ID ACTN2_HUMAN Reviewed; 894 AA. AC P35609; B1ANE4; B2RCS5; Q86TF4; Q86TI8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 27-MAR-2024, entry version 240. DE RecName: Full=Alpha-actinin-2; DE AltName: Full=Alpha-actinin skeletal muscle isoform 2; DE AltName: Full=F-actin cross-linking protein; GN Name=ACTN2; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RC TISSUE=Skeletal muscle; RX PubMed=1339456; DOI=10.1016/s0021-9258(19)50420-3; RA Beggs A.H., Byers T.J., Knoll J.H.M., Boyce F.M., Bruns G.A.P., RA Kunkel L.M.; RT "Cloning and characterization of two human skeletal muscle alpha-actinin RT genes located on chromosomes 1 and 11."; RL J. Biol. Chem. 267:9281-9288(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10548523; DOI=10.1006/bbrc.1999.1661; RA Tiso N., Majetti M., Stanchi F., Rampazzo A., Zimbello R., Nava A., RA Danieli G.A.; RT "Fine mapping and genomic structure of ACTN2, the human gene coding for the RT sarcomeric isoform of alpha-actinin-2, expressed in skeletal and cardiac RT muscle."; RL Biochem. Biophys. Res. Commun. 265:256-259(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS; 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 [7] RP INTERACTION WITH LDB3. RX PubMed=10427098; DOI=10.1083/jcb.146.2.465; RA Faulkner G., Pallavicini A., Formentin E., Comelli A., Ievolella C., RA Trevisan S., Bortoletto G., Scannapieco P., Salamon M., Mouly V., Valle G., RA Lanfranchi G.; RT "ZASP: a new Z-band alternatively spliced PDZ-motif protein."; RL J. Cell Biol. 146:465-475(1999). RN [8] RP INTERACTION WITH MYOZ1. RX PubMed=10984498; DOI=10.1074/jbc.m007493200; RA Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G., RA Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P., RA Valle G., Lanfranchi G.; RT "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc RT of skeletal muscle."; RL J. Biol. Chem. 275:41234-41242(2000). RN [9] RP INTERACTION WITH MYOZ1 AND MYOZ2. RX PubMed=11114196; DOI=10.1073/pnas.260501097; RA Frey N., Richardson J.A., Olson E.N.; RT "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000). RN [10] RP INTERACTION WITH MYOZ1, AND SUBCELLULAR LOCATION. RX PubMed=11171996; DOI=10.1073/pnas.98.4.1595; RA Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C., RA Kunkel L.M., Beggs A.H.; RT "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal RT muscle Z lines."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001). RN [11] RP INTERACTION WITH MYOZ3. RX PubMed=11842093; DOI=10.1074/jbc.m200712200; RA Frey N., Olson E.N.; RT "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin RT family, interacts with multiple Z-disc proteins."; RL J. Biol. Chem. 277:13998-14004(2002). RN [12] RP INTERACTION WITH PARVB. RX PubMed=15159419; DOI=10.1083/jcb.200308141; RA Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H., RA Takabayashi M., Fujimaki K., Fujisawa S., Ohno S., Ishigatsubo Y.; RT "Affixin interacts with alpha-actinin and mediates integrin signaling for RT reorganization of F-actin induced by initial cell-substrate interaction."; RL J. Cell Biol. 165:539-551(2004). RN [13] RP INTERACTION WITH XIRP2. RX PubMed=17046827; DOI=10.1074/jbc.m603244200; RA Huang H.-T., Brand O.M., Mathew M., Ignatiou C., Ewen E.P., McCalmon S.A., RA Naya F.J.; RT "Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin- RT related alpha-actinin-interacting protein."; RL J. Biol. Chem. 281:39370-39379(2006). RN [14] RP INTERACTION WITH SYNPO2. RX PubMed=20554076; DOI=10.1016/j.ejcb.2010.04.004; RA Linnemann A., van der Ven P.F., Vakeel P., Albinus B., Simonis D., RA Bendas G., Schenk J.A., Micheel B., Kley R.A., Fuerst D.O.; RT "The sarcomeric Z-disc component myopodin is a multiadapter protein that RT interacts with filamin and alpha-actinin."; RL Eur. J. Cell Biol. 