BLI4_CAEEL
ID BLI4_CAEEL Reviewed; 942 AA.
AC P51559; A0A0M7RDN9; A0A0M7RDU4; A0A0M7RE83; A0A0M7RFE9; G8JYA5; O44762;
AC O44763; O44764; O44765; O44766;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Endoprotease bli-4;
DE EC=3.4.21.- {ECO:0000303|PubMed:24013594};
DE AltName: Full=Blisterase;
DE AltName: Full=Blistered cuticle protein 4;
DE Flags: Precursor;
GN Name=bli-4; Synonyms=kpc-4; ORFNames=K04F10.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=7774813; DOI=10.1101/gad.9.8.956;
RA Thacker C., Peters K.W., Srayko M., Rose A.M.;
RT "The bli-4 locus of Caenorhabditis elegans encodes structurally distinct
RT kex2/subtilisin-like endoproteases essential for early development and
RT adult morphology.";
RL Genes Dev. 9:956-971(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 FUNCTION, ALTERNATIVE SPLICING, AND MUTAGENESIS OF HIS-127; GLY-307;
RP PRO-313; GLY-341; GLU-378 AND SER-415.
RX PubMed=10903434; DOI=10.1016/s0378-1119(00)00211-0;
RA Thacker C., Srayko M., Rose A.M.;
RT "Mutational analysis of bli-4/kpc-4 reveals critical residues required for
RT proprotein convertase function in C. elegans.";
RL Gene 252:15-25(2000).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19716386; DOI=10.1016/j.molbiopara.2009.08.005;
RA Stepek G., McCormack G., Page A.P.;
RT "The kunitz domain protein BLI-5 plays a functionally conserved role in
RT cuticle formation in a diverse range of nematodes.";
RL Mol. Biochem. Parasitol. 169:1-11(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24013594; DOI=10.1038/nn.3511;
RA Leinwand S.G., Chalasani S.H.;
RT "Neuropeptide signaling remodels chemosensory circuit composition in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 16:1461-1467(2013).
CC -!- FUNCTION: Serine endoprotease which cleaves proproteins at paired basic
CC amino acids (Probable). Involved in cuticle biosynthesis probably by
CC cleaving pro-collagen into its mature form. Acts in ASEL sensory
CC neurons to regulate high salt chemotaxis responses probably by cleaving
CC insulin-like protein ins-6 into its mature and active form
CC (PubMed:24013594). Essential for embryonic and larval development
CC (PubMed:7774813, PubMed:10903434, pubmed:19716386). isoform a, isoform
CC e, isoform f, isoform g and isoform h are involved in cuticle
CC biosynthesis but are dispensable for larval development
CC (PubMed:7774813, PubMed:10903434). {ECO:0000269|PubMed:10903434,
CC ECO:0000269|PubMed:19716386, ECO:0000269|PubMed:24013594,
CC ECO:0000269|PubMed:7774813, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P23188};
CC Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P23188};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=d {ECO:0000312|WormBase:K04F10.4d}; Synonyms=D
CC {ECO:0000303|PubMed:7774813};
CC IsoId=P51559-15; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K04F10.4a}; Synonyms=A
CC {ECO:0000303|PubMed:7774813};
CC IsoId=P51559-6; Sequence=VSP_058863, VSP_058866;
CC Name=b {ECO:0000312|WormBase:K04F10.4b}; Synonyms=B
CC {ECO:0000303|PubMed:7774813};
CC IsoId=P51559-7; Sequence=VSP_058859, VSP_058870;
CC Name=c {ECO:0000312|WormBase:K04F10.4c}; Synonyms=C
CC {ECO:0000303|PubMed:7774813};
CC IsoId=P51559-8; Sequence=VSP_058873, VSP_058874;
CC Name=e {ECO:0000312|WormBase:K04F10.4e};
CC IsoId=P51559-9; Sequence=VSP_058860, VSP_058869;
CC Name=f {ECO:0000312|WormBase:K04F10.4f};
CC IsoId=P51559-10; Sequence=VSP_058864, VSP_058865;
CC Name=g {ECO:0000312|WormBase:K04F10.4g};
CC IsoId=P51559-11; Sequence=VSP_058858, VSP_058871;
CC Name=h {ECO:0000312|WormBase:K04F10.4h};
CC IsoId=P51559-12; Sequence=VSP_058857, VSP_058872;
CC Name=i {ECO:0000312|WormBase:K04F10.4i};
CC IsoId=P51559-13; Sequence=VSP_058861, VSP_058868;
CC Name=j {ECO:0000312|WormBase:K04F10.4j};
CC IsoId=P51559-14; Sequence=VSP_058862, VSP_058867;
CC -!- TISSUE SPECIFICITY: In larvae and adults, expressed in all hypodermal
CC cells, vulva and ventral nerve cords. {ECO:0000269|PubMed:7774813}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at the two-fold embryonic stage
CC throughout adulthood (PubMed:7774813, PubMed:19716386). Expression
CC increases during L2-L3, L3-L4 and L4-adult molting stages
CC (PubMed:19716386). {ECO:0000269|PubMed:19716386,
CC ECO:0000269|PubMed:7774813}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes an arrest at the
CC L1 developmental stage (PubMed:19716386). RNAi-mediated knockdown in
CC ASEL neuron results in a severe reduction in Ca(2+) signal in ASEL
CC neuron and in chemotaxis in response to high salt concentrations
CC (PubMed:24013594). {ECO:0000269|PubMed:19716386,
CC ECO:0000269|PubMed:24013594}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98750.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA98751.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L29438; AAA98750.1; ALT_FRAME; mRNA.
