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Protein

Neuroendocrine convertase 2

Gene

egl-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine endoprotease which cleaves preproteins at paired basic amino acids (PubMed:12657671, PubMed:15180830, PubMed:16945111, PubMed:23665919, PubMed:24671950). Processes FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides (PubMed:12657671, PubMed:16945111). Probably by processing flp-1 and flp-18, modulates the neuronal excitation-inhibition balance and thus the level of activity of the locomotor circuit (PubMed:23658528). Regulates sensitivity to mechanosensory stimuli (PubMed:11717360). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671). Probably by processing flp neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Cleaves pro-insulin-like proteins ins-3, ins-4 and ins-6 into their mature active forms (PubMed:23665919, PubMed:24671950). Together with convertase kpc-1, cleaves pro-insulin-like protein ins-18 (PubMed:24671950). By controlling ins-4 and ins-6 processing and thus the activation of the daf-2/InsR pathway, negatively modulates synapse development and synaptic transmission at neuromuscular junctions (PubMed:23665919). Similarly, by controlling ins-4 and ins-6 processing, negatively regulates dauer formation under optimal environmental conditions (PubMed:24671950). Under adverse environmental conditions, may promote dauer formation by processing ins-18, a daf-2/InsR antagonist (PubMed:24671950). May cleave dense-core vesicle membrane protein ida-1 (PubMed:15180830). Involved in egg-laying, fat storage and locomotion (PubMed:11813735, PubMed:11717360, PubMed:17564681).10 Publications

Catalytic activityi

Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.1 Publication4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei174Charge relay systemPROSITE-ProRule annotation1
Active sitei215Charge relay systemPROSITE-ProRule annotation1
Active sitei390Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

  • FBXO family protein binding Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • arg-arg specific dibasic protein processing Source: UniProtKB
  • determination of adult lifespan Source: UniProtKB
  • dibasic protein processing Source: UniProtKB
  • insulin processing Source: UniProtKB
  • larval feeding behavior Source: UniProtKB
  • negative regulation of dauer entry Source: UniProtKB
  • negative regulation of dense core granule transport Source: UniProtKB
  • negative regulation of turning behavior involved in mating Source: WormBase
  • neuromuscular synaptic transmission Source: UