MACF1_MOUSE
ID MACF1_MOUSE Reviewed; 7354 AA.
AC Q9QXZ0; B1ARU3; P97394; P97395; P97396; Q4PLL5;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4 {ECO:0000305};
DE AltName: Full=Actin cross-linking family 7;
GN Name=Macf1 {ECO:0000312|MGI:MGI:108559};
GN Synonyms=Acf7, Aclp7, Kiaa0754, Macf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RX PubMed=10601340; DOI=10.1083/jcb.147.6.1275;
RA Leung C.L., Sun D., Zheng M., Knowles D.R., Liem R.K.H.;
RT "Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and
RT dystrophin that can interact with the actin and microtubule
RT cytoskeletons.";
RL J. Cell Biol. 147:1275-1286(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=16076900; DOI=10.1242/jcs.02510;
RA Lin C.-M., Chen H.-J., Leung C.L., Parry D.A.D., Liem R.K.H.;
RT "Microtubule actin crosslinking factor 1b: a novel plakin that localizes to
RT the Golgi complex.";
RL J. Cell Sci. 118:3727-3738(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-3909 (ISOFORMS 2 AND 4), AND PARTIAL
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8954775; DOI=10.1006/geno.1996.0587;
RA Bernier G., Mathieu M., De Repentigny Y., Vidal S.M., Kothary R.;
RT "Cloning and characterization of mouse ACF7, a novel member of the dystonin
RT subfamily of actin binding proteins.";
RL Genomics 38:19-29(1996).
RN [5]
RP PROTEIN SEQUENCE OF 881-888; 5824-5832 AND 6671-6678, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16815997; DOI=10.1101/gad.1411206;
RA Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt
RT signaling pathway.";
RL Genes Dev. 20:1933-1945(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3082; SER-3085; SER-7296 AND
RP SER-7299, AND 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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAPRE1; CLASP1 AND
RP CLASP2.
RX PubMed=18854161; DOI=10.1016/j.cell.2008.07.045;
RA Wu X., Kodama A., Fuchs E.;
RT "ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has
RT ATPase activity.";
RL Cell 135:137-148(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-57; SER-280;
RP SER-1376; SER-2077; SER-2081; SER-3082; SER-3085; SER-3889; SER-4458;
RP SER-4483; THR-5394; SER-5988; SER-6923; SER-7296 AND SER-7299,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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 [13]
RP FUNCTION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21295697; DOI=10.1016/j.cell.2010.12.033;
RA Wu X., Shen Q.T., Oristian D.S., Lu C.P., Zheng Q., Wang H.W., Fuchs E.;
RT "Skin stem cells orchestrate directional migration by regulating
RT microtubule-ACF7 connections through GSK3beta.";
RL Cell 144:341-352(2011).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26526844; DOI=10.1007/s12035-015-9508-4;
RA Ka M., Kim W.Y.;
RT "Microtubule-actin crosslinking factor 1 is required for dendritic
RT arborization and axon outgrowth in the developing brain.";
RL Mol. Neurobiol. 53:6018-6032(2016).
CC -!- FUNCTION: [Isoform 2]: F-actin-binding protein which plays a role in
CC cross-linking actin to other cytoskeletal proteins and also binds to
CC microtubules (PubMed:16815997, PubMed:18854161, PubMed:21295697). Plays
CC an important role in ERBB2-dependent stabilization of microtubules at
CC the cell cortex (By similarity). Acts as a positive regulator of Wnt
CC receptor signaling pathway and is involved in the translocation of
CC AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B)
CC from the cytoplasm to the cell membrane (PubMed:16815997). Has actin-
CC regulated ATPase activity and is essential for controlling focal
CC adhesions (FAs) assembly and dynamics (PubMed:18854161). Interaction
CC with CAMSAP3 at the minus ends of non-centrosomal microtubules tethers
CC microtubules minus-ends to actin filaments, regulating focal adhesion
CC size and cell migration (By similarity). May play role in delivery of
CC transport vesicles containing GPI-linked proteins from the trans-Golgi
CC network through its interaction with GOLGA4 (By similarity). Plays a
CC key role in wound healing and epidermal cell migration
CC (PubMed:21295697). Required for efficient upward migration of bulge
CC cells in response to wounding and this function is primarily rooted in
CC its ability to coordinate microtubule dynamics and polarize hair
CC follicle stem cells (PubMed:21295697). As a regulator of actin and
CC microtubule arrangement and stabilization, it plays an essential role
CC in neurite outgrowth, branching and spine formation during brain
CC development (PubMed:26526844). {ECO:0000250|UniProtKB:Q9UPN3,
CC ECO:0000269|PubMed:16815997, ECO:0000269|PubMed:18854161,
CC ECO:0000269|PubMed:21295697, ECO:0000269|PubMed:26526844}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with AXIN1, LRP6 and GOLGA4 (By
CC similarity). Found in a complex composed of MACF1, APC, AXIN1, CTNNB1
CC and GSK3B (By similarity). Interacts with MAPRE1, CLASP1 AND CLASP2
CC (PubMed:18854161). Interacts with CAMSAP3.
