718; Q504R1; Q6FI22;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Actin, gamma-enteric smooth muscle;
DE AltName: Full=Alpha-actin-3;
DE AltName: Full=Gamma-2-actin;
DE AltName: Full=Smooth muscle gamma-actin;
DE Contains:
DE RecName: Full=Actin, gamma-enteric smooth muscle, intermediate form;
DE Flags: Precursor;
GN Name=ACTG2; Synonyms=ACTA3, ACTL3, ACTSG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=2377475; DOI=10.1093/nar/18.14.4263;
RA Miwa T., Kamada S., Kakunaga T.;
RT "The nucleotide sequence of a human smooth muscle (enteric type) gamma-
RT actin cDNA.";
RL Nucleic Acids Res. 18:4263-4263(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1710027; DOI=10.1128/mcb.11.6.3296-3306.1991;
RA Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., Ueyama H.,
RA Kakunaga T.;
RT "Structure, chromosome location, and expression of the human smooth muscle
RT (enteric type) gamma-actin gene: evolution of six human actin genes.";
RL Mol. Cell. Biol. 11:3296-3306(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
RX PubMed=19015515; DOI=10.1073/pnas.0808082105;
RA Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
RA Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.;
RT "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of
RT the Vibrio cholerae MARTX toxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
RX PubMed=26228148; DOI=10.1126/science.aab4090;
RA Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C., Winkelman J.D.,
RA Birukov K.G., Kotha S.R., Parinandi N.L., Vavylonis D., Kovar D.R.,
RA Kudryashov D.S.;
RT "ACD toxin-produced actin oligomers poison formin-controlled actin
RT polymerization.";
RL Science 349:535-539(2015).
RN [11]
RP METHYLATION AT HIS-74.
RX PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
RA Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
RA Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
RA Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
RA Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
RT "SETD3 is an actin histidine methyltransferase that prevents primary
RT dystocia.";
RL Nature 565:372-376(2019).
RN [12] {ECO:0007744|PDB:6JAT}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 61-82 IN COMPLEX WITH SETD3,
RP METHYLATION AT HIS-74, AND MUTAGENESIS OF ILE-72.
RX PubMed=31993215; DOI=10.1038/s41421-019-0135-5;
RA Zheng Y., Zhang X., Li H.;
RT "Molecular basis for histidine N3-specific methylation of actin H73 by
RT SETD3.";
RL Cell Discov. 6:3-3(2020).
RN [13]
RP VARIANT VSCM1 SER-148.
RX PubMed=22960657; DOI=10.1053/j.gastro.2012.08.045;
RA Lehtonen H.J., Sipponen T., Tojkander S., Karikoski R., Jarvinen H.,
RA Laing N.G., Lappalainen P., Aaltonen L.A., Tuupanen S.;
RT "Segregation of a missense variant in enteric smooth muscle actin gamma-2
RT with autosomal dominant familial visceral myopathy.";
RL Gastroenterology 143:1482-1491(2012).
RN [14]
RP VARIANT VSCM1 SER-148.
RX PubMed=24777424; DOI=10.1055/s-0034-1365142;
RA Holla O.L., Bock G., Busk O.L., Isfoss B.L.;
RT "Familial visceral myopathy diagnosed by exome sequencing of a patient with
RT chronic intestinal pseudo-obstruction.";
RL Endoscopy 46:533-537(2014).
RN [15]
RP VARIANTS MMIHS5 CYS-178 AND LEU-178, CHARACTERIZATION OF VARIANTS MMIHS5
RP CYS-178 AND LEU-178, AND INVOLVEMENT IN MMIHS5.
RX PubMed=24337657; DOI=10.1007/s00439-013-1406-0;
RA Thorson W., Diaz-Horta O., Foster J. II, Spiliopoulos M., Quintero R.,
RA Farooq A., Blanton S., Tekin M.;
RT "De novo ACTG2 mutations cause congenital distended bladder, microcolon,
RT and intestinal hypoperistalsis.";
RL Hum. Genet. 133:737-742(2014).
