UNC89_CAEEL
ID UNC89_CAEEL Reviewed; 8081 AA.
AC O01761; Q17362; Q5W614; Q5W615; Q5W616; Q5W617; Q646H5; Q64EQ8; Q7Z119;
AC Q7Z120;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Muscle M-line assembly protein unc-89;
DE AltName: Full=Inactive serine/threonine-protein kinase unc-89 {ECO:0000305};
DE AltName: Full=Obscurin {ECO:0000305};
DE AltName: Full=Uncoordinated protein 89;
GN Name=unc-89; ORFNames=C09D1.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=8603916; DOI=10.1083/jcb.132.5.835;
RA Benian G.M., Tinley T.L., Tang X., Borodovsky M.;
RT "The Caenorhabditis elegans gene unc-89, required for muscle M-line
RT assembly, encodes a giant modular protein composed of Ig and signal
RT transduction domains.";
RL J. Cell Biol. 132:835-848(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5922-7990 (ISOFORMS B/F), ALTERNATIVE
RP SPLICING, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=15313609; DOI=10.1016/j.jmb.2004.07.006;
RA Small T.M., Gernert K.M., Flaherty D.B., Mercer K.B., Borodovsky M.,
RA Benian G.M.;
RT "Three new isoforms of Caenorhabditis elegans UNC-89 containing MLCK-like
RT protein kinase domains.";
RL J. Mol. Biol. 342:91-108(2004).
RN [4]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=16453163; DOI=10.1007/s10974-005-9027-4;
RA Ferrara T.M., Flaherty D.B., Benian G.M.;
RT "Titin/connectin-related proteins in C. elegans: a review and new
RT findings.";
RL J. Muscle Res. Cell Motil. 26:435-447(2005).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17326220; DOI=10.1002/dvdy.21091;
RA Ono K., Yu R., Ono S.;
RT "Structural components of the nonstriated contractile apparatuses in the
RT Caenorhabditis elegans gonadal myoepithelial sheath and their essential
RT roles for ovulation.";
RL Dev. Dyn. 236:1093-1105(2007).
RN [6]
RP FUNCTION, INTERACTION WITH RHO-1; CED-10; MIG-2 AND CDC-42, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18801371; DOI=10.1016/j.jmb.2008.08.083;
RA Qadota H., Blangy A., Xiong G., Benian G.M.;
RT "The DH-PH region of the giant protein UNC-89 activates RHO-1 GTPase in
RT Caenorhabditis elegans body wall muscle.";
RL J. Mol. Biol. 383:747-752(2008).
RN [7]
RP INTERACTION WITH SCPL-1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18337465; DOI=10.1091/mbc.e08-01-0053;
RA Qadota H., McGaha L.A., Mercer K.B., Stark T.J., Ferrara T.M., Benian G.M.;
RT "A novel protein phosphatase is a binding partner for the protein kinase
RT domains of UNC-89 (Obscurin) in Caenorhabditis elegans.";
RL Mol. Biol. Cell 19:2424-2432(2008).
RN [8]
RP INTERACTION WITH LIM-9, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19244614; DOI=10.1016/j.jmb.2009.01.016;
RA Xiong G., Qadota H., Mercer K.B., McGaha L.A., Oberhauser A.F.,
RA Benian G.M.;
RT "A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein
RT kinase regions of UNC-89 (obscurin) in Caenorhabditis elegans muscle.";
RL J. Mol. Biol. 386:976-988(2009).
RN [9]
RP FUNCTION.
RX PubMed=21868609; DOI=10.1534/genetics.111.132449;
RA Raharjo W.H., Ghai V., Dineen A., Bastiani M., Gaudet J.;
RT "Cell architecture: surrounding muscle cells shape gland cell morphology in
RT the Caenorhabditis elegans pharynx.";
RL Genetics 189:885-897(2011).
RN [10]
RP FUNCTION, INTERACTION WITH MEL-26, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22621901; DOI=10.1091/mbc.e12-01-0055;
RA Wilson K.J., Qadota H., Mains P.E., Benian G.M.;
RT "UNC-89 (obscurin) binds to MEL-26, a BTB-domain protein, and affects the
RT function of MEI-1 (katanin) in striated muscle of Caenorhabditis elegans.";
RL Mol. Biol. Cell 23:2623-2634(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22768340; DOI=10.1371/journal.pone.0040182;
RA Spooner P.M., Bonner J., Maricq A.V., Benian G.M., Norman K.R.;
RT "Large isoforms of UNC-89 (obscurin) are required for muscle cell
RT architecture and optimal calcium release in Caenorhabditis elegans.";
RL PLoS ONE 7:E40182-E40182(2012).
RN [12]
RP FUNCTION, INTERACTION WITH CPNA-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA Benian G.M.;
RT "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT is required for myofilament stability in Caenorhabditis elegans.";
RL Mol. Biol. Cell 24:601-616(2013).
RN [13]
RP FUNCTION, INTERACTION WITH UNC-15, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=27009202; DOI=10.1091/mbc.e15-09-0675;
RA Qadota H., Mayans O., Matsunaga Y., McMurry J.L., Wilson K.J., Kwon G.E.,
RA Stanford R., Deehan K., Tinley T.L., Ngwa V.M., Benian G.M.;
RT "The SH3 domain of UNC-89 (obscurin) interacts with paramyosin, a coiled-
RT coil protein, in Caenorhabditis elegans muscle.";
RL Mol. Biol. Cell 27:1606-1620(2016).
RN [14]
RP STRUCTURE BY NMR OF 341-458, AND DOMAIN.
RX PubMed=11080629; DOI=10.1016/s0969-2126(00)00509-8;
RA Blomberg N., Baraldi E., Sattler M., Saraste M., Nilges M.;
RT "Structure of a PH domain from the C. elegans muscle protein UNC-89
RT suggests a novel function.";
RL Structure 8:1079-1087(2000).