CC {ECO:0000250|UniProtKB:Q9UPN3, ECO:0000269|PubMed:18854161}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:18854161, ECO:0000269|PubMed:21295697}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:18854161,
CC ECO:0000269|PubMed:21295697}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UPN3}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9UPN3}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9UPN3}. Note=APC controls its localization to
CC the cell membrane which is critical for its function in microtubule
CC stabilization. Localizes to the tips of microtubules. Associated with
CC the minus-end of microtubules via interaction with CAMSAP3. The
CC phosphorylated form is found in the cytoplasm while the non-
CC phosphorylated form associates with the microtubules.
CC {ECO:0000250|UniProtKB:Q9UPN3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UPN3}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UPN3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Macf1b;
CC IsoId=Q9QXZ0-1; Sequence=Displayed;
CC Name=2; Synonyms=Macf1a;
CC IsoId=Q9QXZ0-2; Sequence=VSP_041396;
CC Name=3;
CC IsoId=Q9QXZ0-3; Sequence=VSP_041395, VSP_041396;
CC Name=4;
CC IsoId=Q9QXZ0-4; Sequence=VSP_041394, VSP_041396;
CC Name=6;
CC IsoId=Q69ZZ9-2; Sequence=External;
CC Name=7;
CC IsoId=Q69ZZ9-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Enriched in the hair follicle stem cells (at
CC protein level). Isoform 1 and isoform 2 are ubiquitous expressed, with
CC higher levels seen in lung, heart, thymus, spleen and brain.
CC {ECO:0000269|PubMed:16076900, ECO:0000269|PubMed:16815997,
CC ECO:0000269|PubMed:21295697}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is highly expressed in neuronal tissues
CC and the foregut of 8.5 dpc embryos and the head fold and primitive
CC streak of 7.5 dpc embryos (at protein level). Isoform 1: Expressed
CC throughout the development of the embryo.
CC {ECO:0000269|PubMed:16815997}.
CC -!- DOMAIN: The C-terminal tail is required for phosphorylation by GSK3B
CC and for microtubule-binding. {ECO:0000269|PubMed:21295697}.
CC -!- PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B.
CC Phosphorylation inhibits microtubule-binding and this plays a critical
CC role in bulge stem cell migration and skin wound repair. Wnt-signaling
CC can repress phosphorylation. {ECO:0000269|PubMed:21295697}.
CC -!- DISRUPTION PHENOTYPE: Mice die at the gastrulation stage and display
CC developmental retardation at 7.5 dpc with defects in the formation of
CC the primitive streak, node, and mesoderm. Conditional knockdown results
CC in markedly decreased dendritic branching of cortical and hippocampal
CC pyramidal neurons, reduced density and aberrant morphology of dendritic
CC spines, and impaired elongation of callosal axons in the brain
CC (PubMed:26526844). {ECO:0000269|PubMed:16815997,
CC ECO:0000269|PubMed:26526844}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52989.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM18553.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM20969.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF150755; AAD32244.1; -; mRNA.
DR EMBL; DQ067088; AAY78553.1; -; mRNA.
DR EMBL; AL606932; CAM18553.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL606918; CAM18553.1; JOINED; Genomic_DNA.
