ACTG_HUMAN
ID ACTG_HUMAN Reviewed; 375 AA.
AC P63261; A8K7C2; P02571; P14104; P99022; Q5U032; Q96E67;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Actin, cytoplasmic 2;
DE AltName: Full=Gamma-actin;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN Name=ACTG1; Synonyms=ACTG;
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].
RX PubMed=3737401; DOI=10.1093/nar/14.13.5275;
RA Erba H.P., Gunning P., Kedes L.;
RT "Nucleotide sequence of the human gamma cytoskeletal actin mRNA: anomalous
RT evolution of vertebrate non-muscle actin genes.";
RL Nucleic Acids Res. 14:5275-5294(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2837653; DOI=10.1128/mcb.8.4.1775-1789.1988;
RA Erba H.P., Eddy R., Shows T., Kedes L., Gunning P.;
RT "Structure, chromosome location, and expression of the human gamma-actin
RT gene: differential evolution, location, and expression of the cytoskeletal
RT beta- and gamma-actin genes.";
RL Mol. Cell. Biol. 8:1775-1789(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, Eye, Lung, Ovary, Placenta, Skin, and Uterus;
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 [6]
RP PROTEIN SEQUENCE OF 2-28.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-113; 148-177; 184-191; 197-206;
RP 239-254; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT GLU-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-116; 119-210; 216-254 AND 291-372, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.,
RA Dozynkiewicz M., Norman J.C.;
RL Submitted (JUN-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 29-39; 85-113; 239-254 AND 292-312, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
RX PubMed=3472224; DOI=10.1073/pnas.84.9.2575;
RA Chou C.C., Davis R.C., Fuller M.L., Slovin J.P., Wong A., Wright J.,
RA Kania S., Shaked R., Gatti R.A., Salser W.A.;
RT "Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and amino
RT acid substitutions that may be cancer related.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2575-2579(1987).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP METHYLATION AT LYS-84, AND DEMETHYLATION BY ALKBH4.
RX PubMed=23673617; DOI=10.1038/ncomms2863;
RA Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y.,
RA Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C.,
RA Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
RT "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.";
RL Nat. Commun. 4:1832-1832(2013).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
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 [19]
RP ACETYLATION AT GLU-2.
RX PubMed=30028079; DOI=10.1111/febs.14605;
RA Wiame E., Tahay G., Tyteca D., Vertommen D., Stroobant V., Bommer G.T.,
RA Van Schaftingen E.;
RT "NAT6 acetylates the N-terminus of different forms of actin.";
RL FEBS J. 285:3299-3316(2018).
RN [20]
RP FUNCTION, AND ACETYLATION AT GLU-2.
RX PubMed=29581253; DOI=10.1073/pnas.1718336115;
RA Drazic A., Aksnes H., Marie M., Boczkowska M., Varland S., Timmerman E.,
RA Foyn H., Glomnes N., Rebowski G., Impens F., Gevaert K., Dominguez R.,
RA Arnesen T.;
RT "NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton
RT assembly and cell motility.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:4399-4404(2018).
RN [21]
RP METHYLATION AT HIS-73.
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 [22]
RP VARIANTS DFNA20 ILE-89; MET-118; LEU-264 AND ALA-332.
RX PubMed=13680526; DOI=10.1086/379286;
RA Zhu M., Yang T., Wei S., DeWan A.T., Morell R.J., Elfenbein J.L.,
RA Fisher R.A., Leal S.M., Smith R.J.H., Friderici K.H.;
RT "Mutations in the gamma-actin gene (ACTG1) are associated with dominant
RT progressive deafness (DFNA20/26).";
RL Am. J. Hum. Genet. 73:1082-1091(2003).
RN [23]
RP VARIANT DFNA20 ILE-278.
RX PubMed=14684684; DOI=10.1136/jmg.40.12.879;
RA van Wijk E., Krieger E., Kemperman M.H., De Leenheer E.M.R., Huygen P.L.M.,
RA Cremers C.W.R.J., Cremers F.P.M., Kremer H.;
RT "A mutation in the gamma actin 1 (ACTG1) gene causes autosomal dominant
RT hearing loss (DFNA20/26).";
RL J. Med. Genet. 40:879-884(2003).
