KETN1_CAEEL
ID KETN1_CAEEL Reviewed; 4963 AA.
AC V6CLP5; A0A0M7RDU5; A0A0M9JJ85; H2L074; H2L075; H2L076; Q5PY59; Q8MXD8;
AC Q9NL87; V6CJB8; V6CKH1; V6CLT3; V6CLU0; V6CLU5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Kettin homolog {ECO:0000305};
GN Name=ketn-1 {ECO:0000303|PubMed:16597697, ECO:0000312|WormBase:F54E2.3g};
GN Synonyms=let-330 {ECO:0000303|PubMed:31411810},
GN MH44 {ECO:0000312|WormBase:F54E2.3g},
GN pqn-43 {ECO:0000312|WormBase:F54E2.3g};
GN ORFNames=F54E2.3 {ECO:0000312|WormBase:F54E2.3g};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAA90302.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10629221; DOI=10.1083/jcb.148.1.101;
RA Hakeda S., Endo S., Saigo K.;
RT "Requirements of Kettin, a giant muscle protein highly conserved in overall
RT structure in evolution, for normal muscle function, viability, and flight
RT activity of Drosophila.";
RL J. Cell Biol. 148:101-114(2000).
RN [2] {ECO:0000312|EMBL:AAV69856.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, INTERACTION WITH F-ACTIN, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16597697; DOI=10.1091/mbc.e06-02-0114;
RA Ono K., Yu R., Mohri K., Ono S.;
RT "Caenorhabditis elegans kettin, a large immunoglobulin-like repeat protein,
RT binds to filamentous actin and provides mechanical stability to the
RT contractile apparatuses in body wall muscle.";
RL Mol. Biol. Cell 17:2722-2734(2006).
RN [3] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10669599; DOI=10.1006/jmbi.1999.3461;
RA Kolmerer B., Clayton J., Benes V., Allen T., Ferguson C., Leonard K.,
RA Weber U., Knekt M., Ansorge W., Labeit S., Bullard B.;
RT "Sequence and expression of the kettin gene in Drosophila melanogaster and
RT Caenorhabditis elegans.";
RL J. Mol. Biol. 296:435-448(2000).
RN [5] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16453162; DOI=10.1007/s10974-005-9028-3;
RA Ono S., Mohri K., Ono K.;
RT "Molecular and biochemical characterization of kettin in Caenorhabditis
RT elegans.";
RL J. Muscle Res. Cell Motil. 26:449-454(2005).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 1739-GLN--ARG-4963 AND 3967-GLN--ARG-4963.
RX PubMed=31411810; DOI=10.1111/febs.15039;
RA Ono K., Qin Z., Johnsen R.C., Baillie D.L., Ono S.;
RT "Kettin, the large actin-binding protein with multiple immunoglobulin
RT domains, is essential for sarcomeric actin assembly and larval development
RT in Caenorhabditis elegans.";
RL FEBS J. 287:659-670(2020).
CC -!- FUNCTION: Positively regulates actin filament organization and provides
CC mechanical stability to the myofibrils during body wall muscle
CC contraction (PubMed:16597697). Required for the organization of
CC sarcomeric actin filaments and myosin protein myo-3 in striated body
CC wall muscle cells (PubMed:31411810). Not required for assembly of dense
CC bodies, which are a type of integrin-based adhesion structure that link
CC the plasma membrane to thin filaments of myofibrils, in body wall
CC muscle (PubMed:31411810). Not required for the atn-1 protein to
CC localize to the dense bodies (PubMed:31411810).
CC {ECO:0000269|PubMed:16597697, ECO:0000269|PubMed:31411810}.
CC -!- SUBUNIT: Interacts (via Ig-like domains) with F-actin.
CC {ECO:0000269|PubMed:16597697}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:10669599, ECO:0000269|PubMed:16453162,
CC ECO:0000269|PubMed:31411810}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16597697}. Note=Localizes to sarcomeres in a
CC punctate pattern (PubMed:31411810). Localizes to actin filaments (thin
CC filaments) close to dense bodies in body wall muscle (PubMed:16597697).