RN [16]
RP VARIANTS MMIHS5 CYS-40; HIS-40; ASN-134; CYS-178; HIS-178 AND CYS-257,
RP VARIANTS VSCM1 HIS-40; THR-45; GLY-63; LEU-110 AND ASP-198, INVOLVEMENT IN
RP MMIHS5, AND INVOLVEMENT IN VSCM1.
RX PubMed=24676022; DOI=10.1371/journal.pgen.1004258;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA Wangler M.F., Gonzaga-Jauregui C., Gambin T., Penney S., Moss T.,
RA Chopra A., Probst F.J., Xia F., Yang Y., Werlin S., Eglite I.,
RA Kornejeva L., Bacino C.A., Baldridge D., Neul J., Lehman E.L., Larson A.,
RA Beuten J., Muzny D.M., Jhangiani S., Gibbs R.A., Lupski J.R., Beaudet A.;
RT "Heterozygous de novo and inherited mutations in the smooth muscle actin
RT (ACTG2) gene underlie megacystis-microcolon-intestinal hypoperistalsis
RT syndrome.";
RL PLoS Genet. 10:E1004258-E1004258(2014).
RN [17]
RP VARIANTS MMIHS5 CYS-178; LEU-178 AND HIS-257, VARIANT VSCM1 ILE-195,
RP INVOLVEMENT IN MMIHS5, AND INVOLVEMENT IN VSCM1.
RX PubMed=27481187; DOI=10.1002/ajmg.a.37857;
RA Moreno C.A., Metze K., Lomazi E.A., Bertola D.R., Barbosa R.H.,
RA Cosentino V., Sobreira N., Cavalcanti D.P.;
RT "Visceral myopathy: Clinical and molecular survey of a cohort of seven new
RT patients and state of the art of overlapping phenotypes.";
RL Am. J. Med. Genet. A 170:2965-2974(2016).
RN [18]
RP VARIANTS MMIHS5 CYS-40; GLN-63; CYS-178; HIS-178 AND LEU-178, INVOLVEMENT
RP IN MMIHS5, TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANTS MMIHS5 CYS-40;
RP GLN-63; CYS-178; HIS-178 AND LEU-178, AND CHARACTERIZATION OF VARIANT VSCM1
RP SER-148.
RX PubMed=26647307; DOI=10.1093/hmg/ddv497;
RA Halim D., Hofstra R.M., Signorile L., Verdijk R.M., van der Werf C.S.,
RA Sribudiani Y., Brouwer R.W., van Ijcken W.F., Dahl N., Verheij J.B.,
RA Baumann C., Kerner J., van Bever Y., Galjart N., Wijnen R.M., Tibboel D.,
RA Burns A.J., Muller F., Brooks A.S., Alves M.M.;
RT "ACTG2 variants impair actin polymerization in sporadic Megacystis
RT Microcolon Intestinal Hypoperistalsis Syndrome.";
RL Hum. Mol. Genet. 25:571-583(2016).
RN [19]
RP VARIANTS MMIHS5 HIS-40 AND CYS-257, AND INVOLVEMENT IN MMIHS5.
RX PubMed=28422808; DOI=10.1097/mpg.0000000000001608;
RA Milunsky A., Baldwin C., Zhang X., Primack D., Curnow A., Milunsky J.;
RT "Diagnosis of chronic intestinal pseudo-obstruction and megacystis by
RT sequencing the ACTG2 gene.";
RL J. Pediatr. Gastroenterol. Nutr. 65:384-387(2017).
RN [20]
RP VARIANTS VSCM1 HIS-40; LEU-148 AND CYS-257, AND VARIANT MMIHS5 CYS-40.