RN [24]
RP VARIANT DFNA20 ALA-370.
RX PubMed=16773128; DOI=10.1038/sj.ejhg.5201670;
RA Rendtorff N.D., Zhu M., Fagerheim T., Antal T.L., Jones M., Teslovich T.M.,
RA Gillanders E.M., Barmada M., Teig E., Trent J.M., Friderici K.H.,
RA Stephan D.A., Tranebjaerg L.;
RT "A novel missense mutation in ACTG1 causes dominant deafness in a Norwegian
RT DFNA20/26 family, but ACTG1 mutations are not frequent among families with
RT hereditary hearing impairment.";
RL Eur. J. Hum. Genet. 14:1097-1105(2006).
RN [25]
RP VARIANT DFNA20 VAL-122.
RX PubMed=18804074; DOI=10.1016/s1673-8527(08)60075-2;
RA Liu P., Li H., Ren X., Mao H., Zhu Q., Zhu Z., Yang R., Yuan W., Liu J.,
RA Wang Q., Liu M.;
RT "Novel ACTG1 mutation causing autosomal dominant non-syndromic hearing
RT impairment in a Chinese family.";
RL J. Genet. Genomics 35:553-558(2008).
RN [26]
RP VARIANTS DFNA20 ASN-118 AND LYS-241.
RX PubMed=19477959; DOI=10.1093/hmg/ddp249;
RA Morin M., Bryan K.E., Mayo-Merino F., Goodyear R., Mencia A.,
RA Modamio-Hoybjor S., del Castillo I., Cabalka J.M., Richardson G.,
RA Moreno F., Rubenstein P.A., Moreno-Pelayo M.A.;
RT "In vivo and in vitro effects of two novel gamma-actin (ACTG1) mutations
RT that cause DFNA20/26 hearing impairment.";
RL Hum. Mol. Genet. 18:3075-3089(2009).
RN [27]
RP VARIANTS BRWS2 ILE-120; VAL-135; PHE-155; LYS-203; TRP-254 AND TRP-256.
RX PubMed=22366783; DOI=10.1038/ng.1091;
RA Riviere J.B., van Bon B.W., Hoischen A., Kholmanskikh S.S., O'Roak B.J.,
RA Gilissen C., Gijsen S., Sullivan C.T., Christian S.L., Abdul-Rahman O.A.,
RA Atkin J.F., Chassaing N., Drouin-Garraud V., Fry A.E., Fryns J.P.,
RA Gripp K.W., Kempers M., Kleefstra T., Mancini G.M., Nowaczyk M.J.,
RA van Ravenswaaij-Arts C.M., Roscioli T., Marble M., Rosenfeld J.A.,
RA Siu V.M., de Vries B.B., Shendure J., Verloes A., Veltman J.A.,
RA Brunner H.G., Ross M.E., Pilz D.T., Dobyns W.B.;
RT "De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter
RT syndrome.";
RL Nat. Genet. 44:440-444(2012).
RN [28]
RP VARIANT DFNA20 HIS-187.
RX PubMed=22938506; DOI=10.1186/1750-1172-7-60;
RA Baek J.I., Oh S.K., Kim D.B., Choi S.Y., Kim U.K., Lee K.Y., Lee S.H.;
RT "Targeted massive parallel sequencing: the effective detection of novel
RT causative mutations associated with hearing loss in small families.";
RL Orphanet J. Rare Dis. 7:60-60(2012).
RN [29]
RP VARIANT DFNA20 LYS-316.
RX PubMed=25388789; DOI=10.1186/s12967-014-0311-1;
RA Wei Q., Zhu H., Qian X., Chen Z., Yao J., Lu Y., Cao X., Xing G.;
RT "Targeted genomic capture and massively parallel sequencing to identify
RT novel variants causing Chinese hereditary hearing loss.";
RL J. Transl. Med. 12:311-311(2014).
RN [30]
RP VARIANT LEU-70, CHARACTERIZATION OF VARIANT LEU-70, INTERACTION WITH CAPZB;
RP TWF1; COFILIN AND PROFILIN, AND SUBCELLULAR LOCATION.