CC Co-localizes with actin filaments in embryos and adults
CC (PubMed:16453162, PubMed:31411810). {ECO:0000269|PubMed:16453162,
CC ECO:0000269|PubMed:16597697, ECO:0000269|PubMed:31411810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=g {ECO:0000312|WormBase:F54E2.3g};
CC IsoId=V6CLP5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F54E2.3a};
CC IsoId=V6CLP5-2; Sequence=VSP_061261, VSP_061264;
CC Name=c {ECO:0000312|WormBase:F54E2.3c};
CC IsoId=V6CLP5-3; Sequence=VSP_061261, VSP_061263;
CC Name=d {ECO:0000312|WormBase:F54E2.3d};
CC IsoId=V6CLP5-4; Sequence=VSP_061261, VSP_061264, VSP_061265,
CC VSP_061266;
CC Name=e {ECO:0000312|WormBase:F54E2.3e};
CC IsoId=V6CLP5-5; Sequence=VSP_061264;
CC Name=f {ECO:0000312|WormBase:F54E2.3f};
CC IsoId=V6CLP5-6; Sequence=VSP_061263;
CC Name=h {ECO:0000312|WormBase:F54E2.3h};
CC IsoId=V6CLP5-7; Sequence=VSP_061262;
CC Name=i {ECO:0000312|WormBase:F54E2.3i};
CC IsoId=V6CLP5-8; Sequence=VSP_061261;
CC Name=j {ECO:0000312|WormBase:F54E2.3j};
CC IsoId=V6CLP5-9; Sequence=VSP_061261, VSP_061262;
CC Name=k {ECO:0000312|WormBase:F54E2.3k};
CC IsoId=V6CLP5-10; Sequence=VSP_061260, VSP_061264;
CC Name=l {ECO:0000312|WormBase:F54E2.3l};
CC IsoId=V6CLP5-11; Sequence=VSP_061259, VSP_061264;
CC -!- TISSUE SPECIFICITY: Expressed in the pharyngeal, body wall, and anal
CC depressor muscles (PubMed:16597697, PubMed:10669599, PubMed:16453162).
CC Expression in these muscles is higher in hermaphrodites than in males
CC (PubMed:10669599). Expressed in the vulva and the myoepithelial sheath
CC of the proximal ovary (PubMed:16597697). Expressed in the proximal
CC gonad of males (PubMed:10669599). Not expressed in the dense bodies of
CC the obliquely striated body wall muscle (PubMed:16453162).
CC {ECO:0000269|PubMed:10669599, ECO:0000269|PubMed:16453162,
CC ECO:0000269|PubMed:16597697}.
CC -!- DEVELOPMENTAL STAGE: First expressed in body wall muscle at the comma
CC stage of embryonic development and co-localizes with actin at the early
CC stage of myofibril assembly (PubMed:16597697). At the two-fold stage,
CC it is expressed in body wall muscles and in the pharynx
CC (PubMed:16597697). At the two-fold embryonic stage, assembles into
CC continuously organized myofibrils (PubMed:31411810). Highly expressed
CC in the body wall muscle and pharynx in three-fold stage embryos
CC (PubMed:16597697, PubMed:31411810). In larvae, highly expressed in the
CC pharyngeal, body wall, and anal depressor muscles (PubMed:10669599,
CC PubMed:31411810). {ECO:0000269|PubMed:10669599,
CC ECO:0000269|PubMed:16597697, ECO:0000269|PubMed:31411810}.
CC -!- DISRUPTION PHENOTYPE: Lethal during the larval stage of development
CC with body elongation defects (PubMed:31411810). L1 stage larvae have
CC severely disorganized actin filaments in the striated body wall muscle
CC whereby actin filaments and tropomyosin assemble into thicker and fewer
CC disorganized bundles (PubMed:31411810). Furthermore, the sarcomeric
CC organization of actin and myo-3 is disrupted in body wall muscle cells
CC (PubMed:31411810). RNAi-mediated knockdown reduces the brood size and
CC results in a defective body wall muscle contractility
CC (PubMed:16597697). RNAi-mediated knockdown results in small round actin
CC aggregates or unusual accumulations of actin in body wall muscle in 23%
CC of animals (PubMed:16597697). Larger actin aggregates form more
CC frequently at the cell periphery in 94% of animals in response to
CC tetramisole, an agonist of acetylcholine receptors (PubMed:16597697).