CC -!- FUNCTION: Structural component of the muscle M line which is involved
CC in assembly and organization of sarcomere myofilaments
CC (PubMed:15313609, PubMed:16453163, PubMed:18801371, PubMed:22621901,
CC PubMed:23283987, PubMed:27009202). The large isoform a, isoform b,
CC isoform d and isoform f play an essential role in maintaining the
CC organization of sarcomeres but not myofilament alignment during body
CC wall muscle development whereas the small isoform c and isoform d
CC appear to have a minor role (PubMed:15313609, PubMed:16453163,
CC PubMed:22768340). Isoform b and isoform f are required for the
CC organization of unc-15/paramyosin into sarcomere thick filaments in
CC body wall muscles (PubMed:27009202). By binding mel-26, a substrate
CC adapter of the cul-3 E3 ubiquitin-protein ligase complex, regulates the
CC organization of myosin thick filaments, likely by preventing the
CC degradation of microtubule severing protein mei-1 (PubMed:22621901).
CC Acts as guanine nucleotide exchange factor (GEF) for Rho GTPase rho-1
CC but not ced-10, mig-2 and cdc-42 (PubMed:18801371). The large isoforms
CC regulate Ca(2+) signaling during muscle contraction by ensuring the
CC correct localization of sarco-endoplamic reticulum Ca(2+) ATPase sca-1
CC and ryanodine receptor unc-68 (PubMed:22768340). By controlling the
CC contraction and/or organization of pharyngeal muscles, plays a role in
CC the formation of pharyngeal gland cell extension (PubMed:21868609).
CC {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:16453163,
CC ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:21868609,
CC ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:22768340,
CC ECO:0000269|PubMed:23283987, ECO:0000269|PubMed:27009202,
CC ECO:0000269|PubMed:8603916}.
CC -!- SUBUNIT: May interact (via fibronectin type-III domain 1, Ig-like C2-
CC type domain 48/49 and protein kinase domain 1 or C-terminus of the
CC interkinase region) with lim-9 (via LIM zinc-binding domain)
CC (PubMed:19244614). May interact (via fibronectin type-III domain 1, Ig-
CC like C2-type domain 48/49 and kinase protein domain 1 or Ig-like C2-
CC type domain 50, fibronectin type-III domain 2 and kinase protein domain
CC 2) with scpl-1 isoforms a and b (via FCP1 homology domain); the
CC interaction may act as a molecular bridge to bring two unc-89 molecules
CC together or to stabilize a loop between the 2 kinase domains
CC (PubMed:18337465, PubMed:19244614). May interact (via SH3 domain) with
CC unc-15 (PubMed:27009202). May interact (via Ig-like C2-type domain 1-3)
CC with cpna-1 (via VWFA domain) (PubMed:23283987). May interact (via Ig-
CC like C2-type domain 2/3 and, Ig-like C2-type domain 50 and fibronectin
CC type-III domain 2) with mel-26 (via MATH domain) (PubMed:22621901). May
CC interact (via DH and PH domains) with rho-1, ced-10, mig-2 and cdc-42
CC (PubMed:18801371). {ECO:0000269|PubMed:18337465,
CC ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:19244614,
CC ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:23283987,
CC ECO:0000269|PubMed:27009202}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:18337465,
CC ECO:0000269|PubMed:19244614, ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:23283987,
CC ECO:0000269|PubMed:27009202, ECO:0000269|PubMed:8603916}.
CC Note=Colocalizes with scpl-1 (isoform b) to the M line
CC (PubMed:19244614). Colocalizes with cpna-1 to the M line
CC (PubMed:23283987). Colocalizes with mel-26 to the M line
CC (PubMed:22621901). Accumulates at the center of thick myofilaments in M
CC line-like structures in myoepithelial sheath cells (PubMed:17326220).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:19244614,
CC ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:23283987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=b;
CC IsoId=O01761-1; Sequence=Displayed;
CC Name=a;
CC IsoId=O01761-2; Sequence=VSP_015545;
CC Name=c;
CC IsoId=O01761-3; Sequence=VSP_015541, VSP_015547;
CC Name=d;
CC IsoId=O01761-4; Sequence=VSP_015542, VSP_015546;
CC Name=e;
CC IsoId=O01761-5; Sequence=VSP_015543, VSP_015545;
CC Name=f;
CC IsoId=O01761-6; Sequence=VSP_015543;
CC Name=g;
CC IsoId=O01761-7; Sequence=VSP_015544, VSP_015548, VSP_015549;
CC -!- TISSUE SPECIFICITY: Expressed in body-wall, pharyngeal muscles and a
CC few muscle cells of the tail (at protein level) (PubMed:8603916,
CC PubMed:18337465, PubMed:19244614, PubMed:22621901, PubMed:22768340,
CC PubMed:23283987, PubMed:27009202). Expressed in gonadal myoepithelial
CC sheath cells (at protein level) (PubMed:17326220). Isoform c: Expressed
CC in body wall and vulval muscles but not in pharyngeal muscles
CC (PubMed:15313609). Isoform d: Specifically expressed in vulval,
CC intestinal, anal depressor and anal sphincter muscles
CC (PubMed:15313609). {ECO:0000269|PubMed:15313609,
CC ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:18337465,
CC ECO:0000269|PubMed:19244614, ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:23283987,
CC ECO:0000269|PubMed:27009202, ECO:0000269|PubMed:8603916}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (PubMed:23283987). Isoform a:
CC Expressed in embryo, throughout larval development and in adults
CC (PubMed:15313609). Isoform b: Expressed in embryo, throughout larval
CC development and in adults and is one of the most abundant
CC (PubMed:15313609). Isoform c: Expressed in embryo, throughout larval
CC development and in adults and is one of the most abundant
CC (PubMed:15313609). Isoform d: Expressed in embryo, throughout larval
CC development and in adults (PubMed:15313609).
