NEC2_CAEEL
ID NEC2_CAEEL Reviewed; 652 AA.
AC G5ECN9; E9P883; Q18772;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Neuroendocrine convertase 2 {ECO:0000250|UniProtKB:P16519};
DE Short=NEC 2 {ECO:0000250|UniProtKB:P16519};
DE EC=3.4.21.94 {ECO:0000305|PubMed:12657671, ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111, ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950};
DE AltName: Full=Egg-laying defective protein 3 {ECO:0000303|PubMed:11813735};
DE AltName: Full=Kex2-like prohormone convertase 2 {ECO:0000303|PubMed:7954663};
DE Short=CELPC2 {ECO:0000303|PubMed:7954663};
DE AltName: Full=Prohormone convertase 2 {ECO:0000250|UniProtKB:P16519};
DE Short=PC2 {ECO:0000303|PubMed:11717360};
DE AltName: Full=Proprotein convertase 2 {ECO:0000303|PubMed:11717360};
DE Flags: Precursor;
GN Name=egl-3 {ECO:0000312|WormBase:C51E3.7a};
GN Synonyms=kpc-2 {ECO:0000312|WormBase:C51E3.7a};
GN ORFNames=C51E3.7 {ECO:0000312|WormBase:C51E3.7a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAA56868.1};
RN [1] {ECO:0000312|EMBL:AAA56868.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND TISSUE SPECIFICITY.
RC STRAIN=BA713 {ECO:0000312|EMBL:AAA56868.1};
RX PubMed=7954663; DOI=10.1007/bf02088586;
RA Gomez-Saladin E., Wilson D.L., Dickerson I.M.;
RT "Isolation and in situ localization of a cDNA encoding a Kex2-like
RT prohormone convertase in the nematode Caenorhabditis elegans.";
RL Cell. Mol. Neurobiol. 14:9-25(1994).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLU-117; GLY-176; CYS-496 AND GLY-594.
RX PubMed=11813735; DOI=10.1093/genetics/104.4.619;
RA Trent C., Tsuing N., Horvitz H.R.;
RT "Egg-laying defective mutants of the nematode Caenorhabditis elegans.";
RL Genetics 104:619-647(1983).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-594 AND GLY-621.
RX PubMed=11717360; DOI=10.1523/jneurosci.21-23-09265.2001;
RA Kass J., Jacob T.C., Kim P., Kaplan J.M.;
RT "The EGL-3 proprotein convertase regulates mechanosensory responses of
RT Caenorhabditis elegans.";
RL J. Neurosci. 21:9265-9272(2001).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF GLY-621.
RX PubMed=12657671; DOI=10.1523/jneurosci.23-06-02122.2003;
RA Jacob T.C., Kaplan J.M.;
RT "The EGL-21 carboxypeptidase E facilitates acetylcholine release at
RT Caenorhabditis elegans neuromuscular junctions.";
RL J. Neurosci. 23:2122-2130(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15180830; DOI=10.1111/j.1600-0854.2004.00195.x;
RA Zahn T.R., Angleson J.K., MacMorris M.A., Domke E., Hutton J.F.,
RA Schwartz C., Hutton J.C.;
RT "Dense core vesicle dynamics in Caenorhabditis elegans neurons and the role
RT of kinesin UNC-104.";
RL Traffic 5:544-559(2004).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-117; GLY-176 AND
RP GLY-594.
RX PubMed=16945111; DOI=10.1111/j.1471-4159.2006.04014.x;
RA Husson S.J., Clynen E., Baggerman G., Janssen T., Schoofs L.;
RT "Defective processing of neuropeptide precursors in Caenorhabditis elegans
RT lacking proprotein convertase 2 (KPC-2/EGL-3): mutant analysis by mass
RT spectrometry.";
RL J. Neurochem. 98:1999-2012(2006).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=17564681; DOI=10.1111/j.1471-4159.2007.04474.x;
RA Husson S.J., Janssen T., Baggerman G., Bogert B., Kahn-Kirby A.H.,
RA Ashrafi K., Schoofs L.;
RT "Impaired processing of FLP and NLP peptides in carboxypeptidase E (EGL-
RT 21)-deficient Caenorhabditis elegans as analyzed by mass spectrometry.";
RL J. Neurochem. 102:246-260(2007).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA Liu T., Kim K., Li C., Barr M.M.;
RT "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT regulate male sexual turning behavior in Caenorhabditis elegans.";
RL J. Neurosci. 27:7174-7182(2007).