89:681-692(2010). RN [15] RP INTERACTION WITH DST, AND SUBCELLULAR LOCATION. RX PubMed=19932097; DOI=10.1016/j.yexcr.2009.11.010; RA Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., RA Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., RA Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.; RT "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle RT and association with plectin and alpha-actinin."; RL Exp. Cell Res. 316:297-313(2010). RN [16] RP UBIQUITINATION BY FBXL22. RX PubMed=22972877; DOI=10.1161/circresaha.112.271007; RA Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M., RA Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.; RT "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box RT protein that regulates sarcomeric protein turnover and is essential for RT maintenance of contractile function in vivo."; RL Circ. Res. 111:1504-1516(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 391-637. RX PubMed=10481917; DOI=10.1016/s0092-8674(00)81981-9; RA Djinovic-Carugo K., Young P., Gautel M., Saraste M.; RT "Structure of the alpha-actinin rod: molecular basis for cross-linking of RT actin filaments."; RL Cell 98:537-546(1999). RN [18] RP STRUCTURE BY NMR OF 823-894 IN COMPLEX WITH A TITIN Z-REPEAT. RX PubMed=11573089; DOI=10.1038/nsb1001-853; RA Atkinson R.A., Joseph C., Kelly G., Muskett F.W., Frenkiel T.A., RA Nietlispach D., Pastore A.; RT "Ca2+-independent binding of an EF-hand domain to a novel motif in the RT alpha-actinin-titin complex."; RL Nat. Struct. Biol. 8:853-857(2001). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 274-746. RX PubMed=11470434; DOI=10.1016/s0969-2126(01)00619-0; RA Ylanne J., Scheffzek K., Young P., Saraste M.; RT "Crystal structure of the alpha-actinin rod reveals an extensive torsional RT twist."; RL Structure 9:597-604(2001). RN [20] RP VARIANT CMD1AA ARG-9, AND VARIANT VAL-604. RX PubMed=14567970; DOI=10.1016/s1096-7192(03)00142-2; RA Mohapatra B., Jimenez S., Lin J.H., Bowles K.R., Coveler K.J., Marx J.G., RA Chrisco M.A., Murphy R.T., Lurie P.R., Schwartz R.J., Elliott P.M., RA Vatta M., McKenna W., Towbin J.A., Bowles N.E.; RT "Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated RT cardiomyopathy and endocardial fibroelastosis."; RL Mol. Genet. Metab. 80:207-215(2003). RN [21] RP VARIANTS CMH23 THR-119; MET-495; ALA-583 AND GLY-628. RX PubMed=20022194; DOI=10.1016/j.jacc.2009.11.016; RA Chiu C., Bagnall R.D., Ingles J., Yeates L., Kennerson M., Donald J.A., RA Jormakka M., Lind J.M., Semsarian C.; RT "Mutations in alpha-actinin-2 cause hypertrophic cardiomyopathy: a genome- RT wide analysis."; RL J. Am. Coll. Cardiol. 55:1127-1135(2010). RN [22] RP VARIANT CMD1AA THR-119. RX PubMed=25224718; DOI=10.1186/s12881-014-0099-0; RA Bagnall R.D., Molloy L.K., Kalman J.M., Semsarian C.; RT "Exome sequencing identifies a mutation in the ACTN2 gene in a family with RT idiopathic ventricular fibrillation, left ventricular noncompaction, and RT sudden death."; RL BMC Med. Genet. 15:99-99(2014). RN [23] RP VARIANT CMH23 THR-228. RX PubMed=25173926; DOI=10.1161/circgenetics.113.000486; RA Girolami F., Iascone M., Tomberli B., Bardi S., Benelli M., Marseglia G., RA Pescucci C., Pezzoli L., Sana M.E., Basso C., Marziliano N., Merlini P.A., RA Fornaro A., Cecchi F., Torricelli F., Olivotto I.; RT "Novel alpha-actinin 2 variant associated with familial hypertrophic RT cardiomyopathy and juvenile atrial arrhythmias: a massively parallel RT sequencing study."; RL Circ. Cardiovasc. Genet. 