CC RNAi-mediated knockdown enhances the disorganization of the actin
CC filaments and results in larger actin aggregates in an atn-1 ok84
CC mutant background (PubMed:16597697). {ECO:0000269|PubMed:16597697,
CC ECO:0000269|PubMed:31411810}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90302.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026846; BAA90302.2; ALT_SEQ; mRNA.
DR EMBL; AY819766; AAV69856.1; -; mRNA.
DR EMBL; BX284605; CCD71805.2; -; Genomic_DNA.
DR EMBL; BX284605; CCD71806.2; -; Genomic_DNA.
DR EMBL; BX284605; CCD71809.2; -; Genomic_DNA.
DR EMBL; BX284605; CDK13527.1; -; Genomic_DNA.
DR EMBL; BX284605; CDK13528.1; -; Genomic_DNA.
DR EMBL; BX284605; CDK13529.1; -; Genomic_DNA.
DR EMBL; BX284605; CDK13530.1; -; Genomic_DNA.
DR EMBL; BX284605; CDK13531.1; -; Genomic_DNA.
DR EMBL; BX284605; CDK13532.1; -; Genomic_DNA.
DR EMBL; BX284605; CUR30035.1; -; Genomic_DNA.
DR EMBL; BX284605; CUR30036.1; -; Genomic_DNA.
DR RefSeq; NP_001294668.1; NM_001307739.1.
DR SMR; V6CLP5; -.
DR IntAct; V6CLP5; 1.
DR STRING; 6239.F54E2.3a; -.
DR EPD; V6CLP5; -.
DR PeptideAtlas; V6CLP5; -.
DR EnsemblMetazoa; F54E2.3a.1; F54E2.3a.1; WBGene00004130. [V6CLP5-2]
DR EnsemblMetazoa; F54E2.3c.1; F54E2.3c.1; WBGene00004130. [V6CLP5-3]
DR EnsemblMetazoa; F54E2.3d.1; F54E2.3d.1; WBGene00004130. [V6CLP5-4]
DR EnsemblMetazoa; F54E2.3e.1; F54E2.3e.1; WBGene00004130. [V6CLP5-5]
DR EnsemblMetazoa; F54E2.3f.1; F54E2.3f.1; WBGene00004130. [V6CLP5-6]
DR EnsemblMetazoa; F54E2.3g.1; F54E2.3g.1; WBGene00004130. [V6CLP5-1]
DR EnsemblMetazoa; F54E2.3h.1; F54E2.3h.1; WBGene00004130. [V6CLP5-7]
DR EnsemblMetazoa; F54E2.3i.1; F54E2.3i.1; WBGene00004130. [V6CLP5-8]
DR EnsemblMetazoa; F54E2.3j.1; F54E2.3j.1; WBGene00004130. [V6CLP5-9]
DR EnsemblMetazoa; F54E2.3k.1; F54E2.3k.1; WBGene00004130. [V6CLP5-10]
DR EnsemblMetazoa; F54E2.3l.1; F54E2.3l.1; WBGene00004130. [V6CLP5-11]
DR GeneID; 178740; -.
DR CTD; 178740; -.
DR WormBase; F54E2.3a; CE49211; WBGene00004130; ketn-1. [V6CLP5-2]
DR WormBase; F54E2.3c; CE49414; WBGene00004130; ketn-1. [V6CLP5-3]
DR WormBase; F54E2.3d; CE49335; WBGene00004130; ketn-1. [V6CLP5-4]
DR WormBase; F54E2.3e; CE38607; WBGene00004130; ketn-1. [V6CLP5-5]
DR WormBase; F54E2.3f; CE49179; WBGene00004130; ketn-1. [V6CLP5-6]
DR WormBase; F54E2.3g; CE49469; WBGene00004130; ketn-1. [V6CLP5-1]
DR WormBase; F54E2.3h; CE49363; WBGene00004130; ketn-1. [V6CLP5-7]
DR WormBase; F54E2.3i; CE49330; WBGene00004130; ketn-1. [V6CLP5-8]
DR WormBase; F54E2.3j; CE49233; WBGene00004130; ketn-1. [V6CLP5-9]
DR WormBase; F54E2.3k; CE51066; WBGene00004130; ketn-1. [V6CLP5-10]
DR WormBase; F54E2.3l; CE51139; WBGene00004130; ketn-1. [V6CLP5-11]
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000169215; -.