RX PubMed=28493397; DOI=10.1002/humu.23246;
RG UK10K;
RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
RA FitzPatrick D.R.;
RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma.";
RL Hum. Mutat. 38:942-946(2017).
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. {ECO:0000305|PubMed:29581253}.
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. Interacts with TWF1, CAPZB, cofilin and
CC profilin (PubMed:28493397). {ECO:0000269|PubMed:28493397}.
CC -!- INTERACTION:
CC P63261; P60709: ACTB; NbExp=16; IntAct=EBI-351292, EBI-353944;
CC P63261; P63261: ACTG1; NbExp=8; IntAct=EBI-351292, EBI-351292;
CC P63261; P40123: CAP2; NbExp=12; IntAct=EBI-351292, EBI-1051165;
CC P63261; O60826: CCDC22; NbExp=3; IntAct=EBI-351292, EBI-3943153;
CC P63261; Q16543: CDC37; NbExp=3; IntAct=EBI-351292, EBI-295634;
CC P63261; P23528: CFL1; NbExp=9; IntAct=EBI-351292, EBI-352733;
CC P63261; Q549N0: CFL2; NbExp=5; IntAct=EBI-351292, EBI-10201319;
CC P63261; Q9Y281: CFL2; NbExp=9; IntAct=EBI-351292, EBI-351218;
CC P63261; P60981: DSTN; NbExp=8; IntAct=EBI-351292, EBI-745191;
CC P63261; Q08426: EHHADH; NbExp=4; IntAct=EBI-351292, EBI-2339219;
CC P63261; P42858: HTT; NbExp=16; IntAct=EBI-351292, EBI-466029;
CC P63261; P40692: MLH1; NbExp=7; IntAct=EBI-351292, EBI-744248;
CC P63261; Q96HA8: NTAQ1; NbExp=7; IntAct=EBI-351292, EBI-741158;
CC P63261; Q1KLZ0: PS1TP5BP1; NbExp=3; IntAct=EBI-351292, EBI-9978131;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:28493397}.
CC -!- PTM: Oxidation of Met-44 and Met-47 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 promote actin
CC repolymerization. {ECO:0000250|UniProtKB:P63260}.
CC -!- PTM: Monomethylation at Lys-84 (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:0000269|PubMed:23673617}.
CC -!- PTM: [Actin, cytoplasmic 2, N-terminally processed]: N-terminal
CC acetylation by NAA80 affects actin filament depolymerization and
CC elongation, including elongation driven by formins (PubMed:29581253).
CC In contrast, filament nucleation by the Arp2/3 complex is not affected
CC (PubMed:29581253). {ECO:0000269|PubMed:29581253}.
CC -!- PTM: Methylated at His-73 by SETD3. {ECO:0000269|PubMed:30626964}.
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-50 of one monomer and Glu-270 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: Deafness, autosomal dominant, 20 (DFNA20) [MIM:604717]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:13680526, ECO:0000269|PubMed:14684684,
CC ECO:0000269|PubMed:16773128, ECO:0000269|PubMed:18804074,
CC ECO:0000269|PubMed:19477959, ECO:0000269|PubMed:22938506,
CC ECO:0000269|PubMed:25388789}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Baraitser-Winter syndrome 2 (BRWS2) [MIM:614583]: A rare
CC developmental disorder characterized by the combination of congenital
CC ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a
CC brain malformation consisting of anterior-predominant lissencephaly.
CC Other typical features include postnatal short stature and
CC microcephaly, intellectual disability, seizures, and hearing loss.
CC {ECO:0000269|PubMed:22366783}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in ACTG1 has been found in a patient with
CC isolated coloboma, a defect of the eye characterized by the absence of
CC ocular structures due to abnormal morphogenesis of the optic cup and
CC stalk, and the fusion of the fetal fissure (optic fissure). Isolated
CC colobomas may be associated with an abnormally small eye
CC (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}.
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}.
CC -!- WEB RESOURCE: Name=Mendelian genes actin, gamma 1 (ACTG1); Note=Leiden
CC Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/ACTG1";
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DR EMBL; X04098; CAA27723.1; -; mRNA.