7:741-750(2014). RN [24] RP VARIANTS CMYP8 ARG-727 AND 732-ALA--ILE-742 DEL, INVOLVEMENT IN CMYP8, AND RP SUBCELLULAR LOCATION. RX PubMed=30701273; DOI=10.1007/s00401-019-01963-8; RA Lornage X., Romero N.B., Grosgogeat C.A., Malfatti E., Donkervoort S., RA Marchetti M.M., Neuhaus S.B., Foley A.R., Labasse C., Schneider R., RA Carlier R.Y., Chao K.R., Medne L., Deleuze J.F., Orlikowski D., RA Boennemann C.G., Gupta V.A., Fardeau M., Boehm J., Laporte J.; RT "ACTN2 mutations cause 'Multiple structured Core Disease' (MsCD)."; RL Acta Neuropathol. 137:501-519(2019). RN [25] RP VARIANTS MPD6 PRO-131 AND ARG-487, AND INVOLVEMENT IN MPD6. RX PubMed=30900782; DOI=10.1002/ana.25470; RA Savarese M., Palmio J., Poza J.J., Weinberg J., Olive M., Cobo A.M., RA Vihola A., Jonson P.H., Sarparanta J., Garcia-Bragado F., Urtizberea J.A., RA Hackman P., Udd B.; RT "Actininopathy: A new muscular dystrophy caused by ACTN2 dominant RT mutations."; RL Ann. Neurol. 85:899-906(2019). CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor CC actin to a variety of intracellular structures. This is a bundling CC protein. CC -!- SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with ACTN3. CC Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C- CC terminal region with the LDB3 PDZ domain. Interacts with XIRP2. CC Interacts with DST isoform 1 (via N-terminus). Interacts with PARVB. CC Interacts with SYNPO2. {ECO:0000269|PubMed:10427098, CC ECO:0000269|PubMed:10984498, ECO:0000269|PubMed:11114196, CC ECO:0000269|PubMed:11171996, ECO:0000269|PubMed:11842093, CC ECO:0000269|PubMed:15159419, ECO:0000269|PubMed:17046827, CC ECO:0000269|PubMed:19932097}. CC -!- INTERACTION: CC P35609; P12814: ACTN1; NbExp=3; IntAct=EBI-77797, EBI-351710; CC P35609; P35609: ACTN2; NbExp=11; IntAct=EBI-77797, EBI-77797; CC P35609; P03950: ANG; NbExp=4; IntAct=EBI-77797, EBI-525291; CC P35609; O43827: ANGPTL7; NbExp=3; IntAct=EBI-77797, EBI-12698369; CC P35609; P05496: ATP5MC1; NbExp=3; IntAct=EBI-77797, EBI-10194585; CC P35609; Q92934: BAD; NbExp=3; IntAct=EBI-77797, EBI-700771; CC P35609; Q5PSV4: BRMS1L; NbExp=7; IntAct=EBI-77797, EBI-5666615; CC P35609; P26842: CD27; NbExp=3; IntAct=EBI-77797, EBI-520729; CC P35609; A8MYP8: CIMAP1B; NbExp=3; IntAct=EBI-77797, EBI-12010090; CC P35609; Q8WXI8: CLEC4D; NbExp=3; IntAct=EBI-77797, EBI-12703404; CC P35609; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-77797, EBI-741032; CC P35609; P29373: CRABP2; NbExp=3; IntAct=EBI-77797, EBI-10204806; CC P35609; P78560: CRADD; NbExp=3; IntAct=EBI-77797, EBI-520375; CC P35609; P50461: CSRP3; NbExp=4; IntAct=EBI-77797, EBI-5658719; CC P35609; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-77797, EBI-529989; CC P35609; Q8WW35: DYNLT2B; NbExp=3; IntAct=EBI-77797, EBI-2692044; CC P35609; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-77797, EBI-742802; CC P35609; Q6P050: FBXL22; NbExp=3; IntAct=EBI-77797, EBI-24224082; CC P35609; P23771: GATA3; NbExp=3; IntAct=EBI-77797, EBI-6664760; CC P35609; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-77797, EBI-4403685; CC P35609; P30711: GSTT1; NbExp=3; IntAct=EBI-77797, EBI-8770084; CC P35609; P62805: H4C9; NbExp=3; IntAct=EBI-77797, EBI-302023; CC P35609; P28222: HTR1B; NbExp=3; IntAct=EBI-77797, EBI-1056863; CC P35609; Q8IYT4: KATNAL2; NbExp=3; IntAct=EBI-77797, EBI-1044332; CC P35609; P22460: KCNA5; NbExp=6; IntAct=EBI-77797, EBI-6426121; CC P35609; Q9H2S1: KCNN2; NbExp=3; IntAct=EBI-77797, EBI-6658875; CC P35609; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-77797, EBI-14086479; CC P35609; Q8IY33: MICALL2; NbExp=7; IntAct=EBI-77797, EBI-2555563; CC P35609; P00540: MOS; NbExp=3; IntAct=EBI-77797, EBI-1757866; CC P35609; Q7Z7H8: MRPL10; NbExp=3; IntAct=EBI-77797, EBI-723524; CC P35609; A0A0S2Z4Y0: MYOT; NbExp=3; IntAct=EBI-77797, EBI-16430371; CC P35609; Q9UBF9: MYOT; NbExp=3; IntAct=EBI-77797, EBI-296701; CC P35609; Q9NPC6: MYOZ2; NbExp=13; IntAct=EBI-77797, EBI-746712; CC P35609; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-77797, EBI-3920396; CC