DR HOGENOM; CLU_000029_0_0_1; -.
DR OMA; QLHWRRE; -.
DR OrthoDB; 184at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004130; Expressed in pharyngeal muscle cell (C elegans) and 7 other tissues.
DR ExpressionAtlas; V6CLP5; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031674; C:I band; IDA:WormBase.
DR GO; GO:0031430; C:M band; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 34.
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 Pfam; PF07679; I-set; 34.
DR SMART; SM00409; IG; 34.
DR SMART; SM00408; IGc2; 25.
DR SUPFAM; SSF48726; SSF48726; 34.
DR PROSITE; PS50835; IG_LIKE; 32.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disulfide bond; Immunoglobulin domain; Muscle protein; Reference proteome;
KW Repeat.
FT CHAIN 1..4963
FT /note="Kettin homolog"
FT /id="PRO_0000454211"
FT DOMAIN 18..105
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 133..220
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 303..392
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 706..796
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 806..893
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 937..1027
FT /note="Ig-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1065..1155
FT /note="Ig-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1199..1281
FT /note="Ig-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1462..1554
FT /note="Ig-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1594..1687
FT /note="Ig-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1728..1819
FT /note="Ig-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1992..2085
FT /note="Ig-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2126..2217
FT /note="Ig-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2258..2350
FT /note="Ig-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2391..2481
FT /note="Ig-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2522..2613
FT /note="Ig-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2654..2745
FT /note="Ig-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2787..2878
FT /note="Ig-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2919..3010
FT /note="Ig-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3051..3141
FT /note="Ig-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3182..3273
FT /note="Ig-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3314..3407
FT /note="Ig-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3448..3539
FT /note="Ig-like 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3584..3677
FT /note="Ig-like 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3720..3811
FT /note="Ig-like 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3821..3913
FT /note="Ig-like 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3962..4052
FT /note="Ig-like 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4098..4185
FT /note="Ig-like 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4546..4634
FT /note="Ig-like 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4645..4733
FT /note="Ig-like 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4752..4842
FT /note="Ig-like 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4872..4960
FT /note="Ig-like 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 396..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3567..3590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4193..4963
FT /note="Required for F-actin binding"
FT /evidence="ECO:0000269|PubMed:16597697"
FT REGION 4319..4357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..517
FT /evidence="ECO:0000255"
