ID   DYST_MOUSE              Reviewed;        7389 AA.
AC   Q91ZU6; Q1KP04; Q3I6J6; Q60824; Q60845; Q8K5D4; Q91ZU7; Q91ZU8;
AC   Q9WU50;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   13-NOV-2013, entry version 114.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c; 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
RT   in neurons and muscles.";
RL   J. Cell Biol. 154:691-697(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 2), PARTIAL NUCLEOTIDE
RP   SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   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   [3]
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;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-270 (ISOFORM 7), ALTERNATIVE SPLICING
RP   (ISOFORMS 1; 6 AND 7), FUNCTION OF ISOFORMS 1; 6 AND 7,
RP   PALMITOYLATION, MYRISTOYLATION, MUTAGENESIS, SUBCELLULAR LOCATION, AND
RP   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   [5]
RP   PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, AND X-RAY
RP   CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803.
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
RT   antigen1 (BPAG1) suggests that plakins are members of the spectrin
RT   superfamily.";
RL   J. Mol. Biol. 366:244-257(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6693-7389 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6870-7389 (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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND
RP   INTERACTION WITH PRPH.
RC   STRAIN=BALB/c;
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
RT   interaction partner of mouse BPAG1-n (dystonin) in neurons.";
RL   J. Cell Biol. 144:435-446(1999).
RN   [8]
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   [9]
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
RT   cell migration in stratified epithelia and neurologic degeneration.";
RL   Cell 81:233-243(1995).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), SUBCELLULAR LOCATION
RP   (ISOFORMS 5 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
RT   microfilaments to intermediate filaments.";
RL   Cell 86:655-665(1996).
RN   [11]
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   [12]
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   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14581450; DOI=10.1083/jcb.200306075;
RA   Liu J.J., Ding J., Kowal A.S., Nardine T., Allen E., Delcroix J.D.,
RA   Wu C., Mobley W., Fuchs E., Yang Y.;
RT   "BPAG1n4 is essential for retrograde axonal transport in sensory
RT   neurons.";
RL   J. Cell Biol. 163:223-229(2003).
RN   [14]
RP   ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6), HOMODIMERIZATION,
RP   MUTAGENESIS OF ARG-1385 AND ARG-1386, SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   by its N-terminus.";
RL   J. Cell Sci. 116:4543-4555(2003).
RN   [15]
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.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [16]
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   [17]
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   [18]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH PLEC,
RP   SUBCELLULAR 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.,
RA   Borradori L.;
RT   "BPAG1 isoform-b: complex distribution pattern in striated and heart
RT   muscle and association with plectin and alpha-actinin.";
RL   Exp. Cell Res. 316:297-313(2010).
RN   [19]
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
CC       networks. Required for anchoring either intermediate filaments to
CC       the actin cytoskeleton in neural and muscle cells or keratin-
CC       containing intermediate filaments to hemidesmosomes in epithelial
CC       cells. The proteins may self-aggregate to form filaments or a two-
CC       dimensional mesh. May regulate the organization and stability of
CC       the microtubule network of sensory neurons to allow axonal
CC       transport.
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.
CC       Required for the regulation of keratinocyte polarity and motility;
CC       mediates integrin ITGB4 regulation of RAC1 activity.
CC   -!- FUNCTION: Isoform 6: required for bundling actin filaments around
CC       the nucleus.
CC   -!- SUBUNIT: Homodimer. Interacts with MAPRE1; probably required for
CC       targeting to the growing microtubule plus ends. Isoform 2
CC       interacts (via N-terminus) with ACTN2. Isoform 2 interacts (via N-
CC       terminus) with PLEC (via N-terminus). Isoform 5 interacts (via N-
CC       terminus) with COL17A1 (via cytoplasmic region). Isoform 5
CC       interacts (via N-terminus) with ITGB4 isoform beta-4a (via
CC       cytoplasmic region). Isoform 5 interacts (via N-terminus) with
CC       ERBB2IP (via C-terminus). Isoform 5 associates (via C-terminal)
CC       with KRT5-KRT14 (via rod region) intermadiate filaments of
CC       keratins (By similarity). Isoform 2 and isoform 6 can homodimerize
CC       (via N-terminus). Isoform 2 interacts (via N-terminus) with PLEC
CC       (via N-terminus). Interacts with the neuronal intermediate
CC       filament protein, PRPH. Interacts with DES. Interacts with SYNE3.