DR EMBL; AL606918; CAM20969.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL606932; CAM20969.1; JOINED; Genomic_DNA.
DR EMBL; U67203; AAC52988.1; -; mRNA.
DR EMBL; U67204; AAC52989.1; ALT_INIT; mRNA.
DR EMBL; U67205; AAC52990.1; -; mRNA.
DR PIR; T30847; T30847.
DR PIR; T30849; T30849.
DR PIR; T42725; T42725.
DR SMR; Q9QXZ0; -.
DR IntAct; Q9QXZ0; 18.
DR MINT; Q9QXZ0; -.
DR STRING; 10090.ENSMUSP00000119600; -.
DR iPTMnet; Q9QXZ0; -.
DR PhosphoSitePlus; Q9QXZ0; -.
DR SwissPalm; Q9QXZ0; -.
DR EPD; Q9QXZ0; -.
DR jPOST; Q9QXZ0; -.
DR MaxQB; Q9QXZ0; -.
DR PaxDb; Q9QXZ0; -.
DR PeptideAtlas; Q9QXZ0; -.
DR PRIDE; Q9QXZ0; -.
DR ProteomicsDB; 291994; -. [Q9QXZ0-1]
DR ProteomicsDB; 291995; -. [Q9QXZ0-2]
DR ProteomicsDB; 291996; -. [Q9QXZ0-3]
DR ProteomicsDB; 291997; -. [Q9QXZ0-4]
DR MGI; MGI:108559; Macf1.
DR eggNOG; KOG0516; Eukaryota.
DR InParanoid; Q9QXZ0; -.
DR ChiTaRS; Macf1; mouse.
DR PRO; PR:Q9QXZ0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXZ0; protein.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR GO; GO:0150011; P:regulation of neuron projection arborization; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 14.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.920.20; -; 1.
DR Gene3D; 3.90.1290.10; -; 5.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
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; 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; PTHR23169; 7.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00681; Plectin; 9.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 18.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00250; PLEC; 19.
DR SMART; SM00150; SPEC; 34.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 6.
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.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calcium; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Golgi apparatus; Leucine-rich repeat; Membrane; Metal-binding; Microtubule;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Wnt signaling pathway.
FT CHAIN 1..7354
FT /note="Microtubule-actin cross-linking factor 1, isoforms
FT 1/2/3/4"
FT /id="PRO_0000073451"
FT DOMAIN 78..181
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 148..171
FT /note="LRR 1"
FT DOMAIN 194..298
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 377..399
FT /note="LRR 3"
FT REPEAT 441..464
FT /note="LRR 4"
FT DOMAIN 868..925
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1050..1073
FT /note="LRR 5"
FT REPEAT 1128..1154
FT /note="LRR 6"
FT REPEAT 1187..1210
FT /note="LRR 7"
FT REPEAT 1257..1282
FT /note="LRR 8"
FT REPEAT 1577..1619
FT /note="Plectin 1"
FT REPEAT 1654..1696
FT /note="Plectin 2"
FT REPEAT 1769..1809
FT /note="Plectin 3"
FT REPEAT 1811..1848
FT /note="Plectin 4"
FT REPEAT 1855..1885
FT /note="Plectin 5"
FT REPEAT 2276..2316