RN [10] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH FSN-1, UBIQUITINATION, AND
RP REGION.
RX PubMed=23665919; DOI=10.1038/emboj.2013.91;
RA Hung W.L., Hwang C., Gao S., Liao E.H., Chitturi J., Wang Y., Li H.,
RA Stigloher C., Bessereau J.L., Zhen M.;
RT "Attenuation of insulin signalling contributes to FSN-1-mediated regulation
RT of synapse development.";
RL EMBO J. 32:1745-1760(2013).
RN [11] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF CYS-496.
RX PubMed=23658528; DOI=10.1371/journal.pgen.1003472;
RA Stawicki T.M., Takayanagi-Kiya S., Zhou K., Jin Y.;
RT "Neuropeptides function in a homeostatic manner to modulate excitation-
RT inhibition imbalance in C. elegans.";
RL PLoS Genet. 9:E1003472-E1003472(2013).
RN [12] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24671950; DOI=10.1242/dev.103846;
RA Hung W.L., Wang Y., Chitturi J., Zhen M.;
RT "A Caenorhabditis elegans developmental decision requires insulin
RT signaling-mediated neuron-intestine communication.";
RL Development 141:1767-1779(2014).
CC -!- FUNCTION: Serine endoprotease which cleaves preproteins at paired basic
CC amino acids (PubMed:12657671, PubMed:15180830, PubMed:16945111,
CC PubMed:23665919, PubMed:24671950). Processes FMRFamide-like (flp) and
CC neuropeptide-like protein (nlp) neuropeptides (PubMed:12657671,
CC PubMed:16945111). Probably by processing flp-1 and flp-18, modulates
CC the neuronal excitation-inhibition balance and thus the level of
CC activity of the locomotor circuit (PubMed:23658528). Regulates
CC sensitivity to mechanosensory stimuli (PubMed:11717360). By processing
CC neuropeptides, modulates basal acetylcholine release at the ventral
CC cord neuromuscular junctions (PubMed:12657671). Probably by processing
CC flp neuropeptides, regulates the turning step of male mating behavior
CC (PubMed:17611271). Cleaves pro-insulin-like proteins ins-3, ins-4 and
CC ins-6 into their mature active forms (PubMed:23665919,
CC PubMed:24671950). Together with convertase kpc-1, cleaves pro-insulin-
CC like protein ins-18 (PubMed:24671950). By controlling ins-4 and ins-6
CC processing and thus the activation of the daf-2/InsR pathway,
CC negatively modulates synapse development and synaptic transmission at
CC neuromuscular junctions (PubMed:23665919). Similarly, by controlling
CC ins-4 and ins-6 processing, negatively regulates dauer formation under
CC optimal environmental conditions (PubMed:24671950). Under adverse
CC environmental conditions, may promote dauer formation by processing
CC ins-18, a daf-2/InsR antagonist (PubMed:24671950). May cleave dense-
CC core vesicle membrane protein ida-1 (PubMed:15180830). Involved in egg-
CC laying, fat storage and locomotion (PubMed:11813735, PubMed:11717360,
CC PubMed:17564681). {ECO:0000269|PubMed:11717360,
CC ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671,
CC ECO:0000269|PubMed:15180830, ECO:0000269|PubMed:16945111,
CC ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:23658528, ECO:0000269|PubMed:23665919,
CC ECO:0000269|PubMed:24671950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of protein hormones and neuropeptides from their
CC precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC EC=3.4.21.94; Evidence={ECO:0000303|PubMed:12657671,
CC ECO:0000305|PubMed:15180830, ECO:0000305|PubMed:16945111,
CC ECO:0000305|PubMed:23665919, ECO:0000305|PubMed:24671950};
CC -!- SUBUNIT: Interacts (via C-terminus) with F-box protein fsn-1 (via SPRY
CC domain); the interaction results in egl-3 proteasomal degradation.
CC {ECO:0000269|PubMed:23665919}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671}. Cytoplasmic
CC vesicle, secretory vesicle lumen {ECO:0000303|PubMed:11717360}.