DR EMBL; L29439; AAA98751.1; ALT_FRAME; mRNA.
DR EMBL; L29440; AAA98752.1; -; mRNA.
DR EMBL; BX284601; CCD70035.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70036.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70037.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70038.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70039.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD70040.1; -; Genomic_DNA.
DR EMBL; BX284601; CUR29975.1; -; Genomic_DNA.
DR EMBL; BX284601; CUR29976.1; -; Genomic_DNA.
DR EMBL; BX284601; CUR29977.1; -; Genomic_DNA.
DR EMBL; BX284601; CUR29978.1; -; Genomic_DNA.
DR PIR; D87803; D87803.
DR PIR; E87803; E87803.
DR PIR; F87803; F87803.
DR PIR; T37314; T37314.
DR RefSeq; NP_001021540.1; NM_001026369.3. [P51559-6]
DR RefSeq; NP_001021541.1; NM_001026370.3.
DR RefSeq; NP_001021542.1; NM_001026371.3.
DR RefSeq; NP_001021543.1; NM_001026372.5. [P51559-15]
DR RefSeq; NP_001021544.2; NM_001026373.4.
DR RefSeq; NP_001021545.1; NM_001026374.3.
DR RefSeq; NP_001303778.1; NM_001316849.1. [P51559-11]
DR RefSeq; NP_001303779.1; NM_001316850.1. [P51559-12]
DR RefSeq; NP_001303780.1; NM_001316851.1.
DR RefSeq; NP_001303781.1; NM_001316852.1. [P51559-14]
DR AlphaFoldDB; P51559; -.
DR SMR; P51559; -.
DR BioGRID; 37786; 1.
DR IntAct; P51559; 1.
DR STRING; 6239.K04F10.4d.1; -.
DR MEROPS; S08.031; -.
DR PaxDb; P51559; -.
DR PeptideAtlas; P51559; -.
DR EnsemblMetazoa; K04F10.4a.1; K04F10.4a.1; WBGene00000254. [P51559-6]
DR EnsemblMetazoa; K04F10.4b.1; K04F10.4b.1; WBGene00000254. [P51559-7]
DR EnsemblMetazoa; K04F10.4c.1; K04F10.4c.1; WBGene00000254. [P51559-8]
DR EnsemblMetazoa; K04F10.4d.1; K04F10.4d.1; WBGene00000254. [P51559-15]
DR EnsemblMetazoa; K04F10.4d.2; K04F10.4d.2; WBGene00000254. [P51559-15]
DR EnsemblMetazoa; K04F10.4e.1; K04F10.4e.1; WBGene00000254. [P51559-9]
DR EnsemblMetazoa; K04F10.4f.1; K04F10.4f.1; WBGene00000254. [P51559-10]
DR EnsemblMetazoa; K04F10.4g.1; K04F10.4g.1; WBGene00000254. [P51559-11]
DR EnsemblMetazoa; K04F10.4h.1; K04F10.4h.1; WBGene00000254. [P51559-12]
DR EnsemblMetazoa; K04F10.4i.1; K04F10.4i.1; WBGene00000254. [P51559-13]
DR EnsemblMetazoa; K04F10.4j.1; K04F10.4j.1; WBGene00000254. [P51559-14]
DR GeneID; 172333; -.
DR KEGG; cel:CELE_K04F10.4; -.
DR UCSC; K04F10.4f; c. elegans. [P51559-15]
DR CTD; 172333; -.
DR WormBase; K04F10.4a; CE11728; WBGene00000254; bli-4. [P51559-6]
DR WormBase; K04F10.4b; CE11730; WBGene00000254; bli-4. [P51559-7]
DR WormBase; K04F10.4c; CE11732; WBGene00000254; bli-4. [P51559-8]
DR WormBase; K04F10.4d; CE11734; WBGene00000254; bli-4. [P51559-15]
DR WormBase; K04F10.4e; CE51144; WBGene00000254; bli-4. [P51559-9]
DR WormBase; K04F10.4f; CE33136; WBGene00000254; bli-4. [P51559-10]
DR WormBase; K04F10.4g; CE51093; WBGene00000254; bli-4. [P51559-11]
DR WormBase; K04F10.4h; CE51059; WBGene00000254; bli-4. [P51559-12]
DR WormBase; K04F10.4i; CE51132; WBGene00000254; bli-4. [P51559-13]
DR WormBase; K04F10.4j; CE51107; WBGene00000254; bli-4. [P51559-14]
DR eggNOG; KOG3525; Eukaryota.
DR InParanoid; P51559; -.
DR OMA; FHDWSLL; -.
DR OrthoDB; 518530at2759; -.
DR PhylomeDB; P51559; -.
DR Reactome; R-CEL-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CEL-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR PRO; PR:P51559; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000254; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:1902075; P:cellular response to salt; IMP:UniProtKB.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd00064; FU; 3.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00261; FU; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding; Protease;
KW Reference proteome; Repeat; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..116
FT /evidence="ECO:0000250|UniProtKB:P29122"
FT /id="PRO_0000439500"
FT CHAIN 117..942
FT /note="Endoprotease bli-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026997"
FT TOPO_DOM 117..871
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 893..942
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 168..483
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 491..629
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REPEAT 674..723
FT /note="FU 1"
FT /evidence="ECO:0000255"
FT REPEAT 725..777
FT /note="FU 2"
FT /evidence="ECO:0000255"
FT REPEAT 804..850
FT /note="FU 3"
FT /evidence="ECO:0000255"
FT REGION 130..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 415
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 300..305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 339..342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT SITE 116..117
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P29122"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 868
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 258..407
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 350..380
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 498..527
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT VAR_SEQ 658..746
FT /note="VEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSG
FT FKCVQKCDDTYYLDGDKCKMCSSHCHTCTKAEVCETC -> IGMPSVLVVIQIIVICLV
FT LGVGLYACRRQQVQDSTVGAPTPSAPEDVAMTSLSPRESEDEQLRKAIAASIEEEAERK
FT MIERALSDAEKL (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_058857"
FT VAR_SEQ 658..735
FT /note="VEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSG
FT FKCVQKCDDTYYLDGDKCKMCSSHCH -> KRTFSKRPQAFSRVRQMPIPSGVTQQRQW
FT VPQRPQPQSVFQQATFGQWVWDPVSQRWVWSRRIRKHQPEPVHRRRYKH (in
FT isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_058858"
FT VAR_SEQ 658..730
FT /note="VEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSG
FT FKCVQKCDDTYYLDGDKCKMC -> GDEVVERIRNHWEVTLEESSHWNWEHAREHKSLQ
FT ELNSSSRTHSFLYSFTKFQPIFLIILVCIFDAIHRQFAV (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058859"
FT VAR_SEQ 658..724
FT /note="VEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSG
FT FKCVQKCDDTYYLDG -> NEPLLRIASSQHYRLSPSSIHQSLLPFAQFSNSYPTPPPF
FT YQSTSNHRPTYIYLPRPRRFLLTNQLI (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058860"
FT VAR_SEQ 658..716
FT /note="VEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSG
FT FKCVQKC -> STKNGGNETLLVDFSKGEKSISPWTFSSYQTGIANLKNYFDQFFMKMF
FT GGTPGVNRPWR (in isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_058861"
FT VAR_SEQ 658..672
FT /note="VEESAPISFPDLTSA -> QVRKSSARYIQRAFP (in isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_058862"
FT VAR_SEQ 658..670
FT /note="VEESAPISFPDLT -> ILITIAIHLVVNA (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058863"
FT VAR_SEQ 659..666
FT /note="EESAPISF -> RTFFGGFG (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_058864"
FT VAR_SEQ 667..942
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_058865"
FT VAR_SEQ 671..942
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058866"
FT VAR_SEQ 673..942
FT /note="Missing (in isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_058867"
FT VAR_SEQ 717..942
FT /note="Missing (in isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_058868"
FT VAR_SEQ 725..942
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_058869"
FT VAR_SEQ 731..942
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058870"
FT VAR_SEQ 736..942
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_058871"
FT VAR_SEQ 747..942
FT /note="Missing (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_058872"
FT VAR_SEQ 779..827
FT /note="ESNLVQAKCIWRKDLCGDGYYINAVGKCDLCDSSCETCTAPGPMSCEKC ->
FT AENFDFCAKNNESGRDTTVFVKFKKPSAFKDYCNLKLVDLDFFIFSLLF (in
FT isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058873"
FT VAR_SEQ 828..942
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058874"
FT MUTAGEN 127
FT /note="H->L: No visible phenotype."
