ID DYST_MOUSE Reviewed; 7393 AA. AC Q91ZU6; E9PXE5; E9QL23; Q1KP04; Q3I6J6; Q60824; Q60845; Q8K5D4; Q91ZU7; AC Q91ZU8; Q9WU50; S4R1U5; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 03-SEP-2014, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Dystonin; DE AltName: Full=Bullous pemphigoid antigen 1; DE Short=BPA; DE AltName: Full=Dystonia musculorum protein; DE AltName: Full=Hemidesmosomal plaque protein; DE AltName: Full=Microtubule actin cross-linking factor 2; GN Name=Dst; Synonyms=Bpag1, Macf2; 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 {ECO:0000312|EMBL:AAK83384.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING. RC STRAIN=BALB/cJ; TISSUE=Epithelium, Muscle, and Neuron; RX PubMed=11514586; DOI=10.1083/jcb.200012098; RA Leung C.L., Zheng M., Prater S.M., Liem R.K.H.; RT "The BPAG1 locus: alternative splicing produces multiple isoforms with RT distinct cytoskeletal linker domains, including predominant isoforms in RT neurons and muscles."; RL J. Cell Biol. 154:691-697(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE RP SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Brain; RX PubMed=7670468; DOI=10.1038/ng0795-301; RA Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.; RT "The mouse dystonia musculorum gene is a neural isoform of bullous RT pemphigoid antigen 1."; RL Nat. Genet. 10:301-306(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6), ALTERNATIVE SPLICING RP (ISOFORMS 2 AND 6), AND SUBCELLULAR LOCATION (ISOFORMS 2 AND 6). RC STRAIN=C3H/HeJ; RX PubMed=16289082; DOI=10.1016/j.yexcr.2005.10.002; RA Young K.G., Pinheiro B., Kothary R.; RT "A Bpag1 isoform involved in cytoskeletal organization surrounding the RT nucleus."; RL Exp. Cell Res. 312:121-134(2006). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING RP (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7, PALMITOYLATION, RP MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6 X CBA; RX PubMed=16797530; DOI=10.1016/j.yexcr.2006.04.025; RA Jefferson J.J., Leung C.L., Liem R.K.; RT "Dissecting the sequence specific functions of alternative N-terminal RT isoforms of mouse bullous pemphigoid antigen 1."; RL Exp. Cell Res. 312:2712-2725(2006). RN [6] RP PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, X-RAY CRYSTALLOGRAPHY RP (3.0 ANGSTROMS) OF 580-803, AND SPECTRIN REPEATS. RX PubMed=17161423; DOI=10.1016/j.jmb.2006.11.036; RA Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.; RT "Structural analysis of the plakin domain of bullous pemphigoid antigen1 RT (BPAG1) suggests that plakins are members of the spectrin superfamily."; RL J. Mol. Biol. 366:244-257(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6697-7393 (ISOFORM 3), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6874-7393 (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Fetal skin, and Fetal spinal cord; 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 [8] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INTERACTION RP WITH PRPH. RC STRAIN=BALB/cJ; RX PubMed=9971739; DOI=10.1083/jcb.144.3.435; RA Leung C.L., Sun D., Liem R.K.; RT "The intermediate filament protein peripherin is the specific interaction RT partner of mouse BPAG1-n (dystonin) in neurons."; RL J. Cell Biol. 144:435-446(1999). RN [9] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RC STRAIN=Swiss Webster / NIH; RA Kubo Y., Ohba M., Iwashita S.; RT "Molecular network in NGF-mediated neural differentiation."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP ALTERNATIVE SPLICING (ISOFORM 5), DISRUPTION PHENOTYPE, SUBCELLULAR RP LOCATION (ISOFORM 5), AND TISSUE SPECIFICITY. RX PubMed=7736575; DOI=10.1016/0092-8674(95)90333-x; RA Guo L., Degenstein L., Dowling J., Yu Q.C., Wollmann R., Perman B., RA Fuchs E.; RT "Gene targeting of BPAG1: abnormalities in mechanical strength and cell RT migration in stratified epithelia and neurologic degeneration."; RL Cell 81:233-243(1995). RN [11] RP ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 5 RP AND 6), AND TISSUE SPECIFICITY. RX PubMed=8752219; DOI=10.1016/s0092-8674(00)80138-5; RA Yang Y., Dowling J., Yu Q.C., Kouklis P., Cleveland D.W., Fuchs E.; RT "An essential cytoskeletal linker protein connecting actin microfilaments RT to intermediate filaments."; RL Cell 86:655-665(1996). RN [12] RP DISRUPTION PHENOTYPE. RX PubMed=10428034; DOI=10.1016/s0092-8674(00)81017-x; RA Yang Y., Bauer C., Strasser G., Wollman R., Julien J.P., Fuchs E.; RT "Integrators of the cytoskeleton that stabilize microtubules."; RL Cell 98:229-238(1999). RN [13] RP INTERACTION WITH DES, AND DISRUPTION PHENOTYPE. RX PubMed=10357897; DOI=10.1006/dbio.1999.9263; RA Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., RA Leclerc N., Kothary R.; RT "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an RT instability of skeletal muscle cytoarchitecture."; RL Dev. Biol. 210:367-380(1999). RN [14] RP FUNCTION, DISRUPTION PHENOTYPE, ALTERNATIVE SPLICING (ISOFORM 1), RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY (ISOFORM 1). RX PubMed=14581450; DOI=10.1083/jcb.200306075; RA Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D., Wu C., RA Mobley W., Fuchs E., Yang Y.; RT "BPAG1n4 is essential for retrograde axonal transport in sensory neurons."; RL J. Cell Biol. 163:223-229(2003). RN [15] RP ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION, MUTAGENESIS RP OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=14576348; DOI=10.1242/jcs.00764; RA Young K.G., Pool M., Kothary R.; RT "Bpag1 localization to actin filaments and to the nucleus is regulated by RT its N-terminus."; RL J. Cell Sci. 116:4543-4555(2003). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [18] RP FUNCTION, INTERACTION WITH TMEM108 (ISOFORM 1), DISRUPTION PHENOTYPE, AND RP SUBCELLULAR LOCATION. RX PubMed=17287360; DOI=10.1073/pnas.0602222104; RA Liu J.J., Ding J., Wu C., Bhagavatula P., Cui B., Chu S., Mobley W.C., RA Yang Y.; RT "Retrolinkin, a membrane protein, plays an important role in retrograde RT axonal transport."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2223-2228(2007). RN [19] RP ALTERNATIVE SPLICING (ISOFORM 6), INTERACTION WITH SYNE3, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=18638474; DOI=10.1016/j.yexcr.2008.06.021; RA Young K.G., Kothary R.; RT "Dystonin/Bpag1 is a necessary endoplasmic reticulum/nuclear envelope RT protein in sensory neurons."; RL Exp. Cell Res. 314:2750-2761(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-237; SER-1381; RP SER-2211; SER-4680; SER-5488; SER-7333; SER-7336 AND SER-7348, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-208 (ISOFORM 7), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [21] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC, SUBCELLULAR RP LOCATION (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. 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 [22] RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION OF ISOFORM 2, SUBCELLULAR RP LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=20209123; DOI=10.1371/journal.pone.0009465; RA Boyer J.G., Bhanot K., Kothary R., Boudreau-Lariviere C.; RT "Hearts of dystonia musculorum mice display normal morphological and RT histological features but show signs of cardiac stress."; RL PLoS ONE 5:E9465-E9465(2010). CC -!- FUNCTION: Cytoskeletal linker protein. Acts as an integrator of CC intermediate filaments, actin and microtubule cytoskeleton networks. CC Required for anchoring either intermediate filaments to the actin CC cytoskeleton in neural and muscle cells or keratin-containing CC intermediate filaments to hemidesmosomes in epithelial cells. The CC proteins may self-aggregate to form filaments or a two-dimensional CC mesh. Regulates the organization and stability of the microtubule CC network of sensory neurons to allow axonal transport. Mediates docking CC of the dynein/dynactin motor complex to vesicle cargos for retrograde CC axonal transport through its interaction with TMEM108 and DCTN1. CC {ECO:0000269|PubMed:17287360}. CC -!- FUNCTION: [Isoform 5]: Plays a structural role in the assembly of CC hemidesmosomes of epithelial cells; anchors keratin-containing CC intermediate filaments to the inner plaque of hemidesmosomes. Required CC for the regulation of keratinocyte polarity and motility; mediates CC integrin ITGB4 regulation of RAC1 activity. CC -!- FUNCTION: [Isoform 6]: Required for bundling actin filaments around the CC nucleus. CC -!- SUBUNIT: Homodimer. Interacts with MAPRE1; probably required for CC targeting to the growing microtubule plus ends. Isoform 2 interacts CC (via N-terminus) with ACTN2. Isoform 2 interacts (via N-terminus) with CC PLEC (via N-terminus). Isoform 5 interacts (via N-terminus) with CC COL17A1 (via cytoplasmic region). Isoform 5 interacts (via N-terminus) CC with ITGB4 isoform beta-4a (via cytoplasmic region). Isoform 5 CC interacts (via N-terminus) with ERBIN (via C-terminus). Isoform 5 CC associates (via C-terminal) with KRT5-KRT14 (via rod region) CC intermediate filaments of keratins (By similarity). Isoform 2 and CC isoform 6 can homodimerize (via N-terminus). Isoform 2 interacts (via CC N-terminus) with PLEC (via N-terminus). Interacts with the neuronal CC intermediate filament protein, PRPH. Interacts with DES. Interacts with CC SYNE3. Isoform 1 interacts with TMEM108 (PubMed:17287360). CC {ECO:0000250|UniProtKB:Q03001, ECO:0000269|PubMed:10357897, CC ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:18638474, CC ECO:0000269|PubMed:19932097, ECO:0000269|PubMed:9971739}. CC -!