CC   -!- INTERACTION:
CC       P21807:Prph (xeno); NbExp=3; IntAct=EBI-446159, EBI-446227;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       axon. Membrane. Note=Associates with axonal microtubules at the
CC       growing distal tip and intermediate filaments, but not with actin
CC       cytoskeleton, in sensory neurons (By similarity). Associates with
CC       intermediate filaments, acin and microtubule cytoskeletons.
CC       Localizes to actin stress fibers and to actin-rich ruffling at the
CC       cortex of cells.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton.
CC       Note=Colocalizes both cortical and cytoplasmic actin filaments.
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
CC       at focal contact attachments at the plasma membrane.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm, cytoskeleton. Cell
CC       junction, hemidesmosome. Note=Colocalizes with the epidermal KRT5-
CC       KRT14 intermediate filaments network of keratins. Colocalizes with
CC       ITGB4 at the leading edge of migrating keratinocytes (By
CC       similarity). Localizes to actin and intermediate filaments
CC       cytoskeletons.
CC   -!- SUBCELLULAR LOCATION: Isoform 6: Nucleus. Nucleus envelope.
CC       Membrane; Single-pass membrane protein. Endoplasmic reticulum
CC       membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton.
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
CC       cells. Translocates to the nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm, cytoskeleton.
CC       Cytoplasm, cell cortex. Cell membrane; Lipid-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC       Name=2; Synonyms=BPAG1-b, BPAG1a1, dystonin-1;
CC         IsoId=Q91ZU6-1; Sequence=Displayed;
CC       Name=1; Synonyms=BPAG1-a, BPAG1a2;
CC         IsoId=Q91ZU6-2; Sequence=VSP_041549;
CC       Name=3;
CC         IsoId=Q91ZU6-3; Sequence=VSP_041550, VSP_041551, VSP_041552;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q91ZU6-4; Sequence=VSP_041551, VSP_041552;
CC         Note=No experimental confirmation available;
CC       Name=5; Synonyms=BPAG1-e;
CC         IsoId=Q91ZU6-5; Sequence=VSP_041541, VSP_041547, VSP_041548;
CC         Note=Ref.7 (BAB93448) sequence is in conflict in positions:
CC         2325:G->D, 2416:A->T, 2530:K->Q;
CC       Name=6; Synonyms=BPAG1n, BPAG1-n1, BPAG1-n2, BPAG1a2, dystonin-2;
CC         IsoId=Q91ZU6-6; Sequence=VSP_041543, VSP_041546;
CC         Note=Incomplete sequence. Transmembrane protein (helical
CC         transmembrane domain from amino acid 18 to 38). Ref.2 (AAC52231)
CC         sequence differs from that shown due to a frameshift in position
CC         51. Ref.2 (AAC52231) sequence is in conflict in position:
CC         101:E->K. Contains a phosphoserine at position 163. Contains a
CC         phosphoserine at position 165. Contains a phosphoserine at
CC         position 167 (By similarity);
CC       Name=7; Synonyms=BPAG1a3;
CC         IsoId=Q91ZU6-8; Sequence=VSP_041542, VSP_041544, VSP_041545;
CC         Note=Incomplete sequence. Probably myristoylated on Gly-2.
CC         Probably S-palmitoylated on Cys-5 and Cys-7. Mutagenesis of
CC         Gly-2 to Ala inhibits cortical localization. Mutagenesis of
CC         Cys-5 to Ser inhibits cortical localization. Mutagenesis of
CC         Cys-7 to Ser inhibits cortical localization;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and 2 are expressed in striated and
CC       heart muscle cells. Isoform 5 is expressed in the skin. Isoform 6
CC       is expressed in sensory neural cells of the dorsal root ganglion
CC       and with low level in the skin (at protein level). Isoform 1 is
CC       expressed predominantly in the brain and spinal cord with low
CC       levels in the heart. Isoform 2 is predominantly expressed in
CC       muscle and heart and with low levels in the brain. Isoform 5 is
CC       expressed in the skin and with low levels in myoblast cells.
CC       Isoform 6 is expressed in neurons. Isoform 7 is expressed in lung
CC       and with low levels in the brain.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is the major form expressed in the
CC       dorsal root ganglia at 14.5 dpc. Isoform 2 is predominantly
CC       expressed in the myocardium, skeletal muscles, bone cartilage and
CC       epithelia of the tongue at 14.5 dpc. Isoform 5 is expressed at
CC       high levels in the epidermis and mucosal epithelia of the
CC       digestive tracts at 14.5 dpc.