CC {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:23283987}.
CC -!- DOMAIN: Protein kinase domains 1 and 2 are predicted to be
CC catalytically inactive (PubMed:16453163). The two kinase domains are
CC required for the organization of thick filament component myosin heavy
CC chain myo-3 but not of myosin heavy chain unc-54 and unc-15/paramyosin
CC (PubMed:27009202). {ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:27009202, ECO:0000303|PubMed:16453163}.
CC -!- DOMAIN: The SH3 domain is required for the organization of thick
CC filament components myosin heavy chain unc-54 and myo-3 and unc-
CC 15/paramyosin. {ECO:0000269|PubMed:27009202}.
CC -!- DOMAIN: The PH domain does not bind inositol 1,4,5-trisphosphate. The
CC PH domain has an unusual closed conformation of the lipid binding site
CC which is lined by negative charged amino acids which probably prevents
CC binding to membrane lipids. {ECO:0000269|PubMed:11080629}.
CC -!- DISRUPTION PHENOTYPE: Mutants lacking isoform a, isoform b, isoform e
CC and isoform f have an abnormal organization of the myofilament lattice
CC of body wall and pharyngeal muscles (PubMed:16453163, PubMed:18801371,
CC PubMed:22621901, PubMed:27009202). In body wall muscles, unc-
CC 15/paramyosin accumulates in large foci outside thick filaments and
CC myosin heavy chains unc-54 and myo-3 fail to assemble into parallel
CC myofibrils (PubMed:27009202). In addition, myosin thick filaments are
CC disorganized with the formation of abnormal myosin heavy chain myo-3
CC aggregates and V-shaped crossing of A bands (PubMed:18801371,
CC PubMed:22621901). In mutants lacking isoform b, isoform c, isoform d
CC and isoform f, myo-3 fails to assemble into parallel myofibrils whereas
CC unc-54 and unc-15 localization is normal (PubMed:27009202). Mutants
CC lacking isoform b, isoform c, isoform d and isoform f have defects only
CC in body wall muscle structure (PubMed:16453163). RNAi-mediated
CC knockdown of isoform a or isoform b, isoform c and isoform d causes
CC similar defects in the organization although RNAi-mediated knockdown of
CC isoform c causes a less severe defect in myofilament organization
CC (PubMed:15313609). In mutants lacking isoform a, isoform b, isoform e
CC and isoform f, mei-1 protein levels are decreased by 20 percent
CC (PubMed:22621901). RNAi-mediated knockdown of isoform a, isoform b,
CC isoform e and isoform f but not of isoforms c and d disrupts sca-1
CC localization to linear punctate structures along in the M line in body
CC wall muscles (PubMed:22768340). RNAi-mediated knockdown has no effect
CC on ovulation (PubMed:17326220). {ECO:0000269|PubMed:15313609,
CC ECO:0000269|PubMed:16453163, ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:18801371, ECO:0000269|PubMed:22621901,
CC ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:27009202}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: In contrast to obscurins in other species, unlikely to have
CC serine/threonine kinase activity as both protein kinase domains are
CC predicted to be catalytically inactive. The Lys residue involved in ATP
CC binding is not conserved in both kinase domains. {ECO:0000305,
CC ECO:0000305|PubMed:16453163}.
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DR EMBL; U33058; AAB00542.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63864.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63865.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63866.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63867.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63868.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63869.1; -; Genomic_DNA.
DR EMBL; FO080458; CCD63870.1; -; Genomic_DNA.
DR EMBL; AY724774; AAU21474.1; -; mRNA.
DR EMBL; AY714779; AAU14146.1; -; mRNA.
DR PIR; T29757; T29757.
DR RefSeq; NP_001020984.1; NM_001025813.1. [O01761-2]
DR RefSeq; NP_001020985.1; NM_001025814.2. [O01761-1]
DR RefSeq; NP_001020988.1; NM_001025817.2. [O01761-5]
DR RefSeq; NP_001020989.1; NM_001025818.1. [O01761-6]
DR RefSeq; NP_001020990.1; NM_001025819.1.
DR RefSeq; NP_001293453.1; NM_001306524.1. [O01761-3]
DR RefSeq; NP_001293454.1; NM_001306525.1. [O01761-4]
DR PDB; 1FHO; NMR; -; A=341-458.
DR PDBsum; 1FHO; -.
DR BMRB; O01761; -.
DR SMR; O01761; -.
DR BioGRID; 37462; 40.
DR IntAct; O01761; 11.
DR STRING; 6239.C09D1.1b; -.
DR iPTMnet; O01761; -.
DR EPD; O01761; -.
DR PaxDb; O01761; -.
DR PeptideAtlas; O01761; -.
DR PRIDE; O01761; -.
DR EnsemblMetazoa; C09D1.1a.1; C09D1.1a.1; WBGene00006820. [O01761-2]
DR EnsemblMetazoa; C09D1.1b.1; C09D1.1b.1; WBGene00006820. [O01761-1]
DR EnsemblMetazoa; C09D1.1c.1; C09D1.1c.1; WBGene00006820. [O01761-3]
DR EnsemblMetazoa; C09D1.1d.1; C09D1.1d.1; WBGene00006820. [O01761-4]
DR EnsemblMetazoa; C09D1.1e.1; C09D1.1e.1; WBGene00006820. [O01761-5]
DR EnsemblMetazoa; C09D1.1f.1; C09D1.1f.1; WBGene00006820. [O01761-6]
DR EnsemblMetazoa; C09D1.1g.1; C09D1.1g.1; WBGene00006820.
