ID ACTC_MOUSE Reviewed; 377 AA. AC P68033; P04270; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 02-SEP-2026, entry version 161. DE RecName: Full=Actin, alpha cardiac muscle 1; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE AltName: Full=Alpha-cardiac actin; DE Contains: DE RecName: Full=Actin, alpha cardiac muscle 1, intermediate form; DE Flags: Precursor; GN Name=Actc1; Synonyms=Actc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-377. RX PubMed=3028523; DOI=10.1007/bf01116542; RA Leader D.P., Gall I., Campbell P.C.; RT "The structure of a cDNA clone corresponding to mouse cardiac muscle actin RT mRNA."; RL Biosci. Rep. 6:741-747(1986). RN [4] RP PROTEIN SEQUENCE OF 71-97 AND 241-256, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP OXIDATION AT MET-46 AND MET-49, AND DEOXIDATION AT MET-46 AND MET-49. RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019; RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., RA Gladyshev V.N.; RT "MsrB1 and MICALs regulate actin assembly and macrophage function via RT reversible stereoselective methionine oxidation."; RL Mol. Cell 51:397-404(2013). RN [6] RP PROTEOLYTIC CLEAVAGE BY ACTMAP, AND ACETYLATION AT CYS-2. RX PubMed=36173861; DOI=10.1126/science.abq5082; RA Haahr P., Galli R.A., van den Hengel L.G., Bleijerveld O.B., RA Kazokaite-Adomaitiene J., Song J.Y., Kroese L.J., Krimpenfort P., RA Baltissen M.P., Vermeulen M., Ottenheijm C.A.C., Brummelkamp T.R.; RT "Actin maturation requires the ACTMAP/C19orf54 protease."; RL Science 377:1533-1537(2022). 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 -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P68137}; 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 -!- INTERACTION: CC P68033; O70468: Mybpc3; NbExp=3; IntAct=EBI-352284, EBI-8347074; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- PTM: Oxidation of Met-46 and Met-49 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:0000269|PubMed:23911929}. CC -!- PTM: Monomethylation at Lys-86 (K86me1) 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:P68032}. CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68032}. CC -!- PTM: [Actin, alpha cardiac muscle 1, intermediate form]: N-terminal CC cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. CC {ECO:0000269|PubMed:36173861}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK014303; BAB29258.1; -; mRNA. DR EMBL; BC062138; AAH62138.1; -; mRNA. DR EMBL; M15501; AAA37167.1; -; mRNA. DR CCDS; CCDS16564.1; -. DR PIR; A54728; A54728. DR RefSeq; NP_033738.1; NM_009608.4. DR PDB; 8Q4G; EM; 8.00 A; A/B/C/D/E/F/I=6-377. DR PDB; 8ZBK; EM; 4.28 A; B/D/I/J/K/M=7-376. DR PDB; 8ZBN; EM; 3.02 A; B/D/I/J/K/M=7-376. DR PDB; 8ZIP; EM; 4.90 A; J=7-376. DR PDB; 8ZIU; EM; 3.54 A; J=7-376. DR PDB; 9E2E; EM; 4.00 A; A/B/C/D/E/F=1-377. DR PDB; 9MO4; EM; 5.30 A; A/B/C/D/E/F=1-377. DR PDB; 9MO5; EM; 5.30 A; A/B/C/D/E/F=1-377. DR PDB; 9MO6; EM; 5.30 A; A/B/C/D/E/F=1-377. DR PDB; 9MO7; EM; 5.20 A; A/B/C/D/E/F=1-377. DR PDB; 9MO8; EM; 5.20 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MO9; EM; 5.60 A; A/B/C/D/E/F=1-377. DR PDB; 9MOA; EM; 5.40 A; A/B/C/D/E/F=1-377. DR PDB; 9MOB; EM; 5.50 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOC; EM; 5.60 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOD; EM; 5.70 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOI; EM; 5.40 A; A/B/C/D/E/F=1-377. DR PDB; 9MOK; EM; 5.60 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOL; EM; 5.20 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOM; EM; 5.10 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MON; EM; 