CC   -!- DOMAIN: Its association with epidermal and simple keratins is
CC       dependent on the tertiary structure induced by heterodimerization
CC       of these intermedaite filaments proteins and most likely involves
CC       recognition sites located in the rod domain of these keratins.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
CC       mediates interaction with MAPRE1 and targeting to the growing
CC       microtubule plus ends (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show progressive deterioration in motor
CC       function and sensory neurodegeneration. Exhibit axonal swellings
CC       packed with disorganized intermediate filaments (IFs) and
CC       microtubules. Show poorly defined Z lines and display a reduction
CC       in sarcomere length. Have increased accumulation of vesicles and
CC       severely disrupted retrograde axonal transport. In stratified
CC       epithelia, hemidesmosomes are normal but they lack the inner plate
CC       and have no cytoskeleton attached.
CC   -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 GAR domain.
CC   -!- SIMILARITY: Contains 5 plectin repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 19 spectrin repeats.
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DR   EMBL; AF396877; AAK83382.1; -; mRNA.
DR   EMBL; AF396878; AAK83383.1; -; mRNA.
DR   EMBL; AF396879; AAK83384.1; -; mRNA.
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   IPI; IPI00131432; -.
DR   IPI; IPI00230689; -.
DR   IPI; IPI00230690; -.
DR   IPI; IPI00230692; -.
DR   IPI; IPI00284272; -.
DR   IPI; IPI00623531; -.
DR   IPI; IPI01019259; -.
DR   PIR; A60776; A60776.
DR   PIR; I49290; I49290.
DR   PIR; I49298; I49298.
DR   UniGene; Mm.336625; -.
DR   UniGene; Mm.478284; -.
DR   UniGene; Mm.487428; -.
DR   PDB; 2IAK; X-ray; 3.00 A; A=580-803.
DR   PDBsum; 2IAK; -.
DR   ProteinModelPortal; Q91ZU6; -.
DR   SMR; Q91ZU6; 31-255, 268-479, 583-1051, 1553-1927, 4476-4570, 5208-5532, 6115-6480, 7098-7170.
DR   IntAct; Q91ZU6; 5.
DR   MINT; MINT-1861530; -.
DR   STRING; 10090.ENSMUSP00000095392; -.
DR   REPRODUCTION-2DPAGE; IPI00230689; -.
DR   REPRODUCTION-2DPAGE; IPI00230690; -.
DR   REPRODUCTION-2DPAGE; IPI00284272; -.
DR   PaxDb; Q91ZU6; -.
DR   PRIDE; Q91ZU6; -.
DR   UCSC; uc007aof.1; mouse.
DR   MGI; MGI:104627; Dst.
DR   eggNOG; COG5069; -.
DR   HOVERGEN; HBG031127; -.
DR   ChEMBL; CHEMBL2176789; -.
DR   ChiTaRS; DST; mouse.
DR   EvolutionaryTrace; Q91ZU6; -.
DR   NextBio; 284082; -.
DR   PRO; PR:Q91ZU6; -.
DR   CleanEx; MM_DST; -.
DR   Genevestigator; Q91ZU6; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; 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:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0009898; C:internal side of plasma 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:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR   GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0046907; P:intracellular transport; IDA:UniProtKB.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:MGI.
DR   GO; GO:0008090; P:retrograde axon cargo transport; IMP:MGI.
DR   Gene3D; 1.10.238.10; -; 1.
DR   Gene3D; 1.10.418.10; -; 2.
DR   Gene3D; 3.30.920.20; -; 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR003108; GAS2_dom.
DR   InterPro; IPR001101; Plectin_repeat.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF02187; GAS2; 1.
DR   Pfam; PF00681; Plectin; 5.
DR   Pfam; PF00435; Spectrin; 18.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00243; GAS2; 1.
DR   SMART; SM00250; PLEC; 9.
DR   SMART; SM00150; SPEC; 32.
DR   SUPFAM; SSF143575; SSF143575; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
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; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative promoter usage;
KW   Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Coiled coil; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Endoplasmic reticulum; Intermediate filament; Lipoprotein; Membrane;
KW   Metal-binding; Microtubule; Muscle protein; Myristate; Nucleus;
KW   Palmitate; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW   Transmembrane.
FT   CHAIN         1   7389       Dystonin.
FT                                /FTId=PRO_0000078141.
FT   DOMAIN       35    252       Actin-binding.
FT   DOMAIN       35    138       CH 1.
FT   DOMAIN      151    252       CH 2.
FT   REPEAT      701    801       Spectrin 1.
FT   DOMAIN      889    941       SH3.
FT   REPEAT     1582   1624       Plectin 1.
FT   REPEAT     1657   1701       Plectin 2.
FT   REPEAT     1772   1815       Plectin 3.
FT   REPEAT     1816   1844       Plectin 4.