DR GeneID; 171990; -.
DR KEGG; cel:CELE_C09D1.1; -.
DR UCSC; C09D1.1g; c. elegans. [O01761-1]
DR CTD; 3346201; -.
DR WormBase; C09D1.1a; CE30426; WBGene00006820; unc-89. [O01761-2]
DR WormBase; C09D1.1b; CE34251; WBGene00006820; unc-89. [O01761-1]
DR WormBase; C09D1.1c; CE34252; WBGene00006820; unc-89. [O01761-3]
DR WormBase; C09D1.1d; CE37701; WBGene00006820; unc-89. [O01761-4]
DR WormBase; C09D1.1e; CE37702; WBGene00006820; unc-89. [O01761-5]
DR WormBase; C09D1.1f; CE37703; WBGene00006820; unc-89. [O01761-6]
DR WormBase; C09D1.1g; CE52389; WBGene00006820; unc-89. [O01761-7]
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG0689; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000171516; -.
DR InParanoid; O01761; -.
DR OMA; MIEIRNP; -.
DR OrthoDB; 184at2759; -.
DR PhylomeDB; O01761; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-432142; Platelet sensitization by LDL.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; O01761; -.
DR PRO; PR:O01761; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006820; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O01761; baseline and differential.
DR GO; GO:0031672; C:A band; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:WormBase.
DR GO; GO:0090736; F:MATH domain binding; IPI:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0031034; P:myosin filament assembly; IMP:WormBase.
DR GO; GO:1905905; P:pharyngeal gland morphogenesis; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IGI:UniProtKB.
DR GO; GO:1905552; P:positive regulation of protein localization to endoplasmic reticulum; IGI:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IGI:UniProtKB.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IGI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0014722; P:regulation of skeletal muscle contraction by calcium ion signaling; IGI:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IGI:UniProtKB.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:WormBase.
DR GO; GO:0071688; P:striated muscle myosin thick filament assembly; IMP:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.10; -; 55.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR007850; RCSD.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 51.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF05177; RCSD; 6.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 51.
DR SMART; SM00408; IGc2; 45.
DR SMART; SM00406; IGv; 5.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48726; SSF48726; 53.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 50.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disulfide bond;
KW Immunoglobulin domain; Muscle protein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..8081
FT /note="Muscle M-line assembly protein unc-89"
FT /id="PRO_0000072704"
FT DOMAIN 63..127
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 152..330
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 342..498
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 547..633
FT /note="Ig-like C2-type 1"
FT DOMAIN 648..736
FT /note="Ig-like C2-type 2"
FT DOMAIN 748..838
FT /note="Ig-like C2-type 3"
FT DOMAIN 946..1033
FT /note="Ig-like C2-type 4"
FT DOMAIN 1044..1132
FT /note="Ig-like C2-type 5"
FT DOMAIN 1140..1227
FT /note="Ig-like C2-type 6"
FT DOMAIN 1375..1475
FT /note="RCSD 1"
FT /evidence="ECO:0000305"
FT DOMAIN 1479..1585
FT /note="RCSD 2"
FT /evidence="ECO:0000305"
FT DOMAIN 1597..1695
FT /note="RCSD 3"
FT /evidence="ECO:0000305"
FT DOMAIN 1700..1799
FT /note="RCSD 4"
FT /evidence="ECO:0000305"
FT DOMAIN 1982..2067
FT /note="Ig-like C2-type 7"
FT DOMAIN 2071..2163
FT /note="Ig-like C2-type 8"
FT DOMAIN 2171..2261
FT /note="Ig-like C2-type 9"
FT DOMAIN 2269..2359
FT /note="Ig-like C2-type 10"
FT DOMAIN 2367..2455
FT /note="Ig-like C2-type 11"