FT /evidence="ECO:0000269|PubMed:10903434"
FT MUTAGEN 307
FT /note="G->E: In h254; lethal at late embryonic stage."
FT /evidence="ECO:0000269|PubMed:10903434"
FT MUTAGEN 313
FT /note="P->L: In h520; lethal at late embryonic stage."
FT /evidence="ECO:0000269|PubMed:10903434"
FT MUTAGEN 341
FT /note="G->E: In h427; lethal at late embryonic stage."
FT /evidence="ECO:0000269|PubMed:10903434"
FT MUTAGEN 378
FT /note="E->K: In h42; lethal at late embryonic stage."
FT /evidence="ECO:0000269|PubMed:10903434"
FT MUTAGEN 415
FT /note="S->E: In h384; probably catalytically inactive.
FT Lethal at late embryonic stage."
FT /evidence="ECO:0000269|PubMed:10903434"
FT CONFLICT 153
FT /note="R -> A (in Ref. 1; AAA98750/AAA98751)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="R -> S (in Ref. 1; AAA98750/AAA98751)"
FT /evidence="ECO:0000305"
FT CONFLICT 663..664
FT /note="PI -> RS (in Ref. 1; AAA98752)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..676
FT /note="AGNCH -> GWKLSC (in Ref. 1; AAA98752)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="C -> Y (in Ref. 1; AAA98752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 103015 MW; C92C40993FECCC12 CRC64;
MRISIGRIAW QILAVLIAVA FTIEHDSICD ESIGACGEPI HTVIRLAKRD DELARRIAAD
HDMHVKGDPF LDTHYFLYHS ETTRTRRHKR AIVERLDSHP AVEWVEEQRP KKRVKRDYIL
LDNDVHHSNP FRRSVLNRDG TRRAQRQQPQ SPREIPSLPF PDPLYKDQWY LHGGAVGGYD
MNVRQAWLQG YAGRNVSVSI LDDGIQRDHP DLAANYDPLA STDINDHDDD PTPQNNGDNK
HGTRCAGEVA ALAGNNQCGV GVAFKAKIGG VRMLDGAVSD SVEAASLSLN QDHIDIYSAS
WGPEDDGKTF DGPGPLAREA FYRGIKNGRG GKGNIFVWAS GNGGSRQDSC SADGYTTSVY
TLSISSATYD NHRPWYLEEC PSSIATTYSS ADFRQPAIVT VDVPGGCTDK HTGTSASAPL
AAGIIALALE ANPELTWRDM QHLVLRTANW KPLENNPGWS RNGVGRMVSN KFGYGLIDGG
ALVNMAKTWK TVPEQHICTY EYRLANPNPR PIVGRFQLNF TLDVNGCESG TPVLYLEHVQ
VHATVRYLKR GDLKLTLFSP SGTRSVLLPP RPQDFNANGF HKWPFLSVQQ WGEDPRGTWL
LMVESVTTNP AATGTFHDWT LLLYGTADPA QSGDPVYSAT PATSQGVLSR VHQLTSQVEE
SAPISFPDLT SAGNCHDECN GGCTESSSAT SCFACKHLTQ TLRNKGGSGF KCVQKCDDTY
YLDGDKCKMC SSHCHTCTKA EVCETCPGSL LLIDVDNMPH YDHGKCVESC PPGLVADYES
NLVQAKCIWR KDLCGDGYYI NAVGKCDLCD SSCETCTAPG PMSCEKCSKG YGKGSIGYCR
PCCPEGSTKS WQCEDCSKPD PTLLIDSNKS SGFGLMFWIV VSLIAACGIC ACKKCASETK
SSNVEYAPLA QYNATNGAIN LGAHTDDEDD DEDEVFVNPQ IV