RX PubMed=29781137; DOI=10.1111/nmo.13371;
RA Ravenscroft G., Pannell S., O'Grady G., Ong R., Ee H.C., Faiz F., Marns L.,
RA Goel H., Kumarasinghe P., Sollis E., Sivadorai P., Wilson M., Magoffin A.,
RA Nightingale S., Freckmann M.L., Kirk E.P., Sachdev R., Lemberg D.A.,
RA Delatycki M.B., Kamm M.A., Basnayake C., Lamont P.J., Amor D.J., Jones K.,
RA Schilperoort J., Davis M.R., Laing N.G.;
RT "Variants in ACTG2 underlie a substantial number of Australasian patients
RT with primary chronic intestinal pseudo-obstruction.";
RL Neurogastroenterol. Motil. 30:e13371-e13371(2018).
RN [21]
RP VARIANT MMIHS5 HIS-40, VARIANTS VSCM1 GLN-41; PHE-143; ARG-149; ASP-196 AND
RP CYS-257, AND VARIANT TRP-336.
RX PubMed=33294969; DOI=10.1111/cge.13895;
RA Matera I., Bordo D., Di Duca M., Lerone M., Santamaria G., Pongiglione M.,
RA Lezo A., Diamanti A., Spagnuolo M.I., Pini Prato A., Alberti D.,
RA Mattioli G., Gandullia P., Ceccherini I.;
RT "Novel ACTG2 variants disclose allelic heterogeneity and bi-allelic
RT inheritance in pediatric chronic intestinal pseudo-obstruction.";
RL Clin. Genet. 99:430-436(2021).
RN [22]
RP VARIANT VSCM1 ASP-196.
RX PubMed=33880338; DOI=10.21037/tp-20-316;
RA Xiong X., Li J., Liu C., Xu F.;
RT "Visceral myopathy diagnosed by a de novo ACTG2 mutation in a patient with
RT chronic intestinal pseudo-obstruction-a case report.";
RL Transl. Pediatr. 10:679-685(2021).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. Each
CC actin can bind to 4 others.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63267-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63267-2; Sequence=VSP_045861;
CC -!- TISSUE SPECIFICITY: In the intestine, abundantly expressed in smooth
CC muscle cells of muscularis mucosa and muscularis propria. Also detected
CC in intestinal vascular smooth muscle cells.
CC {ECO:0000269|PubMed:26647307}.
CC -!- PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC repolymerization. {ECO:0000250|UniProtKB:P63268}.
CC -!- PTM: Monomethylation at Lys-85 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P68133}.
CC -!- PTM: Methylated at His-74 by SETD3. {ECO:0000269|PubMed:30626964,
CC ECO:0000269|PubMed:31993215}.
CC -!- PTM: (Microbial infection) Monomeric actin is cross-linked by
CC V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins
CC mediate the cross-link between Lys-51 of one monomer and Glu-271 of
CC another actin monomer, resulting in formation of highly toxic actin
CC oligomers that cause cell rounding (PubMed:19015515). The toxin can be
CC highly efficient at very low concentrations by acting on formin
CC homology family proteins: toxic actin oligomers bind with high affinity
CC to formins and adversely affect both nucleation and elongation
CC abilities of formins, causing their potent inhibition in both profilin-
CC dependent and independent manners (PubMed:26228148).
CC {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}.
CC -!- DISEASE: Visceral myopathy 1 (VSCM1) [MIM:155310]: An autosomal
CC dominant form of myopathic pseudo-obstruction characterized by impaired
CC function of enteric smooth muscle cells, resulting in abnormal
CC intestinal motility, severe abdominal pain, malnutrition, and even
CC death. The disease shows inter- and intrafamilial variability. Most
CC severely affected patients exhibit prenatal bladder enlargement,
CC intestinal malrotation, neonatal functional gastrointestinal
CC obstruction, and dependence on total parenteral nutrition and urinary
CC catheterization. {ECO:0000269|PubMed:22960657,
CC ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:24777424,
CC ECO:0000269|PubMed:26647307, ECO:0000269|PubMed:27481187,
CC ECO:0000269|PubMed:29781137, ECO:0000269|PubMed:33294969,
CC ECO:0000269|PubMed:33880338}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome 5
CC (MMIHS5) [MIM:619431]: A form of megacystis-microcolon-intestinal
CC hypoperistalsis syndrome, a congenital visceral myopathy primarily
CC affecting females, and characterized by loss of smooth muscle
CC contraction in the bladder and intestine. Affected individuals present
CC at birth with functional obstruction of intestine, microcolon, dilation
CC of bladder, and secondary hydronephrosis. The majority of cases have a
CC fatal outcome due to malnutrition and sepsis, followed by multiorgan
CC failure. MMIHS5 is an autosomal dominant form with significant
CC inter- and intrafamilial variability. {ECO:0000269|PubMed:24337657,
CC ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:26647307,
CC ECO:0000269|PubMed:27481187, ECO:0000269|PubMed:28422808,
CC ECO:0000269|PubMed:29781137, ECO:0000269|PubMed:33294969}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X16940; CAA34814.1; -; mRNA.
DR EMBL; D00654; BAA00546.1; -; Genomic_DNA.
DR EMBL; AK304523; BAG65327.1; -; mRNA.
DR EMBL; AK312955; BAG35794.1; -; mRNA.
DR EMBL; CR536515; CAG38753.1; -; mRNA.
DR EMBL; CR541794; CAG46593.1; -; mRNA.
DR EMBL; AC073046; AAX88909.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99713.1; -; Genomic_DNA.
DR EMBL; BC012617; AAH12617.1; -; mRNA.
DR EMBL; BC094877; AAH94877.1; -; mRNA.
DR CCDS; CCDS1930.1; -. [P63267-1]
DR CCDS; CCDS56124.1; -. [P63267-2]
DR PIR; A40261; A40261.
DR RefSeq; NP_001186822.1; NM_001199893.1. [P63267-2]
DR RefSeq; NP_001606.1; NM_001615.3. [P63267-1]
DR PDB; 6JAT; X-ray; 2.71 A; B/D=61-82.
DR PDBsum; 6JAT; -.
DR AlphaFoldDB; P63267; -.
DR SMR; P63267; -.
DR BioGRID; 106587; 25.
DR CORUM; P63267; -.
DR IntAct; P63267; 18.
DR MINT; P63267; -.
DR STRING; 9606.ENSP00000386857; -.
DR GlyGen; P63267; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P63267; -.
DR MetOSite; P63267; -.
DR PhosphoSitePlus; P63267; -.
DR SwissPalm; P63267; -.
DR BioMuta; ACTG2; -.
DR DMDM; 54036679; -.
DR OGP; P12718; -.
DR jPOST; P63267; -.
DR MassIVE; P63267; -.
DR MaxQB; P63267; -.
DR PaxDb; P63267; -.
DR PeptideAtlas; P63267; -.
DR PRIDE; P63267; -.
DR ProteomicsDB; 20231; -.
DR ProteomicsDB; 57515; -. [P63267-1]
DR Antibodypedia; 3526; 312 antibodies from 32 providers.
DR DNASU; 72; -.
DR Ensembl; ENST00000345517.8; ENSP00000295137.3; ENSG00000163017.14. [P63267-1]
DR Ensembl; ENST00000409624.1; ENSP00000386857.1; ENSG00000163017.14. [P63267-1]
DR Ensembl; ENST00000409731.7; ENSP00000386929.3; ENSG00000163017.14. [P63267-2]
DR GeneID; 72; -.
DR KEGG; hsa:72; -.
DR MANE-Select; ENST00000345517.8; ENSP00000295137.3; NM_001615.4; NP_001606.1.
DR UCSC; uc002sjw.4; human. [P63267-1]
DR CTD; 72; -.
DR DisGeNET; 72; -.
DR GeneCards; ACTG2; -.
DR GeneReviews; ACTG2; -.