DR EMBL; M19283; AAA51579.1; -; Genomic_DNA.
DR EMBL; AK291937; BAF84626.1; -; mRNA.
DR EMBL; BT019856; AAV38659.1; -; mRNA.
DR EMBL; BC000292; AAH00292.1; -; mRNA.
DR EMBL; BC001920; AAH01920.1; -; mRNA.
DR EMBL; BC007442; AAH07442.1; -; mRNA.
DR EMBL; BC009848; AAH09848.1; -; mRNA.
DR EMBL; BC010999; AAH10999.1; -; mRNA.
DR EMBL; BC012050; AAH12050.1; -; mRNA.
DR EMBL; BC015005; AAH15005.1; -; mRNA.
DR EMBL; BC015695; AAH15695.1; -; mRNA.
DR EMBL; BC015779; AAH15779.1; -; mRNA.
DR EMBL; BC018774; AAH18774.1; -; mRNA.
DR EMBL; BC053572; AAH53572.1; -; mRNA.
DR EMBL; M16247; AAA51580.1; -; mRNA.
DR CCDS; CCDS11782.1; -.
DR PIR; A28098; ATHUG.
DR PIR; JC5818; JC5818.
DR RefSeq; NP_001186883.1; NM_001199954.1.
DR RefSeq; NP_001605.1; NM_001614.3.
DR PDB; 5JLH; EM; 3.90 A; A/B/C/D/E=2-375.
DR PDB; 6CXI; EM; 11.00 A; A/B/C/D/E=1-375.
DR PDB; 6CXJ; EM; 11.00 A; A/B/C/D/E=1-375.
DR PDB; 6G2T; EM; 9.00 A; A/B/C/D/E/F=1-375.
DR PDB; 6V62; X-ray; 2.36 A; Y=66-88.
DR PDB; 6V63; X-ray; 2.02 A; Y/Z=66-88.
DR PDB; 6WK1; X-ray; 1.89 A; Y/Z=66-88.
DR PDB; 6WK2; X-ray; 1.76 A; C/Y=66-88.
DR PDB; 7NVM; EM; 3.10 A; K=1-375.
DR PDBsum; 5JLH; -.
DR PDBsum; 6CXI; -.
DR PDBsum; 6CXJ; -.
DR PDBsum; 6G2T; -.
DR PDBsum; 6V62; -.
DR PDBsum; 6V63; -.
DR PDBsum; 6WK1; -.
DR PDBsum; 6WK2; -.
DR PDBsum; 7NVM; -.
DR AlphaFoldDB; P63261; -.
DR SMR; P63261; -.
DR BioGRID; 106586; 248.
DR CORUM; P63261; -.
DR IntAct; P63261; 108.
DR MINT; P63261; -.
DR STRING; 9606.ENSP00000458162; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR GlyGen; P63261; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P63261; -.
DR MetOSite; P63261; -.
DR PhosphoSitePlus; P63261; -.
DR SwissPalm; P63261; -.
DR BioMuta; ACTG1; -.
DR DMDM; 54036678; -.
DR DOSAC-COBS-2DPAGE; P63261; -.
DR OGP; P63261; -.
DR REPRODUCTION-2DPAGE; P63261; -.
DR SWISS-2DPAGE; P63261; -.
DR EPD; P63261; -.
DR jPOST; P63261; -.
DR MassIVE; P63261; -.
DR MaxQB; P63261; -.
DR PaxDb; P63261; -.
DR PeptideAtlas; P63261; -.
DR PRIDE; P63261; -.
DR ProteomicsDB; 57514; -.
DR TopDownProteomics; P63261; -.
DR Antibodypedia; 32827; 383 antibodies from 34 providers.
DR DNASU; 71; -.
DR Ensembl; ENST00000570382.2; ENSP00000466346.2; ENSG00000184009.13.
DR Ensembl; ENST00000571721.6; ENSP00000460660.2; ENSG00000184009.13.
DR Ensembl; ENST00000573283.7; ENSP00000458435.1; ENSG00000184009.13.
DR Ensembl; ENST00000575087.5; ENSP00000459124.1; ENSG00000184009.13.