- INTERACTION: CC Q91ZU6; P21807: Prph; Xeno; NbExp=3; IntAct=EBI-446159, EBI-446227; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC stress fiber. Cell projection, axon {ECO:0000269|PubMed:17287360}. CC Note=Associates with axonal microtubules at the growing distal tip and CC intermediate filaments, but not with actin cytoskeleton, in sensory CC neurons (By similarity). Associates with intermediate filaments, actin CC and microtubule cytoskeletons. Localizes to actin stress fibers and to CC actin-rich ruffling at the cortex of cells. {ECO:0000250, CC ECO:0000269|PubMed:14576348}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:19932097}. Note=Colocalizes both cortical and CC cytoplasmic actin filaments (PubMed:19932097). Localizes to vesicule- CC like structures associated with microtubules (PubMed:14581450, CC PubMed:17287360). {ECO:0000269|PubMed:14581450, CC ECO:0000269|PubMed:17287360, ECO:0000269|PubMed:19932097}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane, sarcolemma. CC Cytoplasm, myofibril, sarcomere, Z line. Cytoplasm, myofibril, CC sarcomere, H zone. Cytoplasm, cytoskeleton. Note=Localizes to CC microtubules and actin microfilaments throughout the cytoplasm and at CC focal contact attachments at the plasma membrane. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytoskeleton. Cell CC junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-KRT14 CC intermediate filaments network of keratins. Colocalizes with ITGB4 at CC the leading edge of migrating keratinocytes (By similarity). Localizes CC to actin and intermediate filaments cytoskeletons. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus. Nucleus envelope. Membrane; CC Single-pass membrane protein. Endoplasmic reticulum membrane; Single- CC pass membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, CC cytoskeleton, stress fiber {ECO:0000269|PubMed:14576348}. CC Note=Associates with actin cytoskeleton in sensory neurons (By CC similarity). Localizes to actin and intermediate filaments CC cytoskeletons. Localizes to central actin stress fibers around the CC nucleus and is excluded form focal contact sites in myoblast cells. CC Translocates to the nucleus. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm, cytoskeleton. Cytoplasm, CC cell cortex. Cell membrane; Lipid-anchor. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7; CC Name=2 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-b, BPAG1a1, CC dystonin-1; CC IsoId=Q91ZU6-1; Sequence=Displayed; CC Name=1 {ECO:0000269|PubMed:11514586}; Synonyms=BPAG1-a CC {ECO:0000303|PubMed:14581450}, BPAG1a2, BPAG1n4 CC {ECO:0000303|PubMed:14581450}; CC IsoId=Q91ZU6-2; Sequence=VSP_041549; CC Name=3 {ECO:0000305}; CC IsoId=Q91ZU6-3; Sequence=VSP_041550, VSP_041551, VSP_041552; CC Name=4 {ECO:0000305}; CC IsoId=Q91ZU6-4; Sequence=VSP_041551, VSP_041552; CC Name=5; Synonyms=BPAG1-e; CC IsoId=Q91ZU6-5; Sequence=VSP_055459, VSP_055460, VSP_055461; CC Name=6; Synonyms=BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2; CC IsoId=Q91ZU6-6; Sequence=VSP_041543, VSP_041546; CC Name=7; Synonyms=BPAG1a3; CC IsoId=Q91ZU6-8; Sequence=VSP_041542, VSP_041544, VSP_041545; CC -!- TISSUE SPECIFICITY: Isoform 1 and 2 are expressed in striated and heart CC muscle cells. Isoform 5 is expressed in the skin. Isoform 6 is CC expressed in sensory neural cells of the dorsal root ganglion and with CC low level in the skin (at protein level). Isoform 1 is expressed CC predominantly in the brain and spinal cord with low levels in the heart CC (PubMed:14581450). Isoform 2 is predominantly expressed in muscle and CC heart and with low levels in the brain. Isoform 5 is expressed in the CC skin and with low levels in myoblast cells. Isoform 6 is expressed in CC neurons. Isoform 7 is expressed in lung and with low levels in the CC brain. {ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:14576348, CC ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:16797530, CC ECO:0000269|PubMed:18638474, ECO:0000269|PubMed:19932097, CC ECO:0000269|PubMed:20209123, ECO:0000269|PubMed:7670468, CC ECO:0000269|PubMed:7736575, ECO:0000269|PubMed:8752219}. CC -!- DEVELOPMENTAL STAGE: Isoform 1 is the major form expressed in the CC dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly expressed CC in the myocardium, skeletal muscles, bone cartilage and epithelia of CC the tongue at 14.5 dpc. Isoform 5 is expressed at high levels in the CC epidermis and mucosal epithelia of the digestive tracts at 14.5 dpc. CC {ECO:0000269|PubMed:11514586, ECO:0000269|PubMed:7670468}. CC -!- DOMAIN: Its association with epidermal and simple keratins is dependent CC on the tertiary structure induced by heterodimerization of these CC intermediate filaments proteins and most likely involves recognition CC sites located in the rod domain of these keratins. CC -!- DOMAIN: The microtubule tip localization signal (MtLS) motif; mediates CC interaction with MAPRE1 and targeting to the growing microtubule plus CC ends. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice show progressive deterioration in motor CC function and sensory neurodegeneration. Exhibit axonal swellings packed CC with disorganized intermediate filaments (IFs) and microtubules. Show CC poorly defined Z lines and display a reduction in sarcomere length. CC Have increased accumulation of vesicles and severely disrupted CC retrograde axonal transport. In stratified epithelia, hemidesmosomes CC are normal but they lack the inner plate and have no cytoskeleton CC attached. {ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:10428034, CC ECO:0000269|PubMed:14581450, ECO:0000269|PubMed:17287360, CC ECO:0000269|PubMed:7736575}. CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. Transmembrane protein CC (helical transmembrane domain from amino acid 18 to 38). {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Incomplete sequence. Probably myristoylated CC on Gly-2. Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of CC Gly-2 to Ala inhibits cortical localization. Mutagenesis of Cys-5 to CC Ser inhibits cortical localization. Mutagenesis of Cys-7 to Ser CC inhibits cortical localization. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK83382.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305}; CC Sequence=AAK83383.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305}; CC Sequence=AAK83384.1; Type=Miscellaneous discrepancy; Note=Many conflicts and frameshifts that might be strain-specific.; Evidence={ECO:0000305}; CC Sequence=AAC52231.1; Type=Frameshift; Evidence={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; AF396877; AAK83382.1; ALT_SEQ; mRNA. DR EMBL; AF396878; AAK83383.1; ALT_SEQ; mRNA. DR EMBL; AF396879; AAK83384.1; ALT_SEQ; mRNA. DR EMBL; AC123072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC124386; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127433; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U22452; AAC52230.1; -; mRNA. DR EMBL; U25158; AAC52231.1; ALT_FRAME; mRNA. DR EMBL; DQ023311; AAY46942.1; -; mRNA. DR EMBL; DQ463750; ABF00406.1; -; mRNA. DR EMBL; AK051626; BAC34695.1; -; mRNA. DR EMBL; AK037206; BAC29753.1; -; mRNA. DR EMBL; AF115383; AAD22959.1; -; mRNA. DR EMBL; AB085694; BAB93448.1; -; mRNA. DR CCDS; CCDS35534.1; -. [Q91ZU6-1] DR CCDS; CCDS35535.1; -. [Q91ZU6-2] DR CCDS; CCDS69875.1; -. [Q91ZU6-5] DR PIR; A60776; A60776. DR PIR; I49290; I49290. DR PIR; I49298; I49298. DR RefSeq; NP_034211.2; NM_010081.2. [Q91ZU6-5] DR RefSeq; NP_598594.2; NM_133833.3. [Q91ZU6-2] DR RefSeq; NP_604443.2; NM_134448.3. [Q91ZU6-1] DR PDB; 2IAK; X-ray; 3.00 A; A=580-803. DR PDBsum; 2IAK; -. DR SMR; Q91ZU6; -. DR BioGRID; 199328; 16. DR IntAct; Q91ZU6; 9. DR MINT; Q91ZU6; -. DR STRING; 10090.ENSMUSP00000138308; -. DR ChEMBL; CHEMBL2176789; -. DR GlyGen; Q91ZU6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q91ZU6; -. DR PhosphoSitePlus; Q91ZU6; -. DR SwissPalm; Q91ZU6; -. DR REPRODUCTION-2DPAGE; IPI00230689; -. DR REPRODUCTION-2DPAGE; IPI00230690; -. DR REPRODUCTION-2DPAGE; IPI00284272; -. DR EPD; Q91ZU6; -. DR jPOST; Q91ZU6; -. DR MaxQB; Q91ZU6; -. DR PaxDb; 10090-ENSMUSP00000095392; -. DR PeptideAtlas; Q91ZU6; -. DR ProteomicsDB; 279588; -. [Q91ZU6-1] DR ProteomicsDB; 279589; -. [Q91ZU6-2] DR ProteomicsDB; 279590; -. [Q91ZU6-3] DR ProteomicsDB; 279591; -. [Q91ZU6-4] DR ProteomicsDB; 279592; -. [Q91ZU6-5] DR ProteomicsDB; 279593; -. [Q91ZU6-6] DR ProteomicsDB; 279594; -. [Q91ZU6-8] DR Pumba; Q91ZU6; -. DR Antibodypedia; 31066; 193 antibodies from 23 providers. DR DNASU; 13518; -. DR Ensembl; ENSMUST00000097785.10; ENSMUSP00000095392.3; ENSMUSG00000026131.22. [Q91ZU6-1] DR Ensembl; ENSMUST00000097786.10; ENSMUSP00000095393.3; ENSMUSG00000026131.22. [Q91ZU6-2] DR Ensembl; ENSMUST00000183302.6; ENSMUSP00000138376.4; ENSMUSG00000026131.22. [Q91ZU6-5] DR GeneID; 13518; -. DR KEGG; mmu:13518; -. DR UCSC; uc007aoi.2; mouse. [Q91ZU6-1] DR UCSC; uc007aoj.2; mouse. [Q91ZU6-2] DR UCSC; uc007aok.1; mouse. [Q91ZU6-8] DR UCSC; uc007aol.2; mouse. [Q91ZU6-5] DR AGR; MGI:104627; -. DR CTD; 667; -. DR MGI; MGI:104627; Dst. DR VEuPathDB; HostDB:ENSMUSG00000026131; -. DR eggNOG; KOG0516; Eukaryota. DR eggNOG; KOG0517; Eukaryota. DR GeneTree; ENSGT00940000155008; -. DR HOGENOM; CLU_000015_1_0_1; -. DR InParanoid; Q91ZU6; -. DR OMA; RQKATMV; -. DR OrthoDB; 5489926at2759; -. DR Reactome; R-MMU-446107; Type I hemidesmosome assembly. DR Reactome; R-MMU-9013420; RHOU GTPase cycle. DR Reactome; R-MMU-9013424; RHOV GTPase cycle. DR Reactome; R-MMU-9696264; RND3 GTPase cycle. DR Reactome; R-MMU-9696270; RND2 GTPase cycle. DR Reactome; R-MMU-9696273; RND1 GTPase cycle. DR BioGRID-ORCS; 13518; 1 hit in 77 CRISPR screens. DR ChiTaRS; Dst; mouse. DR EvolutionaryTrace; Q91ZU6; -. DR PRO; PR:Q91ZU6; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q91ZU6; Protein. DR Bgee; ENSMUSG00000026131; Expressed in aorta tunica media and 259 other cell types or tissues. DR ExpressionAtlas; Q91ZU6; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0031252; C:cell leading edge; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0031673; C:H zone; IDA:UniProtKB. DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB. DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; IDA:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB. DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB. DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB. DR GO; GO:0045098; C:type III intermediate filament; IDA:MGI. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005178; F:integrin binding; ISO:MGI. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central. DR GO; GO:0007409; P:axonogenesis; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0048870; P:cell motility; ISO:MGI. DR GO; GO:0007010; P:cytoskeleton organization; IMP:MGI. DR GO; GO:0031581; P:hemidesmosome assembly; ISO:MGI. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0046907; P:intracellular transport; IDA:UniProtKB. DR GO; GO:0030011; P:maintenance of cell polarity; ISO:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI. DR GO; GO:0009611; P:response to wounding; ISO:MGI. DR GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB. DR GO; GO:0042060; P:wound healing; IBA:GO_Central. DR CDD; cd21236; CH_DYST_rpt1; 1. DR CDD; cd21239; CH_DYST_rpt2; 1. DR CDD; cd00051; EFh; 1. DR CDD; cd00176; SPEC; 15. DR Gene3D; 1.20.58.1060; -; 1. DR Gene3D; 1.20.58.60; -; 30. DR Gene3D; 1.10.418.10; Calponin-like domain; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.30.920.20; Gas2-like domain; 1. DR Gene3D; 3.90.1290.10; Plakin repeat; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001589; Actinin_actin-bd_CS. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR041615; Desmoplakin_SH3. DR InterPro; IPR041573; Desmoplakin_Spectrin-like. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR003108; GAR_dom. DR InterPro; IPR036534; GAR_dom_sf. DR InterPro; IPR049538; PCN-like_spectrin-like_rpt. DR InterPro; IPR043197; Plakin. DR InterPro; IPR035915; Plakin_repeat_sf. DR InterPro; IPR001101; Plectin_repeat. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR23169; ENVOPLAKIN; 1. DR PANTHER; PTHR23169:SF21; EPIPLAKIN; 1. DR Pfam; PF00307; CH; 2. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF02187; GAS2; 1. DR Pfam; PF00681; Plectin; 1. DR Pfam; PF17902; SH3_10; 1. DR Pfam; PF00435; Spectrin; 19. DR Pfam; PF18373; Spectrin_2; 1. DR Pfam; PF21019; Spectrin_3; 1. DR Pfam; PF21020; Spectrin_4; 1. DR Pfam; PF21097; SR_plectin_7; 1. DR SMART; SM00033; CH; 2. DR SMART; SM00054; EFh; 2. DR SMART; SM00243; GAS2; 1. DR SMART; SM00250; PLEC; 9. DR SMART; SM00150; SPEC; 33. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF143575; GAS2 domain-like; 1. DR SUPFAM; SSF75399; Plakin repeat; 2. DR SUPFAM; SSF46966; Spectrin repeat; 26. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS50021; CH; 2. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51460; GAR; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q91ZU6; MM. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative promoter usage; KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Endoplasmic reticulum; Intermediate filament; KW Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule; KW Muscle protein; Myristate; Nucleus; Palmitate; Phosphoprotein; KW Reference proteome; Repeat; SH3 domain; Transmembrane; Ubl conjugation. FT CHAIN 1..7393 FT /note="Dystonin" FT /id="PRO_0000078141" FT DOMAIN 35..138 FT /note="Calponin-homology (CH) 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044, FT ECO:0000305" FT DOMAIN 151..255 FT /note="Calponin-homology (CH) 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044, FT ECO:0000305" FT REPEAT 602..699 FT /note="Spectrin 1" FT REPEAT 701..802 FT /note="Spectrin 2" FT DOMAIN 887..944 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REPEAT 1292..1421 FT /note="Spectrin 3" FT REPEAT 1439..1538 FT /note="Spectrin 4" FT REPEAT 1584..1626 FT /note="Plectin 1" FT REPEAT 1660..1703 FT /note="Plectin 2" FT REPEAT 1774..1817 FT /note="Plectin 3" FT REPEAT 1818..1855 FT /note="Plectin 4" FT REPEAT 1856..1891 FT /note="Plectin 5" FT REPEAT 3321..3427 FT /note="Spectrin 5" FT REPEAT 3569..3678 FT /note="Spectrin 6" FT REPEAT 3852..3971 FT /note="Spectrin 7" FT REPEAT 3978..4084 FT /note="Spectrin 8" FT REPEAT 4091..4190 FT /note="Spectrin 9" FT REPEAT 4200..4299 FT /note="Spectrin 10" FT REPEAT 4447..4552 FT /note="Spectrin 11" FT REPEAT 4559..4663 FT /note="Spectrin 12" FT REPEAT 4673..4773 FT /note="Spectrin 13" FT REPEAT 4780..4882 FT /note="Spectrin 14" FT REPEAT 4889..4989 FT /note="Spectrin 15" FT REPEAT 4999..5098 FT /note="Spectrin 16" FT REPEAT 5105..5208 FT /note="Spectrin 17" FT REPEAT 5215..5319 FT /note="Spectrin 18" FT REPEAT 5326..5428 FT /note="Spectrin 19" FT REPEAT 5435..5537 FT /note="Spectrin 20" FT REPEAT 5653..5755 FT /note="Spectrin 21" FT REPEAT 5763..5863 FT /note="Spectrin 22" FT REPEAT 5870..5976 FT /note="Spectrin 23" FT REPEAT 5983..6085 FT /note="Spectrin 24" FT REPEAT 6092..6195 FT /note="Spectrin 25" FT REPEAT 6202..6304 FT /note="Spectrin 26" FT REPEAT 6311..6413 FT /note="Spectrin 27" FT REPEAT 6420..6522 FT /note="Spectrin 28" FT REPEAT 6529..6632 FT /note="Spectrin 29" FT REPEAT 6639..6740 FT /note="Spectrin 30" FT REPEAT 6747..6849 FT /note="Spectrin 31" FT REPEAT 6859..6989 FT /note="Spectrin 32" FT DOMAIN 7019..7054 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7055..7090 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 7095..7173 FT /note="GAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792" FT REGION 35..252 FT /note="Actin-binding" FT REGION 2114..2200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2216..2253 