P35609; Q86VF7: NRAP; NbExp=2; IntAct=EBI-77797, EBI-5660292; CC P35609; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-77797, EBI-741158; CC P35609; Q53GG5: PDLIM3; NbExp=6; IntAct=EBI-77797, EBI-5658852; CC P35609; Q53GG5-2: PDLIM3; NbExp=3; IntAct=EBI-77797, EBI-12702438; CC P35609; P62140: PPP1CB; NbExp=3; IntAct=EBI-77797, EBI-352350; CC P35609; P25786: PSMA1; NbExp=3; IntAct=EBI-77797, EBI-359352; CC P35609; P47897: QARS1; NbExp=3; IntAct=EBI-77797, EBI-347462; CC P35609; P63244: RACK1; NbExp=3; IntAct=EBI-77797, EBI-296739; CC P35609; O95059: RPP14; NbExp=3; IntAct=EBI-77797, EBI-366542; CC P35609; Q14D33: RTP5; NbExp=7; IntAct=EBI-77797, EBI-10217913; CC P35609; Q8IYX7: SAXO1; NbExp=7; IntAct=EBI-77797, EBI-3957636; CC P35609; O95863: SNAI1; NbExp=7; IntAct=EBI-77797, EBI-1045459; CC P35609; P23497: SP100; NbExp=6; IntAct=EBI-77797, EBI-751145; CC P35609; P23497-2: SP100; NbExp=3; IntAct=EBI-77797, EBI-6589365; CC P35609; Q15506: SPA17; NbExp=3; IntAct=EBI-77797, EBI-1377865; CC P35609; P49458: SRP9; NbExp=3; IntAct=EBI-77797, EBI-350743; CC P35609; Q9H987-2: SYNPO2L; NbExp=3; IntAct=EBI-77797, EBI-12082116; CC P35609; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-77797, EBI-74615; CC P35609; Q8WZ42: TTN; NbExp=16; IntAct=EBI-77797, EBI-681210; CC P35609; O75604: USP2; NbExp=3; IntAct=EBI-77797, EBI-743272; CC P35609; J3KMY6: ZC2HC1C; NbExp=3; IntAct=EBI-77797, EBI-11990572; CC P35609; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-77797, EBI-14104088; CC P35609; O60232: ZNRD2; NbExp=3; IntAct=EBI-77797, EBI-741415; CC P35609; Q61824: Adam12; Xeno; NbExp=3; IntAct=EBI-77797, EBI-77785; CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000269|PubMed:11171996, ECO:0000269|PubMed:19932097, CC ECO:0000269|PubMed:30701273}. Note=Colocalizes with MYOZ1 and FLNC at CC the Z-lines of skeletal muscle. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P35609-1; Sequence=Displayed; CC Name=2; CC IsoId=P35609-2; Sequence=VSP_054923; CC -!- TISSUE SPECIFICITY: Expressed in both skeletal and cardiac muscle. CC -!- PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation. CC {ECO:0000269|PubMed:22972877}. CC -!- DISEASE: Cardiomyopathy, familial hypertrophic, 23, with or without CC left ventricular non-compaction (CMH23) [MIM:612158]: A hereditary CC heart disorder characterized by ventricular hypertrophy, which is CC usually asymmetric and often involves the interventricular septum. The CC symptoms include dyspnea, syncope, collapse, palpitations, and chest CC pain. They can be readily provoked by exercise. The disorder has CC inter- and intrafamilial variability ranging from benign to malignant CC forms with high risk of cardiac failure and sudden cardiac death. CC {ECO:0000269|PubMed:20022194, ECO:0000269|PubMed:25173926}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cardiomyopathy, dilated, 1AA, with or without left ventricular CC non-compaction (CMD1AA) [MIM:612158]: A disorder characterized by CC ventricular dilation and impaired systolic function, resulting in CC congestive heart failure and arrhythmia. Patients are at risk of CC premature death. {ECO:0000269|PubMed:14567970, CC ECO:0000269|PubMed:25224718}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Congenital myopathy 8 (CMYP8) [MIM:618654]: An autosomal CC dominant muscular disorder characterized by progressive early-onset CC muscle weakness, gait difficulties, loss of ambulation, and respiratory CC insufficiency. Morphological and ultrastructural analyses of muscle CC biopsies reveal type 1 fiber predominance, multiple structured cores CC forming a circular arrangement beneath the sarcolemma, and jagged Z- CC lines. {ECO:0000269|PubMed:30701273}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Myopathy, distal, 