DR Ensembl; ENST00000575659.6; ENSP00000459119.2; ENSG00000184009.13.
DR Ensembl; ENST00000575842.5; ENSP00000458162.1; ENSG00000184009.13.
DR Ensembl; ENST00000575994.6; ENSP00000460464.2; ENSG00000184009.13.
DR Ensembl; ENST00000576544.6; ENSP00000461672.1; ENSG00000184009.13.
DR Ensembl; ENST00000615544.5; ENSP00000477968.1; ENSG00000184009.13.
DR Ensembl; ENST00000679480.1; ENSP00000506201.1; ENSG00000184009.13.
DR Ensembl; ENST00000679778.1; ENSP00000505235.1; ENSG00000184009.13.
DR Ensembl; ENST00000680227.1; ENSP00000506253.1; ENSG00000184009.13.
DR Ensembl; ENST00000680727.1; ENSP00000505193.1; ENSG00000184009.13.
DR Ensembl; ENST00000681052.1; ENSP00000505060.1; ENSG00000184009.13.
DR Ensembl; ENST00000681842.1; ENSP00000506126.1; ENSG00000184009.13.
DR GeneID; 71; -.
DR KEGG; hsa:71; -.
DR MANE-Select; ENST00000573283.7; ENSP00000458435.1; NM_001614.5; NP_001605.1.
DR UCSC; uc002kak.3; human.
DR CTD; 71; -.
DR DisGeNET; 71; -.
DR GeneCards; ACTG1; -.
DR GeneReviews; ACTG1; -.
DR HGNC; HGNC:144; ACTG1.
DR HPA; ENSG00000184009; Low tissue specificity.
DR MalaCards; ACTG1; -.
DR MIM; 102560; gene.
DR MIM; 604717; phenotype.
DR MIM; 614583; phenotype.
DR neXtProt; NX_P63261; -.
DR OpenTargets; ENSG00000184009; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 2995; Baraitser-Winter cerebrofrontofacial syndrome.
DR Orphanet; 98942; Coloboma of choroid and retina.
DR Orphanet; 98944; Coloboma of iris.
DR PharmGKB; PA24468; -.
DR VEuPathDB; HostDB:ENSG00000184009; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P63261; -.
DR OMA; KCDESIC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P63261; -.
DR TreeFam; TF354237; -.
DR PathwayCommons; P63261; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-190873; Gap junction degradation.
DR Reactome; R-HSA-196025; Formation of annular gap junctions.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; P63261; -.
DR SIGNOR; P63261; -.
DR BioGRID-ORCS; 71; 337 hits in 1076 CRISPR screens.
DR ChiTaRS; ACTG1; human.
DR GeneWiki; ACTG1; -.
DR GenomeRNAi; 71; -.
DR Pharos; P63261; Tbio.
DR PRO; PR:P63261; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P63261; protein.
DR Bgee; ENSG00000184009; Expressed in ileal mucosa and 205 other tissues.
DR ExpressionAtlas; P63261; baseline and differential.
DR Genevisible; P63261; HS.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; IDA:ARUK-UCL.
DR GO; GO:0120220; C:basal body patch; IEA:Ensembl.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0099143; C:presynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IC:UniProtKB.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IMP:ARUK-UCL.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:ARUK-UCL.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:ARUK-UCL.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; IMP:ARUK-UCL.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:ARUK-UCL.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IMP:ARUK-UCL.
DR GO; GO:0150111; P:regulation of transepithelial transport; IMP:ARUK-UCL.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:0120192; P:tight junction assembly; IMP:ARUK-UCL.