FT COMPBIAS 396..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3567..3581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 827..877
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1201..1265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1618..1671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2016..2069
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2148..2201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3606..3659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3742..3795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..1690
FT /note="MPFKQPLGERDAANRVAPTFIRPLADKRAVVGETIILECQLEGHPDPAIKWL
FT KDGHNVSMCPDYRIEEDGLKHRLVIPQVQAADSGRFTAQASNSAGTKQSTCILICAPAP
FT TPVPGAKSAVASPAPPQTPVGPSAPIFLKELRHQPLKPGAGVTFEGRVIAVPPPNIEWM
FT KNGKPLQNYRAKIEHDQKTGIISLIIPQMFNDDAGEYTIKATNVHGEAISGAQLLPREQ
FT YDRWFSNEQTRLTKDRKQGLLSQTLRPSSVAQKQMQKQGYDTDQGSVDMHWTISESETE
FT PELSALDARGVGTKPIIRTPLRGLRLTEGTDAILQANIVGNPKPRIQWLFNGRPLQVSG
FT PRMQMTYKGSMAVLKISMVTTEEAGDYTVASENRFGKVESSARIEVYPLSVPDERRKEN
FT QLREQQERDRQQQQQALVEASLARERQRDAENRRIREEQDRLRVLFEREKAERERLEEE
FT RRQLEHEKRLRQQQQQQLFEREKSEKEERARLEEERRRLEHEKHLRQQQQTQPYNLHYQ
FT QHHQPHQAWQDLDLVRRPQYASDEYQEPHYAQIRPHQQQQQHYQQQQQSPRQEVTHQNL
FT YEQHRRQQQLIREQQLYQHQHQQHQQQQQQPQEQQQQRFHHFNQYQQHIREQHQNTMPV
FT FRQQQPTQVTNGGIKAANGSAKTANGSANGSANGSAVHAANGGPSSQQARGHEHGAALV
FT NARPPQFLVHPQSVAAKAFETVTFSAKVVGTPTPSLTWQKSDGTVIQSGGKYKIENGPD
FT GSGRLIIEKVDAHDADMYMLVARNDGGSFQSRFSLNVLQAKSPEAPEFTGKFQSTTLYD
FT GDSVKLYCKAAGEGVSFKWFKDNEPISSGGSYAVDNKGNETTLHINNATMKEGGWYRCD
FT ATNKHGTTTLKGRVVVNSRQKFNGPAHREMITLRKVDKVERSRTPVNQLQDVSASKSSP
FT KFEGSLQSQQLVEGQSARLEIKYTPVEDPNLRIAWLLNGKGILASSRIVTFTDFGIAAL
FT EINPVNVFDQGEYTVVAVNPLGEARVSANIAVIGHGSFIQQQQSGSQFGGTAYQSKGAQ
FT APAGTHLDLPNFHSDLRSQEVFEGQQIHLETKLTPINDPDLRVVWLLDGNELPSNDKYR
FT QTLSHGFASLDIPQTSSNDSGLYSCRAFNKLGESENQATIIIVPKSDLQQFEQHRQLDV
FT EDVREIQFAHSSQDLTPKFLSQIQPFHCEQELGRSFFEARIQPINDPTLRVSWLKDGQP
FT LPNANRIQIFQNFGVVSLSLHPTYPEDAGVYTCVLFNSHGQAQSSAELTTVWIDTLQLD
FT SKHADSLPIIGYLDSHQIHIGPQSVERPEEFNSLEAPKFARELAGKIEVMENERVHFEA
FT RILPANDVKMTVEWYHNGNPLPAAHRFHPMFDFGYVALDLLYAYPQDSGTYTLVARNEL
FT GEARSNVELVVGTEKVLYLEPHHPEGLERIKELEQDRRQGIAEVEDRTCDAAPKFLNDL
FT PDIQLNEHENIHVDLRATPVNDPTMVIEWFVNGRPLLTGSRVKTLNEFGFIALDIKGAI
FT AEDSGTYSVRASNLLGEAIRQCVITVTPAGQILSDTQHQESLGKINYLENLNKYGRVEI
FT EDKGPQEPPTFVVPLQADLGDVEEGEPIHLECQVNPINDNSLKIIWLRDGQSLPHGHRF
FT RTFYDFGFVSLDILGFYAQDAGTYTCRAENSLGQAETVATIRCAP -> MSSNKYVFGV
FT NYGPKPTVPPNSSSSLSGMSHILKSTESHSRKPATATRNNGMGLLNLSNSA (in
FT isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_061259"
FT VAR_SEQ 1..1492
FT /note="Missing (in isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_061260"
FT VAR_SEQ 1..639
FT /note="Missing (in isoform a, isoform c, isoform d, isoform
FT i and isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_061261"
FT VAR_SEQ 4417..4457
FT /note="Missing (in isoform h and isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_061262"
FT VAR_SEQ 4418..4532
FT /note="Missing (in isoform c and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_061263"
FT VAR_SEQ 4459..4532
FT /note="Missing (in isoform a, isoform d, isoform e, isoform
FT k and isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_061264"
FT VAR_SEQ 4843..4844
FT /note="PR -> RR (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061265"
FT VAR_SEQ 4845..4963
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061266"
FT MUTAGEN 1739..4963
FT /note="Missing: In s1429; lethal at the L1 larval stage."
FT /evidence="ECO:0000269|PubMed:31411810"
FT MUTAGEN 3967..4963
FT /note="Missing: In s1425; lethal at the L1 larval stage."