FT   REPEAT     1848   1889       Plectin 5.
FT   REPEAT     3845   3925       Spectrin 2.
FT   REPEAT     3997   4079       Spectrin 3.
FT   REPEAT     4440   4548       Spectrin 4.
FT   REPEAT     4552   4657       Spectrin 5.
FT   REPEAT     4775   4877       Spectrin 6.
FT   REPEAT     5208   5315       Spectrin 7.
FT   REPEAT     5322   5423       Spectrin 8.
FT   REPEAT     5430   5532       Spectrin 9.
FT   REPEAT     5647   5751       Spectrin 10.
FT   REPEAT     5758   5856       Spectrin 11.
FT   REPEAT     6002   6082       Spectrin 12.
FT   REPEAT     6089   6191       Spectrin 13.
FT   REPEAT     6197   6300       Spectrin 14.
FT   REPEAT     6308   6410       Spectrin 15.
FT   REPEAT     6415   6519       Spectrin 16.
FT   REPEAT     6523   6629       Spectrin 17.
FT   REPEAT     6636   6736       Spectrin 18.
FT   REPEAT     6741   6844       Spectrin 19.
FT   DOMAIN     7015   7050       EF-hand 1.
FT   DOMAIN     7051   7086       EF-hand 2.
FT   DOMAIN     7091   7169       GAR.
FT   CA_BIND    7028   7039       1 (Potential).
FT   CA_BIND    7064   7075       2 (Potential).
FT   MOTIF      1382   1388       Nuclear localization signal; in isoform
FT                                6.
FT   MOTIF      7369   7372       Microtubule tip localization signal.
FT   COMPBIAS   2362   2422       Asp-rich.
FT   MOD_RES    2857   2857       Phosphoserine (By similarity).
FT   MOD_RES    7250   7250       Phosphoserine (By similarity).
FT   VAR_SEQ       1    381       MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTF
FT                                TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
FT                                REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
FT                                KLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQA
FT                                TEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAV
FT                                QSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITY
FT                                VSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWI
FT                                RHHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEK
FT                                SKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAM
FT                                LEREKALRPEVE -> MRISCPFIVVPLINSCISFSNESLD
FT                                GH (in isoform 5).
FT                                /FTId=VSP_041541.
FT   VAR_SEQ       1    137       MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTF
FT                                TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
FT                                REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
FT                                KLTLGLIWTIILHF -> MGNVCGCVRAEKEEPYFDPAKSP
FT                                LSPEKYSPGRKYFRRKPCQKVVDDTEPVRQSSEREGKKGVS
FT                                QPAGGQPAVSSGELPWEDPAASPTKEDAVQLGKRAATEHGD
FT                                QKPLPSSVDGYPHRVTVSSAQGRYSEVQVSIPDKIISEEDS
FT                                PPYCPETERHLDDVNSKHRTFLRKDNVSLSQTAASSSPILC
FT                                VTEKSLKNSALMGNLSRSCHSVLEQDSDERGHPFGVHRLQL
FT                                TKRRCHSLSSGVSCVSKDAPRDDGC (in isoform 7).
FT                                /FTId=VSP_041542.
FT   VAR_SEQ       1     30       MAGYLSPAAYMYVEEQEYLQAYEDVLERYK -> MIAAAFL
FT                                VLLRPYSIQCALFLLLLLLGTVATIVFFCCWHRKLQKGRHP
FT                                MKSVFSGRSRSRDAALRSHHFRSEGFRASPRHIRRRVAAAA
FT                                AARLEEVKPVVEVHHQSEQESSGRKRRIKKNSRVQPEFYHS
FT                                VQGASTRRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASP
FT                                APGDTLPWNLPKHERSKRKIQGGSVLDPAERAVLRIA (in
FT                                isoform 6).
FT                                /FTId=VSP_041543.
FT   VAR_SEQ     271    272       VK -> KG (in isoform 7).
FT                                /FTId=VSP_041544.
FT   VAR_SEQ     273   7389       Missing (in isoform 7).
FT                                /FTId=VSP_041545.
FT   VAR_SEQ     305   7389       Missing (in isoform 6).
FT                                /FTId=VSP_041546.