FT DOMAIN 2463..2564
FT /note="Ig-like C2-type 12"
FT DOMAIN 2563..2651
FT /note="Ig-like C2-type 13"
FT DOMAIN 2657..2746
FT /note="Ig-like C2-type 14"
FT DOMAIN 2754..2858
FT /note="Ig-like C2-type 15"
FT DOMAIN 2887..2980
FT /note="Ig-like C2-type 16"
FT DOMAIN 2994..3081
FT /note="Ig-like C2-type 17"
FT DOMAIN 3087..3183
FT /note="Ig-like C2-type 18"
FT DOMAIN 3189..3280
FT /note="Ig-like C2-type 19"
FT DOMAIN 3286..3376
FT /note="Ig-like C2-type 20"
FT DOMAIN 3384..3469
FT /note="Ig-like C2-type 21"
FT DOMAIN 3482..3572
FT /note="Ig-like C2-type 22"
FT DOMAIN 3580..3667
FT /note="Ig-like C2-type 23"
FT DOMAIN 3686..3777
FT /note="Ig-like C2-type 24"
FT DOMAIN 3817..3908
FT /note="Ig-like C2-type 25"
FT DOMAIN 3920..4009
FT /note="Ig-like C2-type 26"
FT DOMAIN 4018..4106
FT /note="Ig-like C2-type 27"
FT DOMAIN 4109..4201
FT /note="Ig-like C2-type 28"
FT DOMAIN 4212..4297
FT /note="Ig-like C2-type 29"
FT DOMAIN 4302..4387
FT /note="Ig-like C2-type 30"
FT DOMAIN 4400..4485
FT /note="Ig-like C2-type 31"
FT DOMAIN 4489..4580
FT /note="Ig-like C2-type 32"
FT DOMAIN 4588..4678
FT /note="Ig-like C2-type 33"
FT DOMAIN 4681..4771
FT /note="Ig-like C2-type 34"
FT DOMAIN 4873..4961
FT /note="Ig-like C2-type 35"
FT DOMAIN 4965..5057
FT /note="Ig-like C2-type 36"
FT DOMAIN 5067..5160
FT /note="Ig-like C2-type 37"
FT DOMAIN 5171..5260
FT /note="Ig-like C2-type 38"
FT DOMAIN 5277..5366
FT /note="Ig-like C2-type 39"
FT DOMAIN 5383..5472
FT /note="Ig-like C2-type 40"
FT DOMAIN 5487..5578
FT /note="Ig-like C2-type 41"
FT DOMAIN 5595..5685
FT /note="Ig-like C2-type 42"
FT DOMAIN 5701..5790
FT /note="Ig-like C2-type 43"
FT DOMAIN 5815..5904
FT /note="Ig-like C2-type 44"
FT DOMAIN 5925..6014
FT /note="Ig-like C2-type 45"
FT DOMAIN 6038..6130
FT /note="Ig-like C2-type 46"
FT DOMAIN 6150..6239
FT /note="Ig-like C2-type 47"
FT DOMAIN 6278..6374
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 6413..6502
FT /note="Ig-like C2-type 48"
FT DOMAIN 6507..6596
FT /note="Ig-like C2-type 49"
FT DOMAIN 6592..6878
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 7528..7617
FT /note="Ig-like C2-type 50"
FT DOMAIN 7623..7721
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 7785..8035
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4525..4553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6954..7130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7177..7217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7284..7311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7324..7343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7348..7372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7746..7773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1871..1887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7090..7110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7284..7309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 568..621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 2582..2635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2908..2964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3015..3065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 3707..3759
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 3838..3890
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5298..5350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 5404..5456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5508..5560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 5616..5669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 5836..5888
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5946..5998
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305"
FT DISULFID 7549..7600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..6688