FT /evidence="ECO:0000269|PubMed:31411810"
SQ SEQUENCE 4963 AA; 554874 MW; 360B42A5725847CD CRC64;
MPFKQPLGER DAANRVAPTF IRPLADKRAV VGETIILECQ LEGHPDPAIK WLKDGHNVSM
CPDYRIEEDG LKHRLVIPQV QAADSGRFTA QASNSAGTKQ STCILICAPA PTPVPGAKSA
VASPAPPQTP VGPSAPIFLK ELRHQPLKPG AGVTFEGRVI AVPPPNIEWM KNGKPLQNYR
AKIEHDQKTG IISLIIPQMF NDDAGEYTIK ATNVHGEAIS GAQLLPREQY DRWFSNEQTR
LTKDRKQGLL SQTLRPSSVA QKQMQKQGYD TDQGSVDMHW TISESETEPE LSALDARGVG
TKPIIRTPLR GLRLTEGTDA ILQANIVGNP KPRIQWLFNG RPLQVSGPRM QMTYKGSMAV
LKISMVTTEE AGDYTVASEN RFGKVESSAR IEVYPLSVPD ERRKENQLRE QQERDRQQQQ
QALVEASLAR ERQRDAENRR IREEQDRLRV LFEREKAERE RLEEERRQLE HEKRLRQQQQ
QQLFEREKSE KEERARLEEE RRRLEHEKHL RQQQQTQPYN LHYQQHHQPH QAWQDLDLVR
RPQYASDEYQ EPHYAQIRPH QQQQQHYQQQ QQSPRQEVTH QNLYEQHRRQ QQLIREQQLY
QHQHQQHQQQ QQQPQEQQQQ RFHHFNQYQQ HIREQHQNTM PVFRQQQPTQ VTNGGIKAAN
GSAKTANGSA NGSANGSAVH AANGGPSSQQ ARGHEHGAAL VNARPPQFLV HPQSVAAKAF
ETVTFSAKVV GTPTPSLTWQ KSDGTVIQSG GKYKIENGPD GSGRLIIEKV DAHDADMYML
VARNDGGSFQ SRFSLNVLQA KSPEAPEFTG KFQSTTLYDG DSVKLYCKAA GEGVSFKWFK
DNEPISSGGS YAVDNKGNET TLHINNATMK EGGWYRCDAT NKHGTTTLKG RVVVNSRQKF
NGPAHREMIT LRKVDKVERS RTPVNQLQDV SASKSSPKFE GSLQSQQLVE GQSARLEIKY
TPVEDPNLRI AWLLNGKGIL ASSRIVTFTD FGIAALEINP VNVFDQGEYT VVAVNPLGEA
RVSANIAVIG HGSFIQQQQS GSQFGGTAYQ SKGAQAPAGT HLDLPNFHSD LRSQEVFEGQ
QIHLETKLTP INDPDLRVVW LLDGNELPSN DKYRQTLSHG FASLDIPQTS SNDSGLYSCR
AFNKLGESEN QATIIIVPKS DLQQFEQHRQ LDVEDVREIQ FAHSSQDLTP KFLSQIQPFH
CEQELGRSFF EARIQPINDP TLRVSWLKDG QPLPNANRIQ IFQNFGVVSL SLHPTYPEDA
GVYTCVLFNS HGQAQSSAEL TTVWIDTLQL DSKHADSLPI IGYLDSHQIH IGPQSVERPE
EFNSLEAPKF ARELAGKIEV MENERVHFEA RILPANDVKM TVEWYHNGNP LPAAHRFHPM
FDFGYVALDL LYAYPQDSGT YTLVARNELG EARSNVELVV GTEKVLYLEP HHPEGLERIK
ELEQDRRQGI AEVEDRTCDA APKFLNDLPD IQLNEHENIH VDLRATPVND PTMVIEWFVN
GRPLLTGSRV KTLNEFGFIA LDIKGAIAED SGTYSVRASN LLGEAIRQCV ITVTPAGQIL
SDTQHQESLG KINYLENLNK YGRVEIEDKG PQEPPTFVVP LQADLGDVEE GEPIHLECQV