FT /note="Plectin 6"
FT REPEAT 2352..2393
FT /note="Plectin 7"
FT REPEAT 2394..2425
FT /note="Plectin 8"
FT REPEAT 2487..2528
FT /note="Plectin 9"
FT REPEAT 2671..2715
FT /note="Plectin 10"
FT REPEAT 3225..3244
FT /note="LRR 9"
FT REPEAT 3606..3630
FT /note="LRR 10"
FT REPEAT 3657..3681
FT /note="LRR 11"
FT REPEAT 3845..3920
FT /note="Spectrin 1"
FT REPEAT 3898..3920
FT /note="LRR 12"
FT REPEAT 3962..4070
FT /note="Spectrin 2"
FT REPEAT 4087..4112
FT /note="LRR 13"
FT REPEAT 4223..4249
FT /note="LRR 14"
FT REPEAT 4428..4536
FT /note="Spectrin 3"
FT REPEAT 4473..4496
FT /note="LRR 15"
FT REPEAT 4563..4583
FT /note="LRR 16"
FT REPEAT 4728..4751
FT /note="LRR 17"
FT REPEAT 4759..4863
FT /note="Spectrin 4"
FT REPEAT 5010..5035
FT /note="LRR 18"
FT REPEAT 5131..5153
FT /note="LRR 19"
FT REPEAT 5195..5300
FT /note="Spectrin 5"
FT REPEAT 5240..5263
FT /note="LRR 20"
FT REPEAT 5307..5409
FT /note="Spectrin 6"
FT REPEAT 5414..5506
FT /note="Spectrin 7"
FT REPEAT 5631..5735
FT /note="Spectrin 8"
FT REPEAT 5654..5678
FT /note="LRR 21"
FT REPEAT 5742..5844
FT /note="Spectrin 9"
FT REPEAT 5763..5787
FT /note="LRR 22"
FT REPEAT 5961..6066
FT /note="Spectrin 10"
FT REPEAT 6071..6175
FT /note="Spectrin 11"
FT REPEAT 6181..6284
FT /note="Spectrin 12"
FT REPEAT 6289..6395
FT /note="Spectrin 13"
FT REPEAT 6400..6503
FT /note="Spectrin 14"
FT REPEAT 6452..6475
FT /note="LRR 23"
FT REPEAT 6508..6614
FT /note="Spectrin 15"
FT REPEAT 6621..6722
FT /note="Spectrin 16"
FT REPEAT 6726..6830
FT /note="Spectrin 17"
FT DOMAIN 7001..7036
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7037..7072
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7077..7155
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 1..295
FT /note="Actin-binding"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2120..2155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2806..2841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2951..2978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3058..3099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6904..6937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7077..7354
FT /note="C-terminal tail"
FT REGION 7171..7354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7279..7294
FT /note="4 X 4 AA tandem repeats of [GS]-S-R-[AR]"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2810..2837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3079..3094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7190..7264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7301..7354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7014
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7016
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7018
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7020
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7025