DR HGNC; HGNC:145; ACTG2.
DR HPA; ENSG00000163017; Tissue enhanced (intestine, seminal vesicle, smooth muscle).
DR MalaCards; ACTG2; -.
DR MIM; 102545; gene.
DR MIM; 155310; phenotype.
DR MIM; 619431; phenotype.
DR neXtProt; NX_P63267; -.
DR OpenTargets; ENSG00000163017; -.
DR Orphanet; 2604; Familial visceral myopathy.
DR Orphanet; 2241; Megacystis-microcolon-intestinal hypoperistalsis syndrome.
DR Orphanet; 104077; Myopathic intestinal pseudoobstruction.
DR PharmGKB; PA24469; -.
DR VEuPathDB; HostDB:ENSG00000163017; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000154148; -.
DR HOGENOM; CLU_027965_5_3_1; -.
DR InParanoid; P63267; -.
DR OMA; THKEEYI; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P63267; -.
DR TreeFam; TF354237; -.
DR PathwayCommons; P63267; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; P63267; -.
DR SIGNOR; P63267; -.
DR BioGRID-ORCS; 72; 29 hits in 1071 CRISPR screens.
DR ChiTaRS; ACTG2; human.
DR GeneWiki; ACTG2; -.
DR GenomeRNAi; 72; -.
DR Pharos; P63267; Tbio.
DR PRO; PR:P63267; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P63267; protein.
DR Bgee; ENSG00000163017; Expressed in seminal vesicle and 171 other tissues.
DR ExpressionAtlas; P63267; baseline and differential.
DR Genevisible; P63267; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0071944; C:cell periphery; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0032982; C:myosin filament; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Cytoskeleton; Disease variant; Isopeptide bond; Methylation;
KW Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..376
FT /note="Actin, gamma-enteric smooth muscle, intermediate
FT form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442949"
FT CHAIN 3..376
FT /note="Actin, gamma-enteric smooth muscle"
FT /id="PRO_0000442950"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylglutamate; in Actin, gamma-enteric smooth
FT muscle"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 45
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63268"
FT MOD_RES 48
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63268"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:30626964,
FT ECO:0000269|PubMed:31993215"
FT CROSSLNK 51
FT /note="Isoglutamyl lysine isopeptide (Lys-Glu) (interchain
FT with E-271); by Vibrio toxins RtxA and VgrG1"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT CROSSLNK 271
FT /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT with K-51); by Vibrio toxins RtxA and VgrG1"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT VAR_SEQ 43..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045861"
FT VARIANT 40
FT /note="R -> C (in MMIHS5; interferes with proper
FT polymerization into thin filaments; dbSNP:rs587777385)"
FT /evidence="ECO:0000269|PubMed:24676022,
FT ECO:0000269|PubMed:26647307, ECO:0000269|PubMed:29781137"
FT /id="VAR_071279"
FT VARIANT 40
FT /note="R -> H (in VSCM1 and MMIHS5; dbSNP:rs587777386)"
FT /evidence="ECO:0000269|PubMed:24676022,
FT ECO:0000269|PubMed:28422808, ECO:0000269|PubMed:29781137,
FT ECO:0000269|PubMed:33294969"
FT /id="VAR_071280"
FT VARIANT 41
FT /note="H -> Q (in VSCM1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33294969"
FT /id="VAR_085866"
FT VARIANT 45
FT /note="M -> T (in VSCM1; dbSNP:rs864309490)"
FT /evidence="ECO:0000269|PubMed:24676022"
FT /id="VAR_071281"
FT VARIANT 63