NPINDNSLKI IWLRDGQSLP HGHRFRTFYD FGFVSLDILG FYAQDAGTYT CRAENSLGQA
ETVATIRCAP KDAILGAVQH PRSYARIQEI EAPKPAPQEV PDLPHQPPAF VKQLGPAIQC
MEGDNVYLEA QVTPTDDNSL TYEWLVNGQP LMKAHRFVLS QDFGYIALNI LYCYPEDNGT
YTLVVRNRAG EAQSTVDINC GHTGGNFTDS FHPNSLHRIA ELETPIQRAE PLPDKEKEVP
TIAKPLPATI DSVHESQTLH LEAQVTPIDD NTLRYEWLFN GNPLKASSRY RVLNDFGFVS
LDIDYIIAED SGKYTLVVYN SAGRAETSCE FQVDRLKSIL SDTAHPESLR RIREMEQLQP
AKPSDDDAAA QPPVFTQQLT GPTEPLKEGQ SVHMDCVVQP INDPSLRIEW FHDGRPLMFG
SRIRTIHDFG YVGLEFLHIH PEDTGTYTCK ATNLIGEATT DIFLECKPRR NIYLDTHHES
SWQKIQEIEN RVDEREPTPE LTFQPPTFTE NLADKEDAQE GQSIRLECRL IPVNDPTMRV
TWTRNGQPLP EASRFMPARN FDYVNLDILA LYGEDSGVYT CKAVSAFGEA ATSCTVKCAA
GKSLLLDTMH DASWKRVQEI ENREKLEAVD AEPEKTAPKF VTQLNSSLGE LQEGVPIHLE
AQVEPTNDNQ LTVQWFHNGQ PLANGHRFRT RHDFGYVALD ILYAFAQDTG EWACVARNSL
GEAQTIANFT VLPRGTIYTD SQHPESWQKI QVLEAPRAAA PEKPDAEHDA PQFIEPLDSI
DRMEFQSAHF QTKVTPQTDP NLRIQWFKDG QPLMNSNRFK LTTDFGYISL DIAHTVPEDS
GVYSVKASNA KGDAEVQAQL TVTGNAVILG DTQHEQSWQK IQLIEAPRAP GEEEPDVKHG
PPKFVTQLHS LDGVVEGQPS HFEAQFIPFS DPKTSVQWYL NGNPLSASSR RILRNDFGLV
SLDLQYTLGE DAGEYSVVVK NSEGEDRTSG QLSCTTRAAI LGDTQHEQSW QRIQEIEAPR
APGAEPEGPV YEKPSFVQPL QSVGDLPEGS VALLEARLVP VNDPNLRVQW FYNDQPLMES
NWISTSNDFG CVSLRIAPVY ARHTGVYSCK AWNDSGNAVT SANVGVQGSE GLLLDTSHPA
SLQKIQELEA IDKYARLDAP EREYEKPQWV QGFENYENVG EGQTVTLHGL VEPSGDPHLR
LEWLLNGTPL RNANRFRQEY EFGNAILTIV HVLPHDSGVY TCRAWNTQGE ASTSATVTTA
GYEKILYDSQ HPVSWERIQE LEAPKIVEEI EEIVQKEKPN FLTQLESAEN VPEGVPLHLE
STFQPARDPE LKVVWQKNGQ PLGASQLVQT KHELGWATLD ISSANEDHNG VYTLTITNSE
GEAVSTASIR VAGTGPILGN TRHEESWKRI QILEAPKEAE PEAPAPVYDH PAITTQIDDK
ECNEGDHVHF EALITPVNDP RLQVQWIRNG VPLAHGSKYA IQQDFGICTL DVAYTYPEDE
GVYQLRIWNP EGEAVSSATL KCHGKDAILG DVQHQESWKR IQEIEAPKQK LEEADPEPKG
PPRFIQQLTS PGSLVENQPA HFEATVEPVD DPTLTINWFL NGEPMSASSR VKMINDFGWV
IMDIAQTEPR DSGEWKCVAK NAAGEAVSTA TIEVQGKEVI LQDSLQPQSL DRIRQIEAGK