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7050
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7052
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7054
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7056
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7061
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZHV2"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3082
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 6923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 7245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 7258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 7296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 7299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..181
FT /note="MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQ
FT KKRKSQDSVLDPAERAVVRVADERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHN
FT LISLLEVLSGIKLPREKGRMRFHRLQNVQIALDFLKQRQVKLVNIRNDDITDGNPKLTL
FT GLIWTIILHFQ -> MGNSLGCVKEPKESIAVPEKAPISPKKRVRFKRKWRGKKILTPE
FT ASHREEALEGTGVIEETETLTKLTARLPKEPGVGGAEHPPSDIFLPGDSAPNSGVGDQG
FT MIVQVKESFQAEIQTAHLLLENESSVVGGAWDSLEEGMTVIAHLLDNPAERNCEKSVSQ
FT LVEFPRTASCSSRAVLLPLQGETAVEQGGTLLRHRHRSSTLPRTDYPSETVDQDQPSEG
FT WSVGGRTKSVPSAPPTGSWIAKCSVASSIPKQSGDPIHTEPTHVGLVSCKGPIMPASQS
FT DLSVSGITVSILPSSSGYGSDGLRLHGIRPEDTEPEKTSTPFSEEDGTLSLE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:8954775"
FT /id="VSP_041394"
FT VAR_SEQ 1..73
FT /note="MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQ
FT KKRKSQDSVLDPAERAVVRVA -> EKEFVQAYEDVLERYK (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041395"
FT VAR_SEQ 1543..3569
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10601340,
FT ECO:0000303|PubMed:8954775"
FT /id="VSP_041396"
FT CONFLICT 242
FT /note="D -> N (in Ref. 1; AAD32244 and 4; AAC52988/
FT AAC52989/AAC52990)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="P -> L (in Ref. 1; AAD32244, 2; AAY78553 and 4;
FT AAC52988/AAC52989)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="D -> N (in Ref. 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="C -> A (in Ref. 1; AAD32244 and 4; AAC52988/
FT AAC52989/AAC52990)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="E -> G (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 3795
FT /note="V -> A (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 3909
FT /note="Q -> H (in Ref. 4; AAC52988/AAC52989/AAC52990)"
FT /evidence="ECO:0000305"
FT CONFLICT 4735
FT /note="A -> V (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 4750
FT /note="N -> S (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 4891
FT /note="S -> F (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 5587
FT /note="A -> V (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 5603