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2274..2425 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2473..2820 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3044..3063 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 3281..3317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7180..7199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7217..7275 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 7303..7393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1382..1388 FT /note="Nuclear localization signal; in isoform 6" FT MOTIF 7373..7376 FT /note="Microtubule tip localization signal" FT COMPBIAS 2114..2142 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2181..2195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2281..2308 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2321..2343 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2384..2425 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2479..2499 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2505..2539 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2540..2558 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2560..2576 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2620..2636 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2677..2693 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2763..2780 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2791..2805 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3049..3063 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3295..3309 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7183..7199 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7233..7251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7338..7352 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 7370..7384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 7032 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7034 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7036 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7038 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7043 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7068 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7070 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7072 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7074 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 7079 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 237 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1381 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2211 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2862 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03001" FT MOD_RES 3894 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03001" FT MOD_RES 4680 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 5488 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 7254 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03001" FT MOD_RES 7333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 7336 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 7348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 5401 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:Q03001" FT VAR_SEQ 1..381 FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV FT NIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQATEGYAG FT VRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKIGVIRLLD FT PEDVDVSSPDEKSVITYVSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWIR FT HHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEKSKIKRLYKLLEIWIEFGRI FT KLLQGYHPNDIEKEWGKLIIAMLEREKALRPEVE -> MQSSSYSYRSSDSVFSNTTST FT RTSLDSNENLLSVHCGPTLINSCISFSNESLDGH (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11514586" FT /id="VSP_055459" FT VAR_SEQ 1..137 FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTFTKWINQHLMKV FT RKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKLV FT NIRNDDITDGNPKLTLGLIWTIILHF -> MGNVCGCVRAEKEEPYFDPAKSPLSPEKY FT SPGRKYFRRKPCQKVVDDTEPVRQSSEREGKKGVSQPAGGQPAVSSGELPWEDPAASPT FT KEDAVQLGKRAATEHGDQKPLPSSVDGYPHRVTVSSAQGRYSEVQVSIPDKIISEEDSP FT PYCPETERHLDDVNSKHRTFLRKDNVSLSQTAASSSPILCVTEKSLKNSALMGNLSRSC FT HSVLEQDSDERGHPFGVHRLQLTKRRCHSLSSGVSCVSKDAPRDDGC (in isoform FT 7)" FT /evidence="ECO:0000303|PubMed:16797530" FT /id="VSP_041542" FT VAR_SEQ 1..30 FT /note="MAGYLSPAAYMYVEEQEYLQAYEDVLERYK -> MIAAAFLVLLRPYSIQCA FT LFLLLLLLGTVATIVFFCCWHRKLQKGRHPMKSVFSGRSRSRDAALRSHHFRSEGFRAS FT PRHIRRRVAAAAAARLEEVKPVVEVHHQSEQESSGRKRRIKKNSRVQPEFYHSVQGAST FT RRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASPAPGDTLPWNLPKHERSKRKIQGGS FT VLDPAERAVLRIA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16289082" FT /id="VSP_041543" FT VAR_SEQ 271..272 FT /note="VK -> KG (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16797530" FT /id="VSP_041544" FT VAR_SEQ 273..7393 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16797530" FT /id="VSP_041545" FT VAR_SEQ 305..7393 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16289082" FT /id="VSP_041546" FT VAR_SEQ 