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; ATP-binding; Cytoplasm; Cytoskeleton; Deafness;
KW Direct protein sequencing; Disease variant; Intellectual disability;
KW Isopeptide bond; Methylation; Non-syndromic deafness; Nucleotide-binding;
KW Oxidation; Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000367100"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 2, N-terminally processed"
FT /evidence="ECO:0000305|PubMed:29581253"
FT /id="PRO_0000000831"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylglutamate; in Actin, cytoplasmic 2, N-
FT terminally processed; partial"
FT /evidence="ECO:0000269|PubMed:29581253,
FT ECO:0000269|PubMed:30028079, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:30626964, ECO:0000269|Ref.8"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:23673617"
FT CROSSLNK 50
FT /note="(Microbial infection) Isoglutamyl lysine isopeptide
FT (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA
FT and VgrG1"
FT /evidence="ECO:0000305|PubMed:19015515"
FT CROSSLNK 270
FT /note="(Microbial infection) Isoglutamyl lysine isopeptide
FT (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and
FT VgrG1"
FT /evidence="ECO:0000305|PubMed:19015515"
FT VARIANT 70
FT /note="P -> L (found in a patient with isolated coloboma;
FT decreased incorporation into F-actin; decreased interaction
FT with cofilin; loss of interaction with TWF1, CAPZB and
FT profilin)"
FT /evidence="ECO:0000269|PubMed:28493397"
FT /id="VAR_079849"
FT VARIANT 89
FT /note="T -> I (in DFNA20; dbSNP:rs28999111)"
FT /evidence="ECO:0000269|PubMed:13680526"
FT /id="VAR_032434"
FT VARIANT 118
FT /note="K -> M (in DFNA20; dbSNP:rs104894544)"
FT /evidence="ECO:0000269|PubMed:13680526"
FT /id="VAR_032435"
FT VARIANT 118
FT /note="K -> N (in DFNA20; dbSNP:rs267606630)"
FT /evidence="ECO:0000269|PubMed:19477959"
FT /id="VAR_067824"
FT VARIANT 120
FT /note="T -> I (in BRWS2; dbSNP:rs281875325)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067814"
FT VARIANT 122
FT /note="I -> V (in DFNA20; dbSNP:rs281875330)"
FT /evidence="ECO:0000269|PubMed:18804074"
FT /id="VAR_067825"
FT VARIANT 135
FT /note="A -> V (in BRWS2; dbSNP:rs11549190)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067815"
FT VARIANT 155
FT /note="S -> F (in BRWS2; dbSNP:rs281875326)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067816"
FT VARIANT 160
FT /note="T -> I (in dbSNP:rs11549206)"
FT /id="VAR_048186"
FT VARIANT 187
FT /note="D -> H (in DFNA20)"
FT /evidence="ECO:0000269|PubMed:22938506"
FT /id="VAR_079878"
FT VARIANT 203
FT /note="T -> K (in BRWS2; dbSNP:rs281875327)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067817"
FT VARIANT 241
FT /note="E -> K (in DFNA20; dbSNP:rs267606631)"
FT /evidence="ECO:0000269|PubMed:19477959"
FT /id="VAR_067826"
FT VARIANT 254
FT /note="R -> W (in BRWS2; dbSNP:rs281875328)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067818"
FT VARIANT 256
FT /note="R -> W (in BRWS2; dbSNP:rs281875329)"
FT /evidence="ECO:0000269|PubMed:22366783"
FT /id="VAR_067819"
FT VARIANT 264
FT /note="P -> L (in DFNA20; dbSNP:rs104894546)"
FT /evidence="ECO:0000269|PubMed:13680526"
FT /id="VAR_032436"
FT VARIANT 278
FT /note="T -> I (in DFNA20; dbSNP:rs28999112)"
FT /evidence="ECO:0000269|PubMed:14684684"
FT /id="VAR_032437"
FT VARIANT 316
FT /note="E -> K (in DFNA20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25388789"
FT /id="VAR_079879"
FT VARIANT 332
FT /note="P -> A (in DFNA20; dbSNP:rs104894545)"
FT /evidence="ECO:0000269|PubMed:13680526"
FT /id="VAR_032438"
FT VARIANT 370
FT /note="V -> A (in DFNA20; dbSNP:rs104894547)"
FT /evidence="ECO:0000269|PubMed:16773128"
FT /id="VAR_032439"
FT CONFLICT 316
FT /note="E -> K (in Ref. 10; AAA51580)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> F (in Ref. 10; AAA51580)"
FT /evidence="ECO:0000305"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6WK2"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6WK2"
SQ SEQUENCE 375 AA; 41793 MW; 54D08F986964EFD5 CRC64;
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