FT /note="L -> R (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 5971
FT /note="A -> V (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT CONFLICT 6309
FT /note="N -> T (in Ref. 1; AAD32244 and 2; AAY78553)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9QXZ0-4:42
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 7354 AA; 831878 MW; 2B68195989DE15C7 CRC64;
MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS
VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS
GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF
QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGVKCTNFS SCWSDGKMFN ALIHRYRPDL
VDMERVQVQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI RQHTILMSDK SFPQNPVELK ALYNQYIHFK
ETEILAKERE KGRIKELYKL LEVWIEFGRI KLPQGYHPNH VEEEWGKLIV EMLEREKSLR
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC
EGLIRQLQVD LQILRDEKYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFSSLELVPP
STLTTTHLKA EPLNKTTHSS STSWFRKPMT RTELVSISSS EDEGNLRFVY ELLSWVEEMQ
MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYVETLGK
LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNGKE EEELACDWSD SNPNISAKKT
YFSELTMELE GKQDVFRSLQ DTAEVLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ
HVKENAAYFQ FFSDARDLES FLRNLQDSIK RKYTCDRSTS LSRLEDLLQD SMDEKEQLIQ
SKSSVASLVG RSKTIVQLKP RNPDHVLKST LSVKAICDYR QIEITICKND ECVLEDNSQR
TKWKVISPTG NEAMVPSVCF LIPPPNKEAI EMASRVEQSY QKVMALWHQL HINTKSLISW
NYLRKDLDTV QTWSLEKLRS LAPGECHQVM KNLQAHYEDF LQDSHDSALF SVADRLRIEE
EVEACKAHFQ HLMKSLENED KEETLAKVYI SELKNIRLLL EECEQRLLKQ IQSPASSKTD
RDARQDITLR IAEQEHTQED LQHLRSDLDA ISMKCNVFLQ QSPSGSSATT LRSELNLMVE
KMDHVYGLST VYLNKLKTID VIVRSMQDAE LLVKGYEIKL SQEEAVPADL SALESHRTTL
QHWLSDVKDK NSVFSVLDEE ITKAKKVAEQ LRHPASEPNL DLERYQEKGS QLQERWHRVI
AQLETRQSEV ESIQEVLRDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT
ELFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMISSSDA
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKDLLGWVST
LARNTQGTTT SSHTSASADI EKAILEQQVL AEELTTKKEQ VSEAIKTSQI FLAKHGHKLS
EGEKEQISEQ LRVLNKTYHD LCDGSANQLQ QLQSELAQQT EQKGCRAVAG VIDLGTVEIF
PIFRAMQKGL IDQDTGLVLL ESQIIMSGLI DPENSEKLSL EEGLTRNFIN LPIYQQLLGL
RDSLSLVSRL TGTLGSLSVV EAIEKKIISE RLGLKVLEVH LATGGFSLPP SENCINLEEA
FHQGFIASSL HSELQSHLRS SKNLIDPNTA EKVGLLDLMQ RCIIHQESGL KLLPVKQLAG
GMVSLKSGRK VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI
DQDMACAILI RQLQTGGIID TVTGDRMTID EAVTNNLVAA KIALVILESL WSFMGLLLPE
SGEILPITDA LEQGIVSTEL AHKILHNRQQ IEALFLPTLT EIWSWEKATE SGILDKDLVN
NLRSVCIPDM MPHIQLADSA EQSKVGFAAG KPPVSGPREE GSSHGEKLLF QLMTHSYIHA
HTGQRLLLLD QELVEMLTSR DDCQVILPEV FEIQHQRLNT SEALQELYTG TISQISSAKH
PRKPCESQFL SQNKDYPSQE NCTEAKGERS VVGIECSPAE SPERELFLKE QEAIIENVGS
LKVINKVKLK LQRPLLGSRK EEQAETLREE NISGDPLLVE CPEESEGKDL STEKSKCQTP
TKCSFTCHKE QVKTIKDIPS ETGTSLIKSQ NQMSQFQVDT SVGLRSEFKS EHDMNVNSLE