5.20 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOO; EM; 5.20 A; A/B/C/D/E/F=1-377. DR PDB; 9MOP; EM; 5.00 A; A/B/C/D/E/F=1-377. DR PDB; 9MOU; EM; 5.60 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOW; EM; 4.90 A; A/B/C/D/E/F/G=1-377. DR PDB; 9MOX; EM; 5.20 A; A/B/C/D/E/F=1-377. DR AlphaFoldDB; P68033; -. DR EMDB; EMD-18147; -. DR EMDB; EMD-39904; -. DR EMDB; EMD-39906; -. DR EMDB; EMD-47449; -. DR EMDB; EMD-48447; -. DR EMDB; EMD-48448; -. DR EMDB; EMD-48449; -. DR EMDB; EMD-48450; -. DR EMDB; EMD-48451; -. DR EMDB; EMD-48452; -. DR EMDB; EMD-48453; -. DR EMDB; EMD-48454; -. DR EMDB; EMD-48455; -. DR EMDB; EMD-48456; -. DR EMDB; EMD-48467; -. DR EMDB; EMD-48468; -. DR EMDB; EMD-48469; -. DR EMDB; EMD-48470; -. DR EMDB; EMD-48471; -. DR EMDB; EMD-48476; -. DR EMDB; EMD-48477; -. DR EMDB; EMD-48482; -. DR EMDB; EMD-48483; -. DR EMDB; EMD-48484; -. DR EMDB; EMD-60125; -. DR EMDB; EMD-60130; -. DR SMR; P68033; -. DR BioGRID; 197945; 14. DR FunCoup; P68033; 290. DR IntAct; P68033; 7. DR MINT; P68033; -. DR STRING; 10090.ENSMUSP00000087736; -. DR GlyGen; P68033; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P68033; -. DR PhosphoSitePlus; P68033; -. DR SwissPalm; P68033; -. DR jPOST; P68033; -. DR PaxDb; 10090-ENSMUSP00000087736; -. DR PeptideAtlas; P68033; -. DR Pumba; P68033; -. DR Antibodypedia; 9782; 347 antibodies from 38 providers. DR DNASU; 11464; -. DR Ensembl; ENSMUST00000090269.7; ENSMUSP00000087736.7; ENSMUSG00000068614.8. DR GeneID; 11464; -. DR KEGG; mmu:11464; -. DR UCSC; uc008lpz.1; mouse. DR AGR; MGI:87905; -. DR CTD; 70; -. DR MGI; MGI:87905; Actc1. DR VEuPathDB; HostDB:ENSMUSG00000068614; -. DR eggNOG; KOG0676; Eukaryota. DR GeneTree; ENSGT00940000154710; -. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; P68033; -. DR OMA; FTTSAEF; -. DR OrthoDB; 9545632at2759; -. DR PhylomeDB; P68033; -. DR Reactome; R-MMU-390522; Striated Muscle Contraction. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9013026; RHOB GTPase cycle. DR Reactome; R-MMU-9764561; Regulation of CDH1 Function. DR Reactome; R-MMU-9913351; Formation of the dystrophin-glycoprotein complex (DGC). DR Reactome; R-MMU-9958825; Activation of STAT3 by cadherin engagement. DR BioGRID-ORCS; 11464; 4 hits in 78 CRISPR screens. DR PRO; PR:P68033; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P68033; protein. DR Bgee; ENSMUSG00000068614; Expressed in atrioventricular valve and 262 other cell types or tissues. DR ExpressionAtlas; P68033; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005884; C:actin filament; ISO:GO_Central. DR GO; GO:0044297; C:cell body; ISS:AgBase. DR GO; GO:0005737; C:cytoplasm; ISO:GO_Central. DR GO; GO:0030175; C:filopodium; ISS:AgBase. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0031674; C:I band; IDA:MGI. DR GO; GO:0030027; C:lamellipodium; ISS:AgBase. DR GO; GO:0030017; C:sarcomere; ISO:GO_Central. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0005524; F:ATP binding; ISO:GO_Central. DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB. DR GO; GO:0000146; F:microfilament motor activity; ISO:GO_Central. DR GO; GO:0017022; F:myosin binding; ISO:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0030048; P:actin filament-based movement; ISO:GO_Central. DR GO; GO:0033275; P:actin-myosin filament sliding; ISO:GO_Central. DR GO; GO:0031032; P:actomyosin structure organization; IMP:MGI. DR GO; GO:0060048; P:cardiac muscle contraction; ISO:GO_Central. DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI. DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI. DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IMP:MGI. DR GO; GO:0060047; P:heart contraction; ISO:GO_Central. DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:MGI. DR CDD; cd10224; ASKHA_NBD_actin; 1. DR FunFam; 3.30.420.40:FF:000131; Actin, alpha skeletal muscle; 1. DR FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1. DR FunFam; 3.90.640.10:FF:000047; Actin, alpha skeletal muscle; 1. DR FunFam; 3.30.420.40:FF:000058; Putative actin-related protein 5; 1. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. DR PDBsum; 8Q4G; -. DR PDBsum; 8ZBK; -. DR PDBsum; 8ZBN; -. DR PDBsum; 8ZIP; -. DR PDBsum; 8ZIU; -. DR PDBsum; 9E2E; -. DR PDBsum; 9MO4; -. DR PDBsum; 9MO5; -. DR PDBsum; 9MO6; -. DR PDBsum; 9MO7; -. DR PDBsum; 9MO8; -. DR PDBsum; 9MO9; -. DR PDBsum; 9MOA; -. DR PDBsum; 9MOB; -. DR PDBsum; 9MOC; -. DR PDBsum; 9MOD; -. DR PDBsum; 9MOI; -. DR PDBsum; 9MOK; -. DR PDBsum; 9MOL; -. DR PDBsum; 9MOM; -. DR PDBsum; 9MON; -. DR PDBsum; 9MOO; -. DR PDBsum; 9MOP; -. DR PDBsum; 9MOU; -. DR PDBsum; 9MOW; -. DR PDBsum; 9MOX; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Hydrolase; Methylation; Muscle protein; KW Nucleotide-binding; Oxidation; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..377 FT /note="Actin, alpha cardiac muscle 1, intermediate form" FT /evidence="ECO:0000250|UniProtKB:P62737" FT /id="PRO_0000442999" FT CHAIN 3..377 FT /note="Actin, alpha cardiac muscle 1" FT /evidence="ECO:0000250|UniProtKB:P68135" FT /id="PRO_0000000815" FT MOD_RES 2 FT /note="N-acetylcysteine; in intermediate form" FT /evidence="ECO:0000269|PubMed:36173861" FT MOD_RES 46 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000269|PubMed:23911929" FT MOD_RES 49 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000269|PubMed:23911929" FT MOD_RES 75 FT /note="Tele-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:P62739" FT MOD_RES 86 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P68032" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 16..23 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 59..62 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 72..78 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 81..90 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 91..96 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 105..109 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 115..128 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 132..138 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 139..147 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 150..157 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:8ZBN" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 205..218 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 225..234 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 240..245 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 247..253 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 260..263 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:8ZBN" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 304..307 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 311..322 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 340..350 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 352..356 FT /evidence="ECO:0007829|PDB:8ZBN" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 361..367 FT /evidence="ECO:0007829|PDB:8ZBN" FT HELIX 371..375 FT /evidence="ECO:0007829|PDB:8ZBN" SQ SEQUENCE 377 AA; 42019 MW; E5C10FA19730CAD2 CRC64; MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS KQEYDEAGPS IVHRKCF //