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_015541"
FT VAR_SEQ 1..6685
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_015542"
FT VAR_SEQ 1241..1880
FT /note="Missing (in isoform e and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_015543"
FT VAR_SEQ 6632..6695
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_015544"
FT VAR_SEQ 6633..8081
FT /note="Missing (in isoform a and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_015545"
FT VAR_SEQ 6686..6696
FT /note="DEKLALVVFDN -> MFRLVEDCELC (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_015546"
FT VAR_SEQ 6689..6696
FT /note="LALVVFDN -> MVRFTINC (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_015547"
FT VAR_SEQ 7175..7186
FT /note="DFQVEASEPSTP -> VTEGDGCNMCGE (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_015548"
FT VAR_SEQ 7187..8081
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_015549"
FT CONFLICT 2137
FT /note="A -> P (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 2245..2247
FT /note="AKA -> PKP (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 2258
FT /note="A -> P (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 2284
FT /note="E -> G (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 2297
FT /note="M -> I (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 3531
FT /note="A -> G (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 3884..3888
FT /note="DAGEY -> RRRRI (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 3929
FT /note="A -> V (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5134
FT /note="A -> P (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5145
FT /note="T -> S (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5185
FT /note="G -> A (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5199
FT /note="K -> N (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5202
FT /note="L -> F (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 5213
FT /note="F -> L (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 6178
FT /note="A -> G (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT CONFLICT 6268
FT /note="K -> E (in Ref. 1; AAB00542)"
FT /evidence="ECO:0000305"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:1FHO"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:1FHO"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:1FHO"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:1FHO"
SQ SEQUENCE 8081 AA; 894252 MW; 67C804953CF62228 CRC64;
MASRRQKQFD RKYSSYRKFT ATEDVNYSTH SSRSSYRSES LTSRTDGRGR STSSEIIAGS
ESRSYPVYIA IQDYTPDKED VEAIPLEQGQ IVEVLDKKNS VRWLVRTKAR PPRSGWVPGS
YFETPTEFYK QRRRTREIEN VSLSDEQAAL VKRDQVYHEL LRSEEEFVSS LRTCVDDYIK
VLDDPEVPEA VKKNREELTL NIPELYNFHA NVMLKGLNYY SDDPGKVGQT FVRLEKDFES
HVEFYKQYAD TLKLLEEPEI KRFFEGLSAK NDAGASSFVD HVKEIADRMV QYQNYFKEFV
KYSARAHGSS KSIQKALELV TTIPQRVHDL EFTNNLKQHP GDTGKLGRII RHDAFQVWEG
DEPPKLRYVF LFRNKIMFTE QDASTSPPSY THYSSIRLDK YNIRQHTTDE DTIVLQPQEP
GLPSFRIKPK DFETSEYVRK AWLRDIAEEQ EKYAAERDAI SMTATSEMTA SSVDFDMNAS
DQQSEFSEWS GSRKSSLFPG PEEGGPPRKK VKSPPVISPT GSSTSIYSGG SSSIDWTTTG
TTLEMQGTRV TRTQYGFRTL QESSAKMCLK VTGYPLPDIT WYKDDVQLHE DERHTFYSDE
DGFFAMTIDP VQVTDTGRYT CMATNEYGQA STSAFFRVLK VEKEAAPPAF VTKLRDKECK
EGDVIDFECE VEGWPEPELV WLVDDQPLRP SHDFRLQYDG QTAKLEIRDA QPDDTGVYTV
KIQNEFGSIE SKAELFVQAD PDKNHVAPEF QATIEYVECD EGEEVRFKSV ITGDPNPEII
WFINGKPLSE SEKVKFISED GICILTIKDV TRHFDGMVTC QGSNRLGSAS CDGRLKVRVP
PAPPTFNKPL EDKTVQEKST VVFEVDVSGW PEPTLTFTLC GKELKNGEEG VEIVGHDGFY
RISIPNTSMD KHDGEIVAKA QNEHGTAESR ARLTVEQEEE ESRSAPTFLK DIEDQTVKTG
EFAVFETTVR GNPNPEVTWF INGHKMDQGS PGVKIEAHNH DHKLTIDSAQ YAGTVLCRAE
NAVGRFETKA RLVVLAPEKQ KKPPKFVEIL VDKTETVDNT VVFEVRVEGE PKPTVTWYLK
GEELKQSDRV EIREFDGSIK ISIKNIKIED AGEIRAVATN SEGSDETKAK LTVQKKPFAP
EFDLRPVSLT VEKGSEAVFS AHAFGIPLPT YEWSVNGRKV RDGQEGARVT RDESTVDGAS