1432 FT /note="K -> MKRSKENSEHGAYSDLLQRQRATMVENSKLTGKISELETMVAELKKQ FT KSRVEEELPKVKEAAENELRKQQRNVEDIALQKLRAESEAKQYRRELETIVREKEAAER FT ELERVRQLTAEAEARRAAVEENLRNFRSQLQENTFTRQTLEDHLRRKDSSLSDLEQQKR FT ALVEELQRKRDHEEELLRLVKQMERDLAFQKQVAEKQLKEKQKVELEARRKITEIQFSC FT RESAAVAQARPQREQGRQKEEELKQQVDELTLANRKAEKEMRELKYELSAVQLEKASSE FT EKARLLKDKLDETNNTLKCLKEDLERKDQAQERYSQQLRDLGRQLNQTTDKAEEVRQEA FT NDLKKIKHTYQLELESLHQEKGKLQREVDRVTRAHALAERNIQCLNSQVHASRDEKDLS FT EERRRLCQRKSDHLKEEFERSHAQLLQNIQAEKENNDKIQKLNKELEKSNECAETLKQK FT VDELTRQNNETKLMMQRIQAESKNIVREKQAIQQRCEVLRIQADGFKDQLRNTNEHLHK FT QTKTEQDFHRKIKSLEDDLAQSQNLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKE FT EKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTHRKMILLQEESDKFKRSAD FT EFRKKMEKLMESKVVTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQLQCYR FT EKMQQGPPVEANHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHEHQLLRLQCEIQKK FT STTQDHTFASAFDTAGRECHHPAEISPGNSGHLNLKTRLPLSRWTQEPHQTEGKWPHRA FT AEQLPKEVQFRQPGAPLDRESSQPCYSEYFSQTSTELQITFDDKNPITRLSELETMREQ FT ALHPSRPPVTYQDDKLERELVKLLTPLEIAKNKQCGMHTEVTTLKQEKRLGSSAGGWML FT EGCRTSGGLKGDFLKKSVEPEASPSLDLNQACSVRDEEFQFQGLRHTVTGRQLVEAKLL FT DMRTVEQLRLGLKTVEEVQRSLSKFLTKATSIAGLYLESSKEKMSFTSAAQKIIIDKMI FT ALAFLEAQAATGFIIDPVSGQTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGYSHASKTL FT SVFQAMENRMLDRKKGKHILEAQIASGGVIDPVRGVRVPPEMAVQQGLLNNAVLQFLHE FT PSSNTRVFPNPNNKQALYYSELLQICVFDVDCQCFLLPFGEREISNLNIEKTHKIAVVD FT TKTGAELTAFEAFQRNLIDKGIYLELSGQQYQWKEATFFDSYGHPSHMLTDTKTGLQFN FT ISEAVEQGTLDKALVQKYQEGLTTLTELADFLLSKVVPKKDLHSPIAGYWLTASGERIS FT LLKASRRNLVDRVTALRCLEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFAQQLRQC FT ELVITGISHPVSNKMMSVVEAVNANIISKEMGMRCLEFQYLTGGLIEPKVFSRLTIEEA FT LHVGIIDVLIATRLKDQKSYVRDIMCPQTKRKLTYKEALEKADFDFHTGLKLLEVSEPL FT GTGISNLYYSSQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11514586" FT /id="VSP_055460" FT VAR_SEQ 1433..7393 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:11514586" FT /id="VSP_055461" FT VAR_SEQ 1549..3562 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:11514586" FT /id="VSP_041549" FT VAR_SEQ 7129..7134 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_041550" FT VAR_SEQ 7174..7197 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_041551" FT VAR_SEQ 7265 FT /note="K -> KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSSAE (in FT isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_041552" FT MUTAGEN 1385 FT /note="R->A: Prevents isoform 6 from localizing to the FT nucleus; when associated with A-1386." FT /evidence="ECO:0000269|PubMed:14576348" FT MUTAGEN 1386 FT /note="R->A: Prevents isoform 6 from localizing to the FT nucleus; when associated with A-1385." FT /evidence="ECO:0000269|PubMed:14576348" FT HELIX 590..593 FT /evidence="ECO:0007829|PDB:2IAK" FT STRAND 594..596 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 600..604 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 608..623 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 631..650 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 652..661 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 662..664 FT /evidence="ECO:0007829|PDB:2IAK" FT TURN 667..669 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 670..686 FT /evidence="ECO:0007829|PDB:2IAK" FT TURN 687..689 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 690..722 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 744..767 FT /evidence="ECO:0007829|PDB:2IAK" FT HELIX 773..793 FT /evidence="ECO:0007829|PDB:2IAK" FT CONFLICT Q91ZU6-6:101 FT /note="E -> K (in Ref. 3; AAC52231)" FT /evidence="ECO:0000305" FT MOD_RES Q91ZU6-8:205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES Q91ZU6-8:208 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" SQ SEQUENCE 7393 AA; 834218 MW; C3CDF88978C33EF1 CRC64; MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE SEVAYDWSER NSSVARKKSY HAELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI EITIYKDDEC VLANNSHRAK WKVISPTGNE AMVPSVCFTV PPPNKEAVDF ANRIEQQYQS VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN TASVLKSVTL PDKMPDLGDL EDCKNAKRWL SFCKLQPSTV HDYRQEEGGS DGEEPVTAQS SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVGML LESCGTELGA DTSTRESLSV LTIPDAFPDC ALSEEKHECS AAAAGPDKCH YSHPGHKESL ENAKWDMNEA FCKMGNNDSN GELPRPENLA DTTVVQKGSE SPSRVRVPKP TSSSTQPEGS VLRPESGSIL KGCKSQSEPV TKKYPDGANH SHFLTSETSR PCDSNEREDE ENIQKGPSVF DYSPRLSALL SHDELRQSQG RFSDTSTPQN TGYLCEASTL SPSDQRVLAD QSTREKFQDQ FLGIAAISVS LQGAPCGQKP VDTECSSSQV HYHSEESMSD ASAESGATRQ TDESEKTGSK VEDNSCTMVP GGGSRNDNTS DCGPLSHKGA IDAGDYETSL LAGQQSDTAT DSDSDDYFYD TPLFEDEDHD SLILQGDDRD CLQPEDYDTS LQEENDRTPP PDDIFYDVMK EKENPEFPHG GMDESLGVEN KVCCPQGFPV GIEKPELYLA GEKEFNSGGS EQLVESVSES ENPPGLWDSE SDSLTEGEII GRKERLGASL TPDGHWRGDR EECDTSRESQ SDTDGVGSIQ SSESYRPYMS DGSDLDEEDN GGRSSEDSGD GRGGQGVADE GGEPQYQADP TQLYTAIRKE HGGETQNVSD MIPLDKTHSY SPLETQHGAG VFQPESAGRG GWDTERSSHP ELTTEADEED EASLSTHMAT KGVSLSNAEG TASEEIRLVQ GPDSTGILKA EDLENVSPEI SPSSDNIVRS EAELGGGASE DGHLSFTGSD RDQQGPGRGL VKGRDGQSDK LVDETSIREM GFQKEGVLMS SPEEGGEEER DLEPFPNGSA