KELKEELLVK DGHKQSQEGQ SVADGQTVAL EKTDTEDNAD EPALLHSSPF EDATLSTLSA
QLQDGGIFNE ETGQKLLLNE AIAQGLVSSH TAVKLMGKLN MFRGFFDSQT CESLTTEEVI
DEGLMDEKLL YNVLMSDKAI SGILDPRTHS LCSVKEAVAA GLLDKETATR ILEGQVITGG
IVDLKRGKKL SVTLASNLGL VDTADQTELI NLEKATKGRG AEKAVKERLI ELQMETAGLM
DPESKAPLTV LQSIDRGILE REAAVYLLTK QVLDGGIIHH ISGLRLSVDN AFKHGLIGED
MARQLRKVEN FIHYQFFHPQ TKEALSFSEA IKLDLVSPDL KREIQEIQDF SGNLGDFIYG
QKLTLAKTNK EESLANKTEL PSGVMHGVID PENCTIIPYS ELVKKCRIDT ESGWRYLEVI
PFSDIKDEAG NNVLTPPEAI QLGKVDFASA LKVLEAQANT GGIIDMATGK RVTLASALEK
KLLDENMARI IASHQMLSGG IIDIYSDQRV TLNDAVEKRL ISPELAAMIQ VDPLAEQGGT
GVCELKGDFL RKELLSESSK TPRESYSKEK HEAVLQAGSL CAPEKAGIRG SNGEKAEKGR
KISVEMEGQR QDEKASSDSK VSASILSPFG FEGESSYQVS VTHPCSESCD LKPREETRSC
MKKCAVVERD KVVTQIKMVS HVKQSTSGLD AEEARERQGR MVSKEQGSHY ETAGNLLSER
SVRVDRRVRR EMGGEQSVQM SREAAVLSEE ESDQEVTIGD EPDSFVKSQS MKMIGNDKGK
EAGIEKDISV VCKIEGFPSQ MTSKDASLTN QDALPFYTEG ETKTVNLCSI LKPGEKLSQE
TASTVQKEPL SSEIPRPERL NSQESDEEPQ ISDVPHISKG DMAAQITTRQ ETTDVQDLYI
TSKSSETKDK IFPSKNYIEK LHQEIPMDPT RSHKLKEATI STLETEGISY LDSSDIKSLC
EDSKADHKSC GHQKSKVTTT QAKKSLEVVD LLVRDTEEGS SEDRVGQRGP RVLASLLPEK
LPTRTVQSEN IRQHDAVIPA ISEIREEMAL SLPCSVVKVD GKIPKEKHKE ILGDEQGPFM
AIPSGKGIEG VNPEPCRATQ NVFTRRLCLE HDEKLVSYLS LLRDIEMRTK QIQPLELNVA
ELQDLLGQAK ELDRELKDLS TVVSQELECV DRIVISQPQE VPAQLLKALE KDAKNLQKSL
DSVSDSWSSR FLHLQSAVEV KKATVLNRHK ELQGKLQDLR AWVGRASLTL NSKGCDTETD
ADSLSHTLQP YKDMKQSMAE RKSQLDALAL DIQLFISEHP QDLSLQQNQE MLQFLSELQR
SFQGLVEHTA AQKDVVQGHL QQVQQEVQVK TLQKQQDTCH KKLEDLCNWV GQAERALERH
QGGSSSGKSS LLCAEPKVDL KDLQGDIQSH STSFATAVKD IEGFLEENQT KLSPQELTAL
REKLHQAKEQ YEVLQERTRV AQKELEEAVT SALQQETEKS KAATELAENK RKIDALLDWV
GLLWGHLRES HRLAFQEWSS SLELAMEKQT LAATDGHVDV NQVPETLDRQ YELMKARHQE
LLSQQQNFIV ATQSVQSFLD QHSHNLTPEE RQKLQEKLGE LKEQYAASLA RSEAELKQTQ
ALRDELQKFL QDHKEFENWL QQSENELDSM HKGGSSPEAL NSLLKRQGSF SEDVISHKGD
LRFVTISGQK VLETENNFEE GQEPSATRNL VNEKLKDATE RYTTLHSKCI RLGSHLSMLL
GQYQQFQSSA DSLQAWVLTC EASVGKLLSD TVASDPGVLQ QQLATTKQLQ EELAEHQVPV
EKLQKAAHDL LDIEGEPALD CRPIQETTDS ISSRFQNLSC SLDERSALLQ KAIAQSQSVQ
ESMESLLQSI REVEQNLERD QVASLSSGVI QEALANNMKL KQDIARQKSS LEATHDMVTR
FMETADSNSA SVLQGKLAEL SQRFQQLQLQ QQEKESNLKK LLPQAEMFEQ LSNKLQQFME
NKSRLLASGN QPDQDIAHFS QQIQELTLAM EDQKENLDTL EHLVTTLGSC GFALDLSQHQ
DKIQNLKKDF TELQKTVQER EKDASTCQEQ LDEFRKLIRT FQKWLKETEG NVPPAKTFVS
AKELEKQIEH LKDLISDWES KGALLGEINA KGTALESLIM DITAPDSQAK TGSILPPVGS
SVGSVNGYHT CKDLTEIQCD MFDVNSKYEK LWEVLRERQE SLQTVFSRME EVQKEASSVL
QWLESKEEVL KAMDATLSPT KTETVKAQAE SNKAFLAELE QNSPKIQKVK EALAGLLKTY
PNSQEAENWK KMQEDLNSRW EKATEVTVAR QKQLEESASH LACFQAAESQ LRPWLMEKEL
MMGVLGPLSI DPNMLKQQVQ FMLKEFEARR QQHEQLNEAA QGILTGPGDM SPSASQVHKD
LQSISQKWVE LTDKLNSRSS QIDQAIVKST QYQDLLQDLS EKVKAIGQRL SGQSAISTQP
EAVKQQLEET SEIRSDLGQL DNEIKEAQTL CQELSLLIGE QYLKDELKKR LETVALPLQG
LEDLAADRMN RLQAALASTQ QFQQMFDELR TWLDEKQSQQ AKNCPISAKL ERLQCQLQEN