ILTIDTATYY SEVNHLTISV VAENTLGAEE TGAQLTIEPK KESVVVEKQD LSSSEVQKEI
AQQVKEASPE ATTTITMETS LTSTKTTTMS TTEVTSTVGG VTVETKESES ESATTVIGGG
SGGVTEGSIS VSKIEVVSKT DSQTDVREGT PKRRVSFAEE ELPKEVIDSD RKKKKSPSPD
KKEKSPEKTE EKPASPTKKT GEEVKSPKEK SPASPTKKEK SPAAEEVKSP TKKEKSPSSP
TKKEKSPSSP TKKTGDEVKE KSPPKSPTKK EKSPEKPEDV KSPVKKEKSP DATNIVEVSS
ETTIEKTETT MTTEMTHESE ESRTSVKKEK TPEKVDEKPK SPTKKDKSPE KSITEEIKSP
VKKEKSPEKV EEKPASPTKK EKSPEKPASP TKKSENEVKS PTKKEKSPEK SVVEELKSPK
EKSPEKADDK PKSPTKKEKS PEKSATEDVK SPTKKEKSPE KVEEKPTSPT KKESSPTKKT
DDEVKSPTKK EKSPQTVEEK PASPTKKEKS PEKSVVEEVK SPKEKSPEKA EEKPKSPTKK
EKSPEKSAAE EVKSPTKKEK SPEKSAEEKP KSPTKKESSP VKMADDEVKS PTKKEKSPEK
VEEKPASPTK KEKTPEKSAA EELKSPTKKE KSPSSPTKKT GDESKEKSPE KPEEKPKSPT
PKKSPPGSPK KKKSKSPEAE KPPAPKLTRD LKLQTVNKTD LAHFEVVVEH ATECKWFLDG
KEITTAQGVT VSKDDQFEFR CSIDTTMFGS GTVSVVASNA AGSVETKTEL KVLETPKETK
KPEFTDKLRD MEVTKGDTVQ MDVIALHSPL YKWYQNGNLL EDGKNGVTIK NEENKSSLII
PNAQDSGKIT VEASNEVGSS ESSAQLTVNP PSTTPIVVDG PKSVTIKETE TAEFKATISG
FPAPTVKWTI NEKIVEESRT ITTIKTEDVY TLKISNAKIE QTGTVKVTAQ NSAGQDSKQA
DLKVEPNVKA PKFKSQLTDK VADEGEPLRW NLELDGPSPG TEVSWLLNGQ PLTKSDTVQV
VDHGDGTYHV TIAEAKPEMS GTLTAKAKNA AGECETSAKV TVNGGNKKPE FVQAPQNHET
TLEESVKFSA IVTGKPMPNV TWYLNNKKLI QSEEVKVKYV HETGKTSIRI QKPLMEHNGT
IRVEAENVSG KVQATAQLKV DKKTEVPKFT TNMDDRQVKE GEDVKFTANV EGYPEPSVAW
TLNGEPVSKH PNITVTDKDG EHTIEISAVT PEQAGELSCE ATNPVGSKKR DVQLAVKKVG
DAPTFAKNLE DRLITEGELT LMDAKLNIVK PKPKITWLKD GVEITSDGHY KIVEEEDGSL
KLSILQTKLE DKGRITIKAE SEFGVAECSA SLGVVKGRPM AKPAFQSDIA PINLTEGDTL
ECKLLITGDP TPFVKWYIGT QLVCATEDTE ISNANGVYTM KIHGVTADMT GKIKCVAYNK
AGEVSTEGPL KVVAPIPVEF ETSLCDATCR EGDTLKLRAV LLGEPEPVVS WYVNGKKLEE
SQNIKIHSEK GTYTVTIKDI TCDYSGQVVC EAINEYGKAT SEATLLVLPR GEPPDFLEWL
SNVRARTGTK VVHKVVFTGD PKPSLTWYIN NKEILNSDLY TIVTDDKTST LTINSFNPDV
HVGEIICKAE NDAGEVSCTA NMITYTSDMF SESESEAQAE EFVGDDLTED ESLREEMHRT
PTPVMAPKFI TKIKDTKAKK GHSAVFECVV PDTKGVCCKW LKDGKEIELI ARIRVQTRTG
PEGHITQELV LDNVTPEDAG KYTCIVENTA GKDTCEATLT VIESLEKKSE KKAPEFIVAL
QDKTTKTSEK VVLECKVIGE PKPKVSWLHD NKTITQESIT VESVEGVERV TITSSELSHQ
GKYTCIAENT EGTSKTEAFL TVQGEAPVFT KELQNKELSI GEKLVLSCSV KGSPQPHVDF
YSFSETTKVE TKITSSSRIA IEHDQTNTHW RMVISQITKE DIVSYKAIAT NSIGTATSTS
KITTKVEAPV FEQGLKKTSV KEKEEIKMEV KVGGSAPDVE WFKDDKPVSE DGNHEMKKNP
ETGVFTLVVK QAATTDAGKY TAKASNPAGT AESSAEAEVT QSLEKPTFVR ELVTTEVKIN
ETATLSVTVK GVPDPSVEWL KDGQPVQTDS SHVIAKVEGS GSYSITIKDA RLEDSGKYAC
RATNPAGEAK TEANFAVVKN LVPPEFVEKL SPLEVKEKES TTLSVKVVGT PEPSVEWFKD
DTPISIDNVH VIQKQTAVGS FSLTINDARQ GDVGIYSCRA RNEAGEALTT ANFGIIRDSI
PPEFTQKLRP LEVREQETLD LKVTVIGTPV PNVEWFKDDK PINIDNSHIF AKDEGSGHHT
LTIKQARGED VGVYTCKATN EAGEAKTTAN MAVQEEIEAP LFVQGLKPYE VEQGKPAELV
VRVEGKPEPE VKWFKDGVPI AIDNQHVIEK KGENGSHTLV IKDTNNADFG KYTCQATNKA
GKDETVGELK IPKYSFEKQT AEEVKPLFIE PLKETFAVEG DTVVLECKVN KESHPQIKFF
KNDQPVEIGQ HMQLEVLEDG NIKLTIQNAK KEDVGAYRCE AVNVAGKANT NADLKIQFAA
KVEEHVTDES GQLEEIGQFE TVGDTASSKT DTGRGAPEFV ELLRSCTVTE KQQAILKCKV
KGEPRPKIKW TKEGKEVEMS ARVRAEHKDD GTLTLTFDNV TQADAGEYRC EAENEYGSAW
TEGPIIVTLE GAPKIDGEAP DFLQPVKPAV VTVGETAVLE GKISGKPKPS VKWYKNGEEL
KPSDRVKIEN LDDGTQRLTV TNAKLDDMDE YRCEASNEFG DVWSDVTLTV KEPAQVAPGF
FKELSAIQVK ETETAKFECK VSGTKPDVKW FKDGTPLKED KRVHFESTDD GTQRLVIEDS
KTDDQGNYRI EVSNDAGVAN SKVPLTVVPS ETLKIKKGLT DVNVTQGTKI LLSVEVEGKP
KTVKWYKGTE TVTSSQTTKI VQVTESEYKL EIESAEMSDT GAYRVVLSTD SFSVESSATV
TVTKAAEKIS LPSFKKGLAD QSVPKGTPLV LEVEIEGKPK DVKWYKNGDE IKDGKVEDLG
NGKYRLTIPD FQEKDVGEYS VTAANEAGEI ESKAKVNVSA KPEIVSGLVP TTVKQGETAT
FNVKVKGPVK GVKWYKNGKE IPDAKTKDNG DGSYSLEIPN AQVEDAADYK VVVSNDAGDA
DSSAALTVKL ADDGKDKVKP EIVSGLIPTT VKQGETATFN VKVKGPVKQV KWYKNGKEIP
NAKAKDNGDG SYSLEIPNAQ LDDTADYKVV VSNDAGDADS SAALTVKLPG IAIVKGLEDA
EVPKGKKAVL QVETNKKPKE IKWYKNGKEI TPSDKAQPGS DGDNKPQLVI PDAGDDDAAE
YKVVLTDEDG NTADSSCALT VKLPAKEPKI IKGLEDQVVS IGSPIKLEIE TSGSPKTVKW