6, adult onset, autosomal dominant (MPD6) CC [MIM:618655]: An autosomal dominant muscular disorder characterized by CC adult onset of asymmetric distal muscle weakness, primarily affecting CC the lower limbs and resulting in gait difficulties. Some patients CC develop involvement of proximal and upper limb muscles. CC {ECO:0000269|PubMed:30900782}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the alpha-actinin 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; M86406; AAA51583.1; -; mRNA. DR EMBL; M86804; AAA51584.1; -; Genomic_DNA. DR EMBL; AJ249756; CAB61269.1; -; Genomic_DNA. DR EMBL; AJ249757; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249758; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249759; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249760; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249761; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249762; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249763; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249764; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249765; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249766; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249767; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249768; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249769; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249770; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249771; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249772; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249773; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249774; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249775; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AJ249776; CAB61269.1; JOINED; Genomic_DNA. DR EMBL; AK315250; BAG37672.1; -; mRNA. DR EMBL; AL359185; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471098; EAW70064.1; -; Genomic_DNA. DR EMBL; CH471098; EAW70065.1; -; Genomic_DNA. DR EMBL; BC047901; AAH47901.2; -; mRNA. DR EMBL; BC051770; AAH51770.2; -; mRNA. DR CCDS; CCDS1613.1; -. [P35609-1] DR CCDS; CCDS60455.1; -. [P35609-2] DR PIR; A40199; FAHUA2. DR RefSeq; NP_001094.1; NM_001103.3. [P35609-1] DR RefSeq; NP_001265272.1; NM_001278343.1. [P35609-2] DR RefSeq; NP_001265273.1; NM_001278344.1. DR PDB; 1H8B; NMR; -; A=822-894. DR PDB; 1HCI; X-ray; 2.80 A; A/B=274-746. DR PDB; 1QUU; X-ray; 2.50 A; A=391-637. DR PDB; 4D1E; X-ray; 3.50 A; A=19-894. DR PDB; 5A36; X-ray; 2.00 A; A/B=19-266. DR PDB; 5A37; X-ray; 1.88 A; A/B=19-266. DR PDB; 5A38; X-ray; 1.90 A; A/B=19-266. DR PDB; 5A4B; X-ray; 2.01 A; A/B=19-266. DR PDB; 6SWT; X-ray; 1.20 A; A=19-270. DR PDB; 6TS3; X-ray; 1.28 A; A/B=825-894. DR PDB; 7A8T; X-ray; 2.69 A; A=274-746. DR PDB; 7A8U; X-ray; 3.80 A; A=274-746. DR PDB; 7B55; X-ray; 1.60 A; A=825-894. DR PDB; 7B56; X-ray; 1.45 A; A=825-894. DR PDB; 7B57; X-ray; 1.95 A; A=825-894. DR PDBsum; 1H8B; -. DR PDBsum; 1HCI; -. DR PDBsum; 1QUU; -. DR PDBsum; 4D1E; -. DR PDBsum; 5A36; -. DR PDBsum; 5A37; -. DR PDBsum; 5A38; -. DR PDBsum; 5A4B; -. DR PDBsum; 6SWT; -. DR PDBsum; 6TS3; -. DR PDBsum; 7A8T; -. DR PDBsum; 7A8U; -. DR PDBsum; 7B55; -. DR PDBsum; 7B56; -. DR PDBsum; 7B57; -. DR AlphaFoldDB; P35609; -. DR BMRB; P35609; -. DR SASBDB; P35609; -. DR SMR; P35609; -. DR BioGRID; 106603; 143. DR DIP; DIP-383N; -. DR IntAct; P35609; 102. DR MINT; P35609; -. DR STRING; 9606.ENSP00000355537; -. DR TCDB; 8.A.66.1.3; the dystrophin (dystrophin) family. DR GlyCosmos; P35609; 2 sites, 1 glycan. DR GlyGen; P35609; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P35609; -. DR MetOSite; P35609; -. DR PhosphoSitePlus; P35609; -. DR SwissPalm; P35609; -. DR BioMuta; ACTN2; -. DR DMDM; 543742; -. DR EPD; P35609; -. DR jPOST; P35609; -. DR