TESLNMGKSQ VPPLLTHTEE LSHRGAPHTT TMTTTMTLEG EAKNVQTGLT ESPVLLETLA EIFDTPASKV TRADLTSAVT ASEMKSQVKE DSLTGGPEKE TGPCTSLGHC DKCIHVDMLE PNEHTPSCAL VAPPTVKDNL CSVNNAGEKS VRPQEDWPPA AEVRLSDACV EESISEGKAG ILQFTPENSD STLSRLPHQS VAGWGKSADS VQARLPVSGV RHTSADTLDV GCPQLESSRE KASAEEEPHR ERALSLKPQE REHHMLGFVE DGRSILKSSL DKVHMNLQEV GDPSAGTGTK ISIQNLIRRA ILSELPNEVS NVPSHGISPI SNSSEVRAES GGDPFCITSF LHLLKQNQPP QETPGISELA KVLTQMDCDP EQRGLGSELL PPQLKNAFYK LLFDGYATEK DQAEALGQTS CAVPKMAEEK PHVCSDLRNK EGHHCPLNPQ AVGEAEVEPF SVHIAALPGG EKLGELCSEP PEHSESTSGS KERSSDSSSK EKCSNGLQQC LQHTEKMHEY LVLLQDMKPP LDNQASVESS LEALKSQLKQ LEAFELGLAP IAVFLRKDLK LAEEFLKSFP SDLPRRHHEE LSKSHQRLQN AFSSLSSVSS ERMKLIKLAI NSEMSKLAVR HEDFLHKLTS YSDWVSEKSR SVKAIQTVNV QDTELVKNSV KFLKNVLADL SHTKMQLETT AFDVQSFISD YAQDLSPSQS RQLLRLLNTT QKGFLDLQEL VTTEADRLEA LLQLEQELGH QKVVAERQQE YREKLQGLCD LLTQTENRLI SNQEAFVIGD GTVELQKYQS KQEELQRDMQ GSTQAMEEIV RNTELFLKES GDELSQADRA LIEQKLNEVK MKCAQLNLKA EQSRKELDKA VTTALKEETE KVAAVRQLEE SKTKIENLLN WLSNVEEDSE GVWTKHTQPM EQNGTYLHEG DSKLGAGEED EVNGNLLETD AEGHSEATKG NLNQQYEKVK AQHGKIMAQH QAVLLATQSA QVLLEKQGHY LSPEEKEKLQ KNTQELKVHY EKVLAECEKK VKLTHSLQEE LEKFDTDYSE FEHWLQQSEQ ELANLEAGAD DLSGLMDKLT RQKSFSEDVI SHKGDLRYIT ISGNRVIDAA KSCSKRDSDR IGKDSVETSA THREVQTKLD QVTDRFRSLY SKCSVLGNNL KDLVDQYQQY EDASCGLLSG LQACEAKASK HLREPIALDP KNLQRQLEET KALQGQISSQ QVAVEKLKKT AEVLLDAKGS LLPAKNDIQK TLDDIVGRYD DLSKCVNERN EKLQITLTRS LSVQDALDEM LDWMGSVESS LVKPGQVPLN STALQDLISK DTMLEQDITG RQSSINAMNE KVKTFIETTD PSTASSLQAK MKDLSARFSE ASQKHKEKLA KMVELKAKVE QFEKLSDKLQ TFLETQSQAL TEVAMPGKDV PELSQHMQES TAKFLEHRKD LEALHSLLKE ISSHGLPGDK ALVFEKTNNL SRKFKEMEDT IQEKKDALSS CQEQLSAFQT LAQSLKTWIK ETTKQVPVVK PSLGTEDLRK SLEETKKLQE KWNLKAPEIH KANNSGVSLC NLLSALISPA KAIAAAKSGG VILNGEGTDT NTQDFLANKG LTSIKKDMTD ISHSYEDLGL LLKDKIVELN TKLSKLQKAQ EESSAMMQWL EKMNKTASRW RQTPTPADTE SVKLQVEQNK SFEAELKQNV NKVQELKDKL SELLEENPEA PEAQSWKQAL AEMDTKWQEL NQLTMDRQQK LEESSNNLTQ FQTTEAQLKQ WLMEKELMVS VLGPLSIDPN MLNTQKQQVQ ILLQEFDTRK PQYEQLTAAG QGILSRPGED PSLHGIVNEQ LEAVTQKWDN LTGQLRDRCD WIDQAIVKST QYQSLLRSLS GTLTELDDKL SSGLTSGALP DAVNQQLEAA QRLKQEIEQQ APKIKEAQEV CEDLSALVKE EYLKAELSRQ LEGILKSFKD IEQKTENHVQ HLQSACASSH QFQQMSKDFQ AWLDAKKEEQ RDSPPISAKL DVLESLLNSQ KDFGKTFTEQ SNIYEKTISE GENLLLKTQG AEKAALQLQL NTMKTDWDRF RKQVKEREEK LKDSLEKALK YREQVETLRP WIDRCQHSLD GVTFSLDPTE SESSIAELKS LQKEMDHHFG MLELLNNTAN SLLSVCEVDK EAVTEENQSL MEKVNRVTEQ LQSKTVSLEN MAQKFKEFQE VSRDTQRQLQ DTKEQLEVHH SLGPQAYSNK HLSVLQAQQK SLQTLKQQVD EAKRLAQDLV VEAADSKGTS DVLLQAETLA EEHSELSQQV DEKCSFLETK LQGLGHFQNT IREMFSQFTE CDDELDGMAP VGRDAETLRK QKACMQTFLK KLEALMASND SANRTCKMML ATEETSPDLI GVKRDLEALS KQCNKLLDRA KTREEQVDGA TEKLEEFHRK LEEFSTLLQK AEEHEESQGP VGTETETINQ QLDVFKVFQK EEIEPLQVKQ QDVNWLGQGL IQSAAANTCT QGLEHDLDSV NSRWKTLNKK VAQRTSQLQE ALLHCGRFQD ALESLLSWMA DTEELVANQK PPSAEFKVVK AQIQEQKLLQ RLLEDRKSTV EVIKREGEKI AASAEPADRV KLTRQLSLLD SRWEALLSRA EARNRQLEGI SVVAQEFHET LEPLNEWLTA VEKKLANSEP IGTQAPKLEE QISQHKALQE DILLRKQSVD QALLNGLELL KQTTGDEVLI IQDKLEAIKA RYKDITKLSA DVAKTLEHAL QLAGQLQSMH KELCNWLDKV EVELLSYETQ GLKGEAASQV QERQKELKNE VRSNKALVDS LNEVSSALLE LVPWRAREGL EKTIAEDNER YRLVSDTITQ KVEEIDAAIL RSQQFEQAAD AELSWITETQ KKLMSLGDIR LEQDQTSAQL QVQKAFTMDI LRHKDIIDEL VTSGHKIMTT SSEEEKQSMK KKLDKVLKKY DAVCQINSER HLQLERAQSL VSQFWETYEE LWPWLTETQR IISQLPAPAL EYETLRRQQE EHRQLRELIA EHKPHIDKMN KTGPQLLELS PKEGIYIQEK YVAADTLYSQ IKEDVKKRAV VLDEAISQST QFHDKIDQIL ESLERIAERL RQPPSISAEV EKIKEQIGEN KSVSVDMEKL QPLYETLRQR GEEMIARSEG TEKDVSARAV QDKLDQMVFI WGSIHTLVEE REAKLLDVME LAEKFWCDHM SLVVTIKDTQ DFIRDLEDPG IDPSVVKQQQ EAAEAIREEI DGLQEELDMV ITLGSELIAA CGEPDKPIVK KSIDELNSAW DSLNKAWKDR VDRLEEAMQA AVQYQDGLQG IFDWVDIAGN KLATMSPIGT DLETVKQQIE ELKQFKSEAY QQQIEMERLN HQAELLLKKV TEEADKHTVQ DPLMELKLIW DSLDERIVSR QHKLEGALLA LGQFQHALDE LLAWLTHTKG LLSEQKPVGG DPKAIEIELA KHHVLQNDVL AHQSTVEAVN KAGNDLIESS EGEEASNLQY KLRILNQRWQ DILEKTDQRK QQLDSALRQA KGFHGEIEDL QQWLTDTERH LLASKPLGGL PETAKEQLNA HMEVCTAFAI KEETYKSLML RGQQMLARCP RSAETNIDQD ITNLKEKWES VKSKLNEKKT KLEEALHLAM NFHNSLQDFI NWLTQAEQTL NVASRPSLIL DTILFQIDEH KVFANEVNSH REQIIELDKT GTHLKYFSQK QDVVLIKNLL ISVQSRWEKV VQRLVERGRS LDEARKRAKQ FHEAWSKLME WLEESEKSLD SELEIANDPD KIKAQLVQHK EFQKSLGGKH SVYDTTNRTG RSLKEKTSLA DDNLKLDNML SELRDKWDTI CGKSVERQNK LEEALLFSGQ FTDALQALID WLYRVEPQLA EDQPVHGDID LVMNLIDNHK VFQKELGKRT SSVQALKRSA RELIEGSRDD SSWVRVQMQE LSTRWETVCA LSISKQTRLE SALQQAEEFH SVVHTLLEWL AEAEQTLRFH GALPDDEDAL RTLIEQHKEF MKRLEEKRAE LSKATGMGDA LLAVCHPDSI TTIKHWITII QARFEEVLAW AKQHQQRLAG ALAGLIAKQE LLETLLAWLQ WAETTLTEKD KEVIPQEIEE VKTLIAEHQT FMEEMTRKQP DVDKVTKTYK RRATDPPSLQ SHIPVLDKGR AGRKRFPASG FYPSGSQTQI ETKNPRVNLL VSKWQQVWLL ALERRRKLND ALDRLEELRE FANFDFDIWR KKYMRWMNHK KSRVMDFFRR IDKDQDGKIT RQEFIDGILS SKFPTSRLEM SAVADIFDRD GDGYIDYYEF VAALHPNKDA YKPITDADKI EDEVTRQVAK CKCAKRFQVE QIGDNKYRFF LGNQFGDSQQ LRLVRILRST VMVRVGGGWM ALDEFLVKND PCRVHHHGSK MLRSESNSSI TATQPTLAKG RTNMELREKF ILADGASQGM AAFRPRGRRS RPSSRGASPN RSTSASSHAC QAASPPVPAA ASTPKGTPIQ GSKLRLPGYL SGKGFHSGED SALITTAAAR VRTQFAESRK TPSRPGSRAG SKAGSRASSR RGSDASDFDI SEIQSVCSDV ETVPQTHRPV PRAGSRPSTA KPSKIPTPQR RSPASKLDKS SKR //