CC Secreted {ECO:0000303|PubMed:24671950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:C51E3.7a};
CC IsoId=G5ECN9-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C51E3.7b};
CC IsoId=G5ECN9-2; Sequence=VSP_058830;
CC Name=c {ECO:0000312|WormBase:C51E3.7c};
CC IsoId=G5ECN9-3; Sequence=VSP_058829;
CC -!- TISSUE SPECIFICITY: Expressed in head and tail ganglia (PubMed:7954663,
CC PubMed:11717360, PubMed:12657671, PubMed:24671950). Expressed in
CC neurons including mechanosensory and motor neurons, and interneurons
CC (at protein level) (PubMed:11717360, PubMed:12657671). Expressed in the
CC nerve ring, ventral nerve cord and intestine (PubMed:24671950).
CC {ECO:0000269|PubMed:11717360, ECO:0000269|PubMed:12657671,
CC ECO:0000269|PubMed:24671950, ECO:0000269|PubMed:7954663}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:23665919}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; U04995; AAA56868.1; -; mRNA.
DR EMBL; BX284605; CAB01635.1; -; Genomic_DNA.
DR EMBL; BX284605; CAB01642.1; -; Genomic_DNA.
DR EMBL; BX284605; CBZ01786.1; -; Genomic_DNA.
DR PIR; C89181; C89181.
DR PIR; T20131; T20131.
DR RefSeq; NP_001023732.1; NM_001028561.3. [G5ECN9-1]
DR RefSeq; NP_001256192.1; NM_001269263.1. [G5ECN9-3]
DR RefSeq; NP_505614.3; NM_073213.6.
DR AlphaFoldDB; G5ECN9; -.
DR SMR; G5ECN9; -.
DR STRING; 6239.C51E3.7a; -.
DR MEROPS; S08.109; -.
DR EPD; G5ECN9; -.
DR PaxDb; G5ECN9; -.
DR PeptideAtlas; G5ECN9; -.
DR EnsemblMetazoa; C51E3.7a.1; C51E3.7a.1; WBGene00001172. [G5ECN9-1]
DR EnsemblMetazoa; C51E3.7c.1; C51E3.7c.1; WBGene00001172. [G5ECN9-3]
DR GeneID; 179412; -.
DR KEGG; cel:CELE_C51E3.7; -.
DR CTD; 179412; -.
DR WormBase; C51E3.7a; CE08940; WBGene00001172; egl-3. [G5ECN9-1]
DR WormBase; C51E3.7b; CE08941; WBGene00001172; egl-3. [G5ECN9-2]
DR WormBase; C51E3.7c; CE45708; WBGene00001172; egl-3. [G5ECN9-3]
DR eggNOG; KOG3526; Eukaryota.
DR GeneTree; ENSGT00940000156965; -.
DR InParanoid; G5ECN9; -.
DR OMA; PFMTDVI; -.
DR OrthoDB; 308083at2759; -.
DR PhylomeDB; G5ECN9; -.
DR PRO; PR:G5ECN9; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001172; Expressed in larva and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0098770; F:FBXO family protein binding; IPI:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0090474; P:arg-arg specific dibasic protein processing; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
DR GO; GO:0090472; P:dibasic protein processing; IMP:UniProtKB.
DR GO; GO:0030070; P:insulin processing; IMP:UniProtKB.
DR GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR GO; GO:1905910; P:negative regulation of dauer entry; IGI:UniProtKB.
DR GO; GO:1904810; P:negative regulation of dense core granule transport; IMP:UniProtKB.
DR GO; GO:0061096; P:negative regulation of turning behavior involved in mating; IMP:WormBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IGI:UniProtKB.
DR GO; GO:0061837; P:neuropeptide processing; IMP:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:UniProtKB.
DR GO; GO:1905852; P:positive regulation of backward locomotion; IGI:UniProtKB.
DR GO; GO:0060456; P:positive regulation of digestive system process; IMP:UniProtKB.
DR GO; GO:1905850; P:positive regulation of forward locomotion; IMP:UniProtKB.
DR GO; GO:1905954; P:positive regulation of lipid localization; IMP:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
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 GO; GO:0043058; P:regulation of backward locomotion; IGI:UniProtKB.
DR GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:UniProtKB.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:UniProtKB.
DR GO; GO:1904014; P:response to serotonin; IMP:UniProtKB.