MassIVE; P35609; -. DR MaxQB; P35609; -. DR PaxDb; 9606-ENSP00000443495; -. DR PeptideAtlas; P35609; -. DR PRIDE; P35609; -. DR ProteomicsDB; 3424; -. DR ProteomicsDB; 55100; -. [P35609-1] DR Pumba; P35609; -. DR Antibodypedia; 1323; 495 antibodies from 39 providers. DR DNASU; 88; -. DR Ensembl; ENST00000366578.6; ENSP00000355537.4; ENSG00000077522.15. [P35609-1] DR Ensembl; ENST00000542672.7; ENSP00000443495.1; ENSG00000077522.15. [P35609-2] DR GeneID; 88; -. DR KEGG; hsa:88; -. DR MANE-Select; ENST00000366578.6; ENSP00000355537.4; NM_001103.4; NP_001094.1. DR UCSC; uc001hyf.4; human. [P35609-1] DR AGR; HGNC:164; -. DR CTD; 88; -. DR DisGeNET; 88; -. DR GeneCards; ACTN2; -. DR GeneReviews; ACTN2; -. DR HGNC; HGNC:164; ACTN2. DR HPA; ENSG00000077522; Group enriched (heart muscle, skeletal muscle, tongue). DR MalaCards; ACTN2; -. DR MIM; 102573; gene. DR MIM; 612158; phenotype. DR MIM; 618654; phenotype. DR MIM; 618655; phenotype. DR neXtProt; NX_P35609; -. DR OpenTargets; ENSG00000077522; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy. DR PharmGKB; PA25; -. DR VEuPathDB; HostDB:ENSG00000077522; -. DR eggNOG; KOG0035; Eukaryota. DR GeneTree; ENSGT00940000153968; -. DR HOGENOM; CLU_005217_1_1_1; -. DR InParanoid; P35609; -. DR OMA; VRYDNGY; -. DR OrthoDB; 2872403at2759; -. DR PhylomeDB; P35609; -. DR TreeFam; TF352676; -. DR PathwayCommons; P35609; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-373753; Nephrin family interactions. DR Reactome; R-HSA-390522; Striated Muscle Contraction. DR Reactome; R-HSA-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors. DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission. DR Reactome; R-HSA-9620244; Long-term potentiation. DR SignaLink; P35609; -. DR BioGRID-ORCS; 88; 17 hits in 1146 CRISPR screens. DR ChiTaRS; ACTN2; human. DR EvolutionaryTrace; P35609; -. DR GeneWiki; Actinin,_alpha_2; -. DR GenomeRNAi; 88; -. DR Pharos; P35609; Tbio. DR PRO; PR:P35609; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P35609; Protein. DR Bgee; ENSG00000077522; Expressed in skeletal muscle tissue of rectus abdominis and 156 other cell types or tissues. DR ExpressionAtlas; P35609; baseline and differential. DR GO; GO:0005884; C:actin filament; TAS:ProtInc. DR GO; GO:0030054; C:cell junction; IBA:GO_Central. DR GO; GO:0042995; C:cell projection; IBA:GO_Central. DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043197; C:dendritic spine; TAS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0030175; C:filopodium; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl. DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl. DR GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl. DR GO; GO:0031143; C:pseudopodium; TAS:UniProtKB. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:UniProtKB. DR GO; GO:0051373; F:FATZ binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0005178; F:integrin binding; TAS:UniProtKB. DR GO; GO:0030274; F:LIM domain binding; IEA:Ensembl. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc. DR GO; GO:0031432; F:titin binding; IPI:BHF-UCL. DR GO; GO:0070080; F:titin Z domain binding; IMP:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0051695; P:actin filament uncapping; IMP:UniProtKB. DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB. DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB. DR GO; GO:0030035; P:microspike assembly; IDA:UniProtKB. DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central. DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:BHF-UCL. DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:BHF-UCL. DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; IMP:UniProtKB. DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:UniProtKB. DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:UniProtKB. DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL. DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0042391; P:regulation of membrane potential; IMP:BHF-UCL. DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB. DR CDD; cd21214; CH_ACTN_rpt1; 1. DR CDD; cd21216; CH_ACTN_rpt2; 1. DR CDD; cd00051; EFh; 1. DR CDD; cd00176; SPEC; 1. DR Gene3D; 1.20.58.60; -; 4. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 2. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR014837; EF-hand_Ca_insen. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR11915:SF429; ALPHA-ACTININ-2; 1. DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF08726; EFhand_Ca_insen; 1. DR Pfam; PF00435; Spectrin; 4. DR SMART; SM00033; CH; 2. DR SMART; SM00054; EFh; 2. DR SMART; SM01184; efhand_Ca_insen; 1. DR SMART; SM00150; SPEC; 3. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF46966; Spectrin repeat; 4. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS50222; EF_HAND_2; 2. DR Genevisible; P35609; HS. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Calcium; Cardiomyopathy; KW Cytoplasm; Disease variant; Metal-binding; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..894 FT /note="Alpha-actinin-2" FT /id="PRO_0000073435" FT DOMAIN 38..142 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 151..257 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT REPEAT 281..391 FT /note="Spectrin 1" FT REPEAT 401..506 FT /note="Spectrin 2" FT REPEAT 516..627 FT /note="Spectrin 3" FT REPEAT 637..740 FT /note="Spectrin 4" FT DOMAIN 753..788 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 789..824 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 1..254 FT /note="Actin-binding" FT BINDING 766 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 770 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 777 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 802 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 804 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 808 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT MOD_RES 237 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JI91" FT VAR_SEQ 234..261 FT /note="IVNTPKPDERAIMTYVSCFYHAFAGAEQ -> LVYTARPDERAIMTYVSCYY FT HAFAGAQK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054923" FT VARIANT 9 FT /note="Q -> R (in CMD1AA; dbSNP:rs121434525)" FT /evidence="ECO:0000269|PubMed:14567970" FT /id="VAR_054628" FT VARIANT 119 FT /note="A -> T (in CMH23 and CMD1AA; dbSNP:rs727502886)" FT /evidence="ECO:0000269|PubMed:20022194, FT ECO:0000269|PubMed:25224718" FT /id="VAR_071970" FT VARIANT 131 FT /note="L -> P (in MPD6; uncertain significance; FT dbSNP:rs1572114611)" FT /evidence="ECO:0000269|PubMed:30900782" FT /id="VAR_083364" FT VARIANT 228 FT /note="M -> T (in CMH23; dbSNP:rs786205144)" FT /evidence="ECO:0000269|PubMed:25173926" FT /id="VAR_074292" FT VARIANT 487 FT /note="C -> R (in MPD6; dbSNP:rs1572140109)" FT /evidence="ECO:0000269|PubMed:30900782" FT /id="VAR_083365" FT VARIANT 495 FT /note="T -> M (in CMH23; dbSNP:rs200248944)" FT /evidence="ECO:0000269|PubMed:20022194" FT /id="VAR_071971" FT VARIANT 583 FT /note="E -> A (in CMH23; dbSNP:rs200631005)" FT /evidence="ECO:0000269|PubMed:20022194" FT /id="VAR_071972" FT VARIANT 604 FT /note="M -> V (in dbSNP:rs35997569)" FT /evidence="ECO:0000269|PubMed:14567970" FT /id="VAR_033487" FT VARIANT 628 FT /note="E -> G (in CMH23; dbSNP:rs786204951)" FT /evidence="ECO:0000269|PubMed:20022194" FT /id="VAR_071973" FT VARIANT 727 FT /note="L -> R (in CMYP8; dbSNP:rs1572148902)" FT /evidence="ECO:0000269|PubMed:30701273" FT /id="VAR_083366" FT VARIANT 732..742 FT /note="Missing (in CMYP8; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30701273" FT /id="VAR_083367" FT