EEFQKNLNQH SGSYEVIVAE GEALLLSVPP GEEKKTLQNQ LVELRSHWED LSKKTANRQS
RLKDCMQKAQ KYQGHVEDLV PWIDECKSKM SELQVTLDPV QLESSLLRSK AMLNEAEKRR
SLLEILNSAA DILINSSEID EDEIRDEKAG LNQNMDAITE ELQAKTSSLE EMTQRLKEFQ
ESFKNIEKKV EGAKHQLEIF DALGSQACSN KNLEKLKAQQ EVLQALEPQV DYLRNFTQGL
VEDAPDGSDA SPLVHQAEVA QQEFLEVKQR VSSSCLTMEN KLEGIGQFHC RVREMFSQLA
DLDDELDGMG AIGRDTDSLQ SQIEDVRLFL NKIQALRFDI EDSEAECRKM LEEEGTLDLL
GLKRELEALN KQCGKLTERG KVRQEQLELT LGRVEDFYRK LKALNDAATA AEEGEALQWI
VGTEVDVINQ QLADFKLFQK DQVDPLQVKL QQVNGLGQGL IQSAGKNCDV QGLEHDMDEI
NTRWNTLNKK VAQRIAQLQE ALLHCGKFQD ALEPLLSWLT DTEELIANQK PPSAEYKVVK
AQIQEQKLLQ RLLDDRKATV DMLQAEGGRI AQSAELADRE KITGQLESLE RRWTDLLSKA
AARQKQLEDI LVLAKQFHET AEPISDFLSV TANKLANSEP VGTQTAKIHQ QIIRHKALNE
EIINRKKNVD QAIKNGQALL KQTTGEEVLL IQEKLDGIKT RYADITLTSS KALRTLEQAR
QLATKFHSTY EELTGWLREA EEELAASGGQ SPTGEQIPQF QQRQKELKKE VMEHRLVLDT
VNEVSHALLE LVPWRAREGL DKLVSDANEQ YKLISDTVGQ RVDEIDAAIQ RSQQYEQAAD
AELAWVAETK RKLMALGPIR LEQDQTTAQL QVQKAFSIDI IRHKDSMDEL FSHRGEIFST
CGEEQKAVLQ EKTECLIQQY EAVSLLNSER YARLERAQVL VNQFWETYEE LSPWAEETLA
LIAQLPPPAV DHEQLRQQQE EMRQLRESIA EHKPHIDKIL KIGPQLKELN PEEGKMVEEK
YQKAENMYAQ IKDEVRQRAL ALDEAVSQSA QFHDKIEPML ETLENLSSRL RMPPLIPAEV
DKIRECISDN KSATVELEKL QPSFEALKRR GEELIGRSQG ADKDLAAKEI QDKLDQMVFF
WEDIKARSEE REIKFLDVLE LAEKFWYDMA ALLTTIKDTQ DIVHDLESPG IDPSIIKQQV
EAAETIKEET DGLHEELEFI RILGADLIFA CGETEKPEVK KSIDEMNNAW ENLNKTWKER
LEKLEDAMQA AVQYQDTLQA MFDWLDNTVI KLCTMPPVGT DLNTVKDQLN EMKEFKVEVY
QQQIEMEKLN HQGELMLKKA TDETDRDIIR EPLTELKHLW ENLGEKIAHR QHKLEGALLA
LGQFQHALEE LMSWLTHTEE LLDAQRPISG DPKVIEVELA KHHVLKNDVL AHQATVATVN
KAGSELLESS AGDDASSLRS RLETMNQCWE SVLQKTEERE QQLQSTLQQA QGFHSEIEDF
LLELNRMENQ LSASKPTGGL PETAREQLDT HMELHSQLRA KEEIYNQLLD KGRLMLLSRG
DSGSGSKTEQ SVALLEQKWH AVSSKVEERK SKLEEALSLA TEFQNSLQEF INWLTLAEQS
LNIASPPSLI LNTVLSQIEE HKVFANEVND HRDQIIELDQ TGNQLKFLSQ KQDVVLIKNL
LVSVQSRWEK VVQRSIERGR SLDDARKRAK QFHEAWKKLI DWLEDAESHL DSELEISNDP
DKIKLQLSKH KEFQKTLGGK QPVYDTTIRT GRALKEKTLL AGDTQKLDNL LGEVRDKWDT
VCGKSVERQH KLEEALLFSG QFMDALQALV DWLYKVEPQL AEDQPVHGDL DLVMNLMDAH
KVFQKELGKR TGTVQVLKRS GRELIEGSRD DTTWVKGQLQ ELSTRWDTVC KLSVSKQSRL
EQALKQAEEF RDTVHMLLEW LSEAEQTLRF RGALPDDTEA LQSLIDTHKE FMKKVEEKRV
DVNTAVAMGE AILAVCHPDC ITTIKHWITI IRARFEEVLT WAKQHQQRLE TALSELVANA
ELLEELLAWI QWAETTLIQR DQEPIPQNID RVKALITEHQ SFMEEMTRKQ PDVDRVTKTY
KRKSVEPTHA PFMEKSRSGS RKSLNQPTPP PMPILSQSEA KNPRINQLSA RWQQVWLLAL
ERQRKLNDAL DRLEELCPEL KEFANFDFDV WRKKYMRWMN HKKSRVMDFF RRIDKDQDGK
ITRQEFIDGI LASKFPTTKL EMTAVADIFD RDGDGYIDYY EFVAALHPNK DAYRPTTDAD
KIEDEVTRQV AQCKCAKRFQ VEQIGENKYR FFLGNQFGDS QQLRLVRILR STVMVRVGGG
WMALDEFLVK NDPCRARGRT NIELREKFIL PEGASQGMTP FRSRGRRSKP SSRAASPTRS
SSSASQSNHS CTSMPSSPAT PASGTKVISS SGSKLKRPTP AFHSSRTSLA GDTSNSSSPA
STGAKANRAD PKKSASRPGS RAGSRAGSRA SSRRGSDASD FDLLETQSAC SDTSESSAAG
GQGSSRRGLT KPSKIPTMSK KTTTASPRTP GPKR