YKNGKELPGA AAKTIKIQKI DDNKYVLEIP SSVVEDTGDY KVEVANEAGS ANSSGKITVE
PKITFLKPLK DQSITEGENA EFSVETNTKP RIVKWYKNGQ EIKPNSRFII EQKTDTKYQL
VIKNAVRDDA DTYKIVLENT AGEAESSAQL TVKKAKAGLC KIVKGLEDQV VAKGAKMVFE
VKIQGEPEDV RWLRDANVIS AGANAIIEKI DDTTYRLIIP SADLKDAGEY TVEVINESGK
AKSDAKGEVD EKPEIVRGLE NIEIPEGDDD VFKVEVSAPV RQVKWYKNDQ EIKPNSHLEA
KKIGPKKYEL AINRAQLDDG ADYKVVLSNA AGDCDSSAAL TVVKPNVLKI VDGLKDVDVE
EPQPVELKVK VEGIPKVIKW YKNGQELKPD ADGFKFEEKP ESGEFSLTIP SSKKSDGGAY
RVVLGNDKGE VYSGSVVHVK SAKSSEPTSG ANFLSPLKDT EVEEGDMLTL QCTIAGEPFP
EVIWEKDGVV LQKDDRITMR VALDGTATLR IRSAKKSDIG QYRVTAKNEA GSATSDCKVT
VTEQGEQPSK PKFVIPLKTG AALPGDKKEF NVKVRGLPKP TLQWFLNGIP IKFDDRITLD
DMADGNYCLT IRDVREEDFG TLKCIAKNEN GTDETVCEFQ QGAGHDDGSR DDLRYPPRFN
VPLWDRRIPV GDPMFIECHV DANPTAEVEW FKDGKKIEHT AHTEIRNTVD GACRIKIIPF
EESDIGVYMC VAVNELGQAE TQATYQVEIL EHVEEEKRRE YAPKINPPLE DKTVNGGQPI
RLSCKVDAIP RASVVWYKDG LPLRADSRTS IQYEEDGTAT LAINDSTEED IGAYRCVATN
AHGTINTSCS VNVKVPKQEV KKEGEEPFFT KGLVDLWADR GDSFTLKCAV TGDPFPEIKW
YRNGQLLRNG PRTVIETSPD GSCSLTVNES TMSDEGIYRC EAENAHGKAK TQATAHVQMA
LGKTEKPKMD EGKPPKFILE LSDMSVSLGN VIDLECKVTG LPNPSVKWSK DGGPLIEDSR
FEWSNEASKG VYQLRIKNAT VHDEGTYRCV ATNENGSATT KSFVRMDDGL GSGVVTASQP
PRFTLKMGDV RTTEGQPLKL ECKVDASPLP EMVWYKDGAI VTPSDRIQIS LSPDGVATLL
IPSCVYDDDG IYRVIATNPS GTAQDKGTAT VKKLPRDSGA RRSADRDVFD ANKAPKLMEP
LENIRIPEKQ SFRLRCKFSG DPKPTIKWFK DGERVFPYGR LQLIESPDGV CELVVDSATR
QDAGGYRCVA ENTYGSARTS CDVNVIRGDR KPRDIDSSIR EGKAPGFTTP LTIRRAKPGD
SVTFECLPFG NPFPSIKWLK DGLELFSDEK IKMEAAADGT QRLILSDVTF LSEGYFRCVA
TNEHGTASTK AELVIEGDRT IGSRPLPEVN GEPEECKPRI RRGLYNMSIH EGNVVEMIVC
ATGIPTPTVK WYKDGQEIVG DGPDGKRVIF TDERGIHHLV IVNASPDDEG EYSLEATNKL
GSAKTEGSLN IIRPRHIADA DERGGMPFPP GFVRQLKNKH VFNHMPTIFD CLVVGHPAPE
VEWFHNGKKI VPGGRIKIQS CGGGSHALII LDTTLEDAGE YVATAKNSHG SASSSAVLDV
TVPFLDSIKF NGEIDVTPYL TEEYGFKKLN TASLPTPPDR GPFIKEVTGH YLTLSWIPTK
RAPPRYPQVT YVIEIRELPE KQWSLLEYNI PEPVCKVRNL ELGKSYQFRV RAENIYGISD
PSPASPPSRL MAPPQPVFDR RTNKVIPLLD PYAEKALDMR YSEQYACAPW FSPGVVEKRY
CAENDTLTIV LNVSGFPDPD IKWKFRGWDI DTSSPTSKCK VYTYGGSETT LAITGFSKEN
VGQYQCFAKN DYGDAQQNIM VDLATRPNFI QPLVNKTFSS AQPMRMDVRV DGEPFPELKW
MKEWRPIVES SRIKFVQDGP YLCSLIINDP MWRDSGIYSC VAVNDAGQAT TSCTVTVEAE
GDYNDVELPR RRVTIESRRV RELYEISEKD EKLAAEGAPF RVKEKATGRE FLAQLRPIDD
ALMRHVDIHN SLDHPGIVQM HRVLRDEKLA LVVFDNANST IDGLSSLAHP GVEIAEPKGV
NRETCVRVFV RQLLLALKHM HDLRIAHLDL RPETILLQDD KLKLADFGQA RRLLRGLITG
EIKGSPEFVS PEIVRSYPLT LATDMWSTGV LTYVLLTGLS PFHGDNDNET LANVDSCQFD
SSPLGNFSYD AGDFVKKLLT EIPVSRLTVD EALDHPWIND EKLKTEPLSA DTLREFKYQH
KWLERRVFVQ QTPSEQILEA ILGPATAQAQ QNAPVAPEGR RPAEIYDYLR IQPKKPPPTV
EYVPQPRKEH PPFIDEFGQL IDGDAFDRPE GTGFEGPHRQ PPQIPPQPQR PNQAAHDSRR
HEQQPQHQGQ PQRIPVDQYG RPLVDPRYLN DPSHRPSSLD DAPFYVDKYG NPVHFDKYGR
PMAPQNLEKR KLIPQDKGET PSHSKKEKTQ HPVATPILAS PGGDQQQQKI PMRMIRGERR
EIEEEIANRI LSDISEEGSI AGSLASLEDF EIPKDFQVEA SEPSTPTLTP EVTIRETIPK
PTPSPTSPQK SPVPQPQGLL IPAKVTYSDS ILAGLPAADK KVLEDAENDP SIPVGAPLFL
EGLHGSDLTI DTTSASGLIK VTSPAINLSP NPKSPRRSTP GTKSPVVLSP RQEHSMEVLI
ATKRGKPGFL PPGELAEDID DEDAFMDDRK KQVKPKDHDG ENDFKDEKER LEKDKNRRTV
NLDDLDKYRP SAFYKDDSDF GHPGYDIDAT PWDSHYQIGP DTYLMAARGA AFNSRVRNYR
EELFGMGAPT VKQGFLGVRN RDITVRERRR YTDILRETTQ GLEPKSHEQS TALLQKAPSA
TAIERIKADI EKVTPCATKK NDDGTFAPIF TARLRDVYLR KNQPAIFECA VSASPAPKVT
WDFQGKILES NDRVTIEQDN NVARLILNHA APYDLGEYVC TAINEYGTDK SSCRLISGET
PSRPGRPEAE LSSDTEIFIQ WEAPEGPTYL EGITYRLEYR VAGPNDHGDP WITVSEKIDD
ESVIVKHLSP LGIYQFRVTA QNGFGLGLPS LSSRIVQTHG KGAPKLQIDV LKSEIRLNVV
SMPQKSTNQL GGISEESEED SEARTANEDM KSNLQLQTDD PTGRFQIGGL KFKGRFSVIR
DAVDSTTEGH AHCAVKIRHP SSEAISEYES LRDGQHENVQ RLIAAFNNSN FLYLLSERLY
EDVFSRFVFN DYYTEEQVAL TMRQVTSALH FLHFKGIAHL DVNPHNIMFQ SKRSWVVKLV
DFGRAQKVSG AVKPVDFDTK WASPEFHIPE TPVTVQSDMW GMGVVTFCLL AGFHPFTSEY
DREEEIKENV INVKCDPNLI PVNASQECLS FATWALKKSP VRRMRTDEAL SHKFLSSDPS
MVRRRESIKY SASRLRKLAA MIRQPTFSQP ISEELESKYG K