HELIX 21..29 FT /evidence="ECO:0007829|PDB:5A36" FT HELIX 32..52 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:6SWT" FT TURN 62..68 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 70..80 FT /evidence="ECO:0007829|PDB:6SWT" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:5A36" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 119..123 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 127..142 FT /evidence="ECO:0007829|PDB:6SWT" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 153..165 FT /evidence="ECO:0007829|PDB:6SWT" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 184..193 FT /evidence="ECO:0007829|PDB:6SWT" FT TURN 195..197 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 208..222 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 231..236 FT /evidence="ECO:0007829|PDB:6SWT" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 242..256 FT /evidence="ECO:0007829|PDB:6SWT" FT HELIX 274..277 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 280..304 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 313..328 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 331..354 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 364..366 FT /evidence="ECO:0007829|PDB:1HCI" FT HELIX 368..383 FT /evidence="ECO:0007829|PDB:7A8T" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 393..416 FT /evidence="ECO:0007829|PDB:1QUU" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 420..425 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 428..431 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 434..470 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 476..536 FT /evidence="ECO:0007829|PDB:1QUU" FT TURN 537..540 FT /evidence="ECO:0007829|PDB:1QUU" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 551..562 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 564..588 FT /evidence="ECO:0007829|PDB:1QUU" FT HELIX 604..632 FT /evidence="ECO:0007829|PDB:1QUU" FT TURN 666..669 FT /evidence="ECO:0007829|PDB:1HCI" FT HELIX 671..704 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 717..745 FT /evidence="ECO:0007829|PDB:7A8T" FT HELIX 753..762 FT /evidence="ECO:0007829|PDB:4D1E" FT STRAND 767..770 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 777..784 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 794..799 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 812..820 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 825..838 FT /evidence="ECO:0007829|PDB:6TS3" FT TURN 839..841 FT /evidence="ECO:0007829|PDB:6TS3" FT STRAND 843..845 FT /evidence="ECO:0007829|PDB:6TS3" FT HELIX 847..853 FT /evidence="ECO:0007829|PDB:6TS3" FT HELIX 856..865 FT /evidence="ECO:0007829|PDB:6TS3" FT STRAND 871..873 FT /evidence="ECO:0007829|PDB:4D1E" FT HELIX 881..889 FT /evidence="ECO:0007829|PDB:6TS3" SQ SEQUENCE 894 AA; 103854 MW; 7F612C1C3B3E2299 CRC64; MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDYIASK GVKLVSIGAE EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW KDGLGLCALI HRHRPDLIDY SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP DERAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE HLAEKFRQKA STHETWAYGK EQILLQKDYE SASLTEVRAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN DRCQKICDQW DRLGTLTQKR REALERMEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ DMFIVHSIEE IQSLITAHEQ FKATLPEADG ERQSIMAIQN EVEKVIQSYN IRISSSNPYS TVTMDELRTK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG PWIQNKMEEI ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ LIQEALVFDN KHTNYTMEHI RVGWELLLTT IARTINEVET QILTRDAKGI TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA CLISMGYDLG EAEFARIMTL VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS DKPYILAEEL RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YAAFSSALYG ESDL //