FT /note="R -> G (in VSCM1; dbSNP:rs864309491)"
FT /evidence="ECO:0000269|PubMed:24676022"
FT /id="VAR_071282"
FT VARIANT 63
FT /note="R -> Q (in MMIHS5; interferes with proper
FT polymerization into thin filaments)"
FT /evidence="ECO:0000269|PubMed:26647307"
FT /id="VAR_085867"
FT VARIANT 110
FT /note="P -> L (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:24676022"
FT /id="VAR_071283"
FT VARIANT 134
FT /note="Y -> N (in MMIHS5; dbSNP:rs587777388)"
FT /evidence="ECO:0000269|PubMed:24676022"
FT /id="VAR_071284"
FT VARIANT 143
FT /note="L -> F (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:33294969"
FT /id="VAR_085868"
FT VARIANT 148
FT /note="R -> L (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:29781137"
FT /id="VAR_085869"
FT VARIANT 148
FT /note="R -> S (in VSCM1; interferes with proper
FT polymerization into thin filaments; dbSNP:rs587777383)"
FT /evidence="ECO:0000269|PubMed:22960657,
FT ECO:0000269|PubMed:24777424, ECO:0000269|PubMed:26647307"
FT /id="VAR_071285"
FT VARIANT 149
FT /note="T -> R (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:33294969"
FT /id="VAR_085870"
FT VARIANT 178
FT /note="R -> C (in MMIHS5; interferes with proper
FT polymerization into thin filaments leading to impaired
FT contractility of the smooth muscle; dbSNP:rs78001248)"
FT /evidence="ECO:0000269|PubMed:24337657,
FT ECO:0000269|PubMed:24676022, ECO:0000269|PubMed:26647307,
FT ECO:0000269|PubMed:27481187"
FT /id="VAR_071286"
FT VARIANT 178
FT /note="R -> H (in MMIHS5; interferes with proper
FT polymerization into thin filaments; dbSNP:rs587777384)"
FT /evidence="ECO:0000269|PubMed:24676022,
FT ECO:0000269|PubMed:26647307"
FT /id="VAR_071287"
FT VARIANT 178
FT /note="R -> L (in MMIHS5; interferes with proper
FT polymerization into thin filaments leading to impaired
FT contractility of the smooth muscle; dbSNP:rs587777384)"
FT /evidence="ECO:0000269|PubMed:24337657,
FT ECO:0000269|PubMed:26647307, ECO:0000269|PubMed:27481187"
FT /id="VAR_071288"
FT VARIANT 195
FT /note="T -> I (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:27481187"
FT /id="VAR_085871"
FT VARIANT 196
FT /note="E -> D (in VSCM1)"
FT /evidence="ECO:0000269|PubMed:33294969,
FT ECO:0000269|PubMed:33880338"
FT /id="VAR_085872"
FT VARIANT 198
FT /note="G -> D (in VSCM1; dbSNP:rs864309492)"
FT /evidence="ECO:0000269|PubMed:24676022"
FT /id="VAR_071289"
FT VARIANT 257
FT /note="R -> C (in MMIHS5 and VSCM1; dbSNP:rs587777387)"
FT /evidence="ECO:0000269|PubMed:24676022,
FT ECO:0000269|PubMed:28422808, ECO:0000269|PubMed:29781137,
FT ECO:0000269|PubMed:33294969"
FT /id="VAR_071290"
FT VARIANT 257
FT /note="R -> H (in MMIHS5)"
FT /evidence="ECO:0000269|PubMed:27481187"
FT /id="VAR_085873"
FT VARIANT 336
FT /note="R -> W (found in a severe infantile gastrointestinal
FT motility disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:33294969"
FT /id="VAR_085874"
FT MUTAGEN 72
FT /note="I->A,D,K: Abolished methylation by SETD3."
FT /evidence="ECO:0000269|PubMed:31993215"
FT MUTAGEN 72
FT /note="I->L,M: Slightly decreased methylation by SETD3."
FT /evidence="ECO:0000269|PubMed:31993215"
FT CONFLICT 130
FT /note="V -> F (in Ref. 4; CAG38753)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="G -> C (in Ref. 3; BAG65327)"
FT /evidence="ECO:0000305"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6JAT"
SQ 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