FT   VAR_SEQ    1432   1432       K -> MKRSKENSEHGAYSDLLQRQRATMVENSKLTGKISE
FT                                LETMVAELKKQKSRVEEELPKVKEAAENELRKQQRNVEDIA
FT                                LQKLRAESEAKQYRRELETIVREKEAAERELERVRQLTAEA
FT                                EARRAAVEENLRNFRSQLQENTFTRQTLEDHLRRKDSSLSD
FT                                LEQQKRALVEELQRKRDHEEELLRLVKQMERDLAFQKQVAE
FT                                KQLKEKQKVELEARRKITEIQFSCRESAAVAQARPQREQGR
FT                                QKEEELKQQVDELTLANRKAEKEMRELKYELSAVQLEKASS
FT                                EEKARLLKDKLDETNNTLKCLKEDLERKDQAQERYSQQLRD
FT                                LGGQLNQTTDKAEEVRQEANDLKKIKHTYQLELESLHQEKG
FT                                KLQREVDRVTRAHALAERNIQCLNSQVHASRDEKDLSEERR
FT                                RLCQRKSDHLKEEFERSHAQLLQNIQAEKENNDKIQKLNKE
FT                                LEKSNECAETLKQKVDELTRQNNETKLMMQRIQAESKNIVR
FT                                EKQAIQQRCEVLRIQADGFKDQLRNTNEHLHKQTKTEQDFH
FT                                RKIKSLEDDLAQSQNLVSEFKQKCDQQSMIIQKTEKEVRSL
FT                                SAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHL
FT                                KTIEEQMTHRKMILLQEESDKFKRSADEFRKKMEKLMESKV
FT                                VTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQL
FT                                QCYREKMQQGPPVEANHYQKCRRLEEELLAQRREVENLKQK
FT                                MDQQIKEHEHQLLRLQCEIQKKSTTQDHTFASAFDTAGREC
FT                                HHPAEISPGNSGHLNLKTRLPLSRWTQEPHQTEGKWPHRAA
FT                                EQLPKEVQFRQPGAPLDRESSQPCYSEYFSQTSTELQITFD
FT                                DKNPITRLSELETMREQALHPSRPPVTYQDDKLERELVKLL
FT                                TPLEIAKNKQCGMHTEVTTLKQEKRLGSSAGGWMLEGCRTS
FT                                GGLKGDFLKKSVEPEASPSLDLNQACSVRDEEFQFQGLRHT
FT                                VTGRQLVEAKLLDMRTVEQLRLGLKTVEEVQRSLSKFLTKA
FT                                TSIAGLYLESSKEKMSFTSAAQKIIIDKMIALAFLEAQAAT
FT                                GFIIDPVSGQTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGY
FT                                SHASKTLSVFQAMENRMLDRKKGKHILEAQIASGGVIDPVR
FT                                GVRVPPEMAVQQGLLNNAVLQFLHEPSSNTRVFPNPNNKQA
FT                                LYYSELLQICVFDVDCQCFLLPFGEREISNLNIEKTHKIAV
FT                                VDTKTGAELTAFEAFQRNLIDKGIYLELSGQQYQWKEATFF
FT                                DSYGHPSHMLTDTKTGLQFNISEAVEQGTLDKALVQKYQEG
FT                                LTTLTELADFLLSKVVPKKDLHSPIAGYWLTASGERISLLK
FT                                ASRRNLVDRVTALRCLEAQICTGGIIDPLTGKKYRVAEALH
FT                                RGLVDEGFAQQLRQCELVITGISHPVSNKMMSVVEAVNANI
FT                                ISKEMGMRCLEFQYLTGGLIEPKVFSRLTIEEALHVGIIDV
FT                                LIATRLKDQKSYVRDIMCPQTKRKLTYKEALEKADFDFHTG
FT                                LKLLEVSEPLGTGISNLYYSSQ (in isoform 5).
FT                                /FTId=VSP_041547.
FT   VAR_SEQ    1433   7389       Missing (in isoform 5).
FT                                /FTId=VSP_041548.
FT   VAR_SEQ    1549   3557       Missing (in isoform 1).
FT                                /FTId=VSP_041549.
FT   VAR_SEQ    7125   7130       Missing (in isoform 3).
FT                                /FTId=VSP_041550.
FT   VAR_SEQ    7170   7193       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_041551.
FT   VAR_SEQ    7261   7261       K -> KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSS
FT                                AE (in isoform 3 and isoform 4).
FT                                /FTId=VSP_041552.
FT   MUTAGEN    1385   1385       R->A: Prevents isoform 6 from localizing
FT                                to the nucleus; when associated with A-
FT                                1386.
FT   MUTAGEN    1386   1386       R->A: Prevents isoform 6 from localizing
FT                                to the nucleus; when associated with A-
FT                                1385.
FT   CONFLICT   6193   6193       T -> A (in Ref. 1; AAK83383).
FT   CONFLICT   7097   7097       G -> E (in Ref. 6; BAC29753/BAC34695).
FT   CONFLICT   7241   7241       G -> A (in Ref. 6; BAC29753/BAC34695).
SQ   SEQUENCE   7389 AA;  833638 MW;  BFED827ED8A88AAD 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 HVELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR
     AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI
     HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI
     EITIYKDDEC VLANNSHRAK WKVISPTGNE AVVPSVCFTV 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
     TASVLKDVKL PDKMPDLGDL EDCKNAKRWL SFCKFQPSTV HDYRQEEGGS DGEEPVTAQS
     SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVSML LESCGAELGA DTSTRESLSV
     LTIPDAFPDC ALSEEKHECS ADKCHYSHPG HKESLENAKW DMNEAFCKMG NNDSNGELPR
     PENLADTTVV QKGSESPSRV RVPKPTSSST QPEGSVLRPE SGSILKGCKS QSEPVTKKYP
     DGTNHSHFLT SETSRPCDSN EREDEENIQK GPSVFDYSPR LSALLSHDEL RQSQGRFSDT
     STPQNTGYLC EASTLSPSDQ RVLADQSTRE KFQDRFLGIA AISVSLQGAP CGQKPVDTEC
     SSSQVHYHSE ESMSDASAES GATRQTDESE KTGSKVEDNS CTMVPGGGSR NDNTSDCGPL
     SHKGAIDAGD YETSLLAGQQ SDTATDSDSD DYFYDTPLFE DEDHDSLILQ GDDRDCLQPE
     DYDTSLQEEN DRTPPPDDIF YDVMKEKENP EFPHGGMDES LGVENKVCCP QGFPVGIEKP
     ELYLAGEKEF NSGGSEQLVE SVSESENPPG LWDSESDSLT EGEIIGRKER LGASLTPDGH
     WRGDREECDT SRESQSDTDG VGSIQSSESY RPYMSDGSDL DEEDNGGRSS EDSGDGRGGQ
     GVADEGGEPQ YQADPTQLYT AIRKEHGGET QNVSDMIPLD KTHSYSPLET QHGAGVFQPE
     SAGKGGWDTE RSSHPELTTE ADEEDEASLS THMATKGVSL SNAEGTASEE IRLVQGPDSS
     GILKAEDLEN VSPEISPSSD NIVRSEAELG GGASEDGHLS FTGSDRDQQG PGRGLVKGRD
     GQSDKLVDET SIREMGFQKE GVLMSSPEEG GEEERDLEPF PNGSATESLN MGKSQVPPLL
     THTEELSHRG APHTTTMTTT MTLEGEAKNV QTGLTESPVL LETLAEIFDT PASKVTRADL
     TSAVTASEMK SQVKEDSLTG GPEKETGPCT SLGHCDKCIH VDMLEPNEHT PSCALVAPPT
     VKDNLCSVNN AGEKSVRPQE DWPPAAEVRL SDACVEESIS EGKAGILQFT PENSDSTLSR
     LPHQSVAGWG KSADSVQARL PVSGVRHTSA DTLDVGCPQL ESSREKASAE EEPHRERALS
     LKPQEREHHM LGFVEDGRSI LKSSLDKVHM NLQEVGDPSA GTGTKISIQN LIRRAILSEL
     PNEVSNVPSH GISPISNSSE VRAESGGDPF CITSFLHLLK QNQPPQETPG ISELAKVLTQ
     MDCDPEQRGL GSELLPPQLK NAFYKLLFDG YATEKDQAEA LGQTSCAVPK MAEEKPHVCS
     DLRNKEGHHC PLNPQAVGEA EVEPFSVHIA ALPGGEKLGE LCSEPPEHSE STSGSKERSS
     DGSSKEKCSN GLQQCLQHTE KMHEYLVLLQ DMKPPLDNQA SVESSLEALK SQLKQLEAFE
     LGLAPIAVFL RKDLKLAEEF LKSFPSDLPR RHHEELSKSH QRLQNAFSSL SSVSSERMKL
     IKLAINSEMS KLAVRHEDFL HKLTSYSDWV SEKSRSVKAI QTVNVQDTEL VKNSVKFLKN
     VLADLSHTKM QLETTAFDVQ SFISDYAQDL SPSQSRQLLR LLNTTQKGFL DLQELVTTEA
     DRLEALLQLE QELGHQKVVA ERQQEYREKL QGLCDLLTQT ENRLISNQEA FVIGDGTVEL
     QKYQSKQEEL QRDMQGSTQA MEEIVRNTEL FLKESGDELS QADRALIEQK LNEVKMKCAQ
     LNLKAEQSRK ELDKAVTTAL KEETEKVAAV RQLEESKTKI ENLLNWLSNV EEDSEGVWTK
     HTQPMEQNGT YLHEGDSKLG AGEEDEVNGN LLETDAEGHS EATKGNLNQQ YEKVKAQHGK
     IMAQHQAVLL ATQSAQVLLE KQGHYLSPEE KEKLQKNTQE LKVHYEKVLA ECEKKVKLTH
     SLQEELEKFD TDYSEFEHWL QQSEQELANL EAGADDLSGL MDKLTRQKSF SEDVISHKGD
     LRYITISGNR VIDAAKSCSK RDSDRIGKDS VETSATHREV QTKLDQVTDR FRSLYSKCSV
     LGNNLKDLVD QYQQYEDASC GLLSGLQACE AKASKHLREP IALDPKNLQR QLEETKALQG
     QISSQQVAVE KLKKTAEVLL DAKGSLLPAK NDIQKTLDDI VGRYDDLSKC VNERNEKLQI
     TLTRSLSVQD ALDEMLDWMG SVESSLVKPG QVPLNSTALQ DLISKDTMLE QDITGRQSSI
     NAMNEKVKTF IETTDPSTAS SLQAKMKDLS ARFSEASQKH KEKLAKMVEL KAKVEQFEKL
     SDKLQTFLET QSQALTEVAM PGKDVPELSQ HMQESTAKFL EHRKDLEALH SLLKEISSHG
     LPGDKALVFE KTNNLSRKFK EMEDTIQEKK DALSSCQEQL SAFQTLAQSL KTWIKETTKQ
     VPVVKPSLGT EDLRKSLEET KKLQEKWNLK APEIHKASNS GVSLCNLLSA LISPAKAIAA
     AKSGGVILNG EGTDTNTQDF LANKGLTSIK KDMTDISHSY EDLGLLLKDK IVELNTKLSK
     LQKAQEESSA MMQWLEKMNK TASRWRQTPT PADTESVKLQ VEQNKSFEAE LKQNVNKVQE
     LKDKLSELLE ENPEAPEAQS WKQALAEMDT KWQELNQLTM DRQQKLEESS NNLTQFQTTE
     AQLKQWLMEK ELMVSVLGPL SIDPNMLNTQ KQQVQILLQE FDTRKPQYEQ LTAAGQGILS
     RPGEDPSLHG IVNEQLEAVT QKWDNLTGQL RDRCDWIDQA IVKSTQYQSL LRSLSGTLTE
     LDDKLSSGLT SGALPDAVNQ QLEAAQRLKQ EIEQQAPKIK EAQEVCEDLS ALVKEEYLKA
     ELSRQLEGIL KSFKDIEQKT ENHVQHLQSA CASSHQFQQM SKDFQAWLDA KKEEQRDSPP
     ISAKLDVLES LLNSQKDFGK TFTEQSNIYE KTISEGENLL LKTQGAEKAA LQLQLNTMKT
     DWDRFRKQVK EREEKLKDSL EKALKYREQV ETLRPWIDRC QHSLDGVTFS LDPTESESSI
     AELKSLQKEM DHHFGMLELL NNTANSLLSV CEVDKEAVTE ENQSLMEKVN RVTEQLQSKT
     VSLENMAQKF KEFQEVSRDT QRQLQDTKEQ LEVHHSLGPQ AYSNKHLSVL QAQQKSLQTL
     KQQVDEAKRL AQDLVVEAAD SKGTSDVLLQ AETLAEEHSE LSQQVDEKCS FLETKLQGLG
     HFQNTIREMF SQFTECDDEL DGMAPVGRDA ETLRKQKACM QTFLKKLEAL MASNDSANRT
     CKMMLATEET SPDLIGVKRD LEALSKQCNK LLDRAKTREE QVDGATEKLE EFHRKLEEFS
     TLLQKAEEHE ESQGPVGTET ETINQQLDVF KVFQKEEIEP LQVKQQDVNW LGQGLIQSAA
     ANTCTQGLEH DLDSVNSRWK TLNKKVAQRT SQLQEALLHC GRFQDALESL LSWMADTEEL
     VANQKPPSAE FKVVKAQIQE QKLLQRLLED RKSTVEVIKR EGEKIAASAE PADRVKLTRQ
     LSLLDSRWEA LLSRAEARNR QLEGISVVAQ EFHGTLEPLN EWLTAVEKKL ANSEPIGTQA
     PKLEEQISQH KALQEDILLR KQSVDQALLN GLELLKQTTG DEVLIIQDKL EAIKARYKDI
     TKLSADVAKT LEHALQLAGQ LQSMHKELCN WLDKVEVELL SYETQGLKGE AASQVQERQK
     ELKNEVRSNK ALVDSLNEVS SALLELVPCR AKEGLEKTIA DDNEPLPDCE PTQSRHKVEE
     IDAAILRSQQ FEQAADAELS WITETQKKLM SLGDIRLEQD QTSAQLQVQK AFTMDILRHK
     DIIDELVTSG HKIMTTSGEE EKQSMKKKLD KVLKKYDAVC QINSERHLQL ERAQSLVSQF
     WETYEELWPW LTETQRIISQ LPAPALEYET FERQQEEHRQ LRELIAEHKP HIDKMNKTGP
     QLLELSPKEG IYIQEKYVAA DTLYSQIKED VKKRAVVLDE AISQSTQFHD KIDQILESLE
     RIAERLRQPP SISAEVEKIK EQIGENKSVS VDMEKLQPLY ETLRQRGEEM IARSEGTEKD
     VSARAVQDKL DQMVFIWGSI HTLVEEREAK LLDVMELAEK FWCDHMSLVV TIKDTQDFIR
     DLEDPGIDPS VVKQQQEAAE AIREEIDGLQ EELDMVITLG SELIAACGEP DKPIVKKSID
     ELNSAWDSLN KAWKDRVDRL EEAMQAAVQY QDGLQGIFDW VDIAGDKLAT MSPIGTDLET
     VKQQIEELKQ FKSEAYQQQM EMERLNHQAE LLLKKVTEEA DKHTVQDPLM ELKLIWDSLD
     ERIVSRQHKL EGTLLALGQF QHALDELLAW LTHTKGLLSE QKPVGGDPKA IEIELAKHHV
     LQNDVLAHQS TVEAVNKAGN DLIESSEGEE ASNLQYKLRI LNQRWQDILE KTDQRKQQLD
     SALRQAKGFH GEIEDLQQWL TDTERHLLAS KPLGGLPETA KEQLNAHMEV CTAFAIKEET
     YKSLMLRGQQ MLARCPRSAE TNIDQDITNL KEKWESVKSK LNEKKTKLEE ALHLAMNFHN
     SLQDFINWLT QAEQTLNVAS RPSLILDTIL FQIDEHKVFA NEVNSHREQI IELDKTGTHL
     KYFSQKQDVV LIKNLLISVQ SRWEKVVQRL VERGRSLDEA RKRAKQFHEA WSKLMEWLEE
     SEKSLDSELE IANDPDKIKA QLVQHKEFQK SLGGKHSVYD TTNRTGRSLK EKTSLADDNL
     KLDNMLSELR DKWDTICGKS VERQNKLEEA LLFSGQFTDA LQALIDWLYR VEPQLAEDQP
     VHGDIDLVMS LIDNHKVFQK ELGKRTSSVQ ALKRSARELI EGSRDDSSWV RVQMQELSTR
     WETVCALSIS KQTRLESALQ QAEEFHSVVH TLLEWLAEAE QTLRFHGALP DDEDALRTLI
     EQHKEFMKRL EEKRAELSKA TGMGDALLAV CHPDSITTIK HWITIIQARF EEVLAWAKQH
     QQRLAGALAG LIAKQELLET LLAWLQWAET TLTEKDKEVI PQEIEEVKTL IAEHQTFMEE
     MTRKQPDVDK VTKTYKRRAT DPPSLQSHIP VLDKGRAGRK RFPASGFYPS GSQTQIETKN
     PRVNLLVSKW QQVWLLALER RRKLNDALDR LEELREFANF DFDIWRKKYM RWMNHKKSRV
     MDFFRRIDKD QDGKITRQEF IDGILSSKFP TSRLEMSAVA DIFDRDGDGY IDYYEFVAAL
     HPNKDAYKPI TDADKIGDEV TRQVAKCKCA KRFQVEQIGD NKYRFFLGNQ FGDSQQLRLV
     RILRSTVMVR VGGGWMALDE FLVKNDPCRV HHHGSKMLRS ESNSSITATQ PTLAKGRTNM
     ELREKFILAD GASQGMAAFR PRGRRSRPSS RGASPNRSTS GSSHACQAAS PPVPAAASTP
     KGTPIQGSKL RLPGYLSGKG FHSGEDSALI TTAAARVRTQ FAESRKTPSR PGSRAGSKAG
     SRASSRRGSD ASDFDISEIQ SVCSDVETVP QTHRPVPRAG SRPSTAKPSK IPTPQRRSPA
     SKLDKSSKR
//