PAPEERPDQQ FEAPAIVNAL QVQGALEEGG SAHLQTQFTP VADPSIKVEW LKDGQPIFHS
NRYKMVHDFG FAVLDILHLL KHDAGEYTFR VSNNSGEAST STSFEVSESS GLILQPQNEQ
KAKAVEILED NLRRRPEEIE QELKEATPVF IEPLSAPVET EEGGRAHFTA RYEPVNDNQL
QVQWYHDGRP LKNGSRIKTI NSFGYVVLEI SPTYPEDNGE YICRAVNRVG EAVTSTKLTC
TPKEGIISAT QLPERMANAG RRIAEIEAPR PAREDAPDAD HGPPKFTSAL AGPPELQEGQ
QAHLECQVTP VADPRLVIEW FHNGQPVNHT NRMKAIHDFG FVVLQLTPAE PQDSGTWTCR
ATNQHGSDEV STELKVVGGG GVSYEWQSTA ERKERITELE DWIHRPKEDL NLPAVDYPAP
SFSQGLTDLG QLNEADATAF VCVLEPIGDP TLRVQWEHNG HPIPYSNRIS CTNEFGVATL
LIKHLIAADA GEYKCVATNV KGSATSVGKI AVESSTQIDA PQVVQQLVDS VENILEGDSI
HLECRVTPIN DPRLHVEWLR NGAPLPEASR FKPTFEFGFV SLDILYAYPE DNGDYELVVR
NDKGEARSKT KITVLPRPSL DYTSQTHGNQ QDSLESHFKQ HSQAKLQLTA NDIYNESDKR
APEFRTQLQN IGVLEGEFCR FETQVAPIND PYLKVEWFKD KKPVLLGHRF RSTLDFGFAC
LDLLYALPDD TGEYHCVATN RHGQTMISAK LACQGASHVI TDSQMPQGLR VSNVKKDNKN
IYWSEQGGAV QPKQKQAPQF TIPLRNLQVT ENQPARFECA VTGYPRPKVT WFINGNQCLH
GHRFKLNFDG LHYLTVSKSR ISDAGEVVAI ARNTEGETIS TATLDIFQND DFRQTKLRPA
NFKTSDELRE RELQWQRDTL GSLGPAFEAA PKPDAQKLMH VERAQSPIEP MESQELIQKF
TRPRDDNFYN KLSYVELQKP QFKGMELEEV NLKAGKVEKY QPPVEEMERV NLKAIPEKDQ
QEVGWERPDW AGQDGTSKLP GADEGRFKKL PTPAPELDVP ARDQVKLKTA KPTRGKDLEA
GEKVKLKTEK AKIKEIQQKP EQPKEEPIVH KDAVQLKTQQ LPKTGIKGDH FTVDREKDLK
ETPAVVKPVI EETRISNKSI SNVVHESSEY TSSYASNQSR LTYQAYREHK ESTSSDVYLS
VETADSFSQV QRLEYSPRSP RRERIIGFHM IRPQPTKIGQ SKQAPPTISQ QLKPLQGELG
KAAKFVIEFA GAAPVKVTWL KDGKEIKSTF RTLITTTPTN SSLHIGRLEN SHAGEYTVRL
ENAAGTVESL ANLTVAPPTT QGKAPDFSAR LNDLRIQQNG PAEFSCQIGG EPKPTIQWFK
DGQPLPNDDR FQVVEEGGAY KLKFSNIIST DAGIYEIVAK NGVGEARCKA RLNVNLQKTG
KGAEEGPRYE APRFTSQIQP IVVDEGKGAQ FSAQFSGFPD PTIRWYRNNE PVKHADGYEI
SQSKGEAILR ISAARNEDVA EYKVEASNPA GKASSVANLV LTPRSGRIAK STISRGGSAS
YQSSDKAAAD SPHFIAKLSD ISARQGHTVK FSAEVDGNPE PTVQWQFKGK PISASNNVKI
SRDGKRAILE LARVTPDSAG EYQIVIRNDK GAATSQAKLT LSR