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; IPR008979; Galactose-bd-like_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 SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 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; Cell projection; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Ubl conjugation;
KW Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..107
FT /evidence="ECO:0000255"
FT /id="PRO_0000439343"
FT CHAIN 108..652
FT /note="Neuroendocrine convertase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5008958380"
FT DOMAIN 136..481
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 501..652
FT /note="Required for ubiquitination-mediated degradation"
FT /evidence="ECO:0000269|PubMed:23665919"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 390
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 232..382
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 324..354
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 496..522
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058829"
FT VAR_SEQ 93..188
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058830"
FT MUTAGEN 117
FT /note="E->Q: In n588; loss of nlp and flp neuropeptide
FT production. Egg-laying defects characterized by egg
FT retention and resistance to serotonin and imipramine-
FT induced egg-laying. Coiling behavior."
FT /evidence="ECO:0000269|PubMed:11813735,
FT ECO:0000269|PubMed:16945111"
FT MUTAGEN 176
FT /note="G->E: In n729; loss of nlp and flp neuropeptide
FT production. Egg-laying defects characterized by egg
FT retention and resistance to serotonin and imipramine-
FT induced egg-laying. Coiling behavior."
FT /evidence="ECO:0000269|PubMed:11813735,
FT ECO:0000269|PubMed:16945111"
FT MUTAGEN 496
FT /note="C->Y: In n589; temperature-sensitive mutant. Egg-
FT laying defects characterized by egg retention and
FT resistance to serotonin and imipramine-induced egg-laying.
FT Coiling behavior. Increases spontaneous convulsions in an
FT acr-2 n2420 mutant background."
FT /evidence="ECO:0000269|PubMed:11813735,
FT ECO:0000269|PubMed:23658528"
FT MUTAGEN 594
FT /note="G->E: In n150; temperature-sensitive mutant. Loss of
FT nlp and flp neuropeptide production. Egg-laying defects
FT characterized by egg retention and resistance to serotonin
FT and imipramine-induced egg-laying. Restores sensitivity to
FT nose touch in a glr-1 n2461 mutant background."
FT /evidence="ECO:0000269|PubMed:11717360,
FT ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:16945111"
FT MUTAGEN 621
FT /note="G->R: In nu349; egg-laying defects characterized by
FT egg retention and resistance to serotonin and imipramine-
FT induced egg-laying. Loss of localization to secretory
FT vesicles in axons. Loss of FMRFamide-like peptide (FaRP)
FT production in neurons. Resistance to acetylcholine esterase
FT inhibitor aldicarb-induced paralysis. Insensitive to body
FT touch but not to nose touch. Restores sensitivity to nose
FT touch, high osmolarity and volatile repellents in a glr-1
FT n2461 or lin-10 n1508 mutant background."
FT /evidence="ECO:0000269|PubMed:11717360,
FT ECO:0000269|PubMed:12657671"
SQ SEQUENCE 652 AA; 72046 MW; 39E378E75C081A2B CRC64;
MKNTHVDLIC VFLSIFIGIG EAVDVYTNHF HVHLKEGGGL EDAHRIAKRH GFINRGQVAA
SDNEYHFVQP ALVHARTRRS AGHHAKLHND DEVLHVEQLK GYTRTKRGYR PLEQRLESQF
DFSAVMSPSD PLYGYQWYLK NTGQAGGKAR LDLNVERAWA MGFTGKNITT AIMDDGVDYM
HPDIKNNFNA EASYDFSSND PFPYPRYTDD WFNSHGTRCA GEIVAARDNG VCGVGVAYDG
KVAGIRMLDQ PYMTDLIEAN SMGHEPSKIH IYSASWGPTD DGKTVDGPRN ATMRAIVRGV
NEGRNGLGSI FVWASGDGGE DDDCNCDGYA ASMWTISINS AINNGENAHY DESCSSTLAS
TFSNGGRNPE TGVATTDLYG RCTRSHSGTS AAAPEAAGVF ALALEANPSL TWRDLQHLTV
LTSSRNSLFD GRCRDFPSLG INDNHRDSHG NCSHFEWQMN GVGLEYNHLF GFGVLDAAEM
VMLAMAWKTS PPRYHCTAGL IDTPHEIPAD GNLILEINTD GCAGSQFEVR YLEHVQAVVS
FNSTRRGDTT LYLISPMGTR TMILSRRPKD DDSKDGFTNW PFMTTHTWGE NPTGKWRLVA
RFQGPGAHAG TLKKFELMLH GTREAPYNLI EPIVGQTNKK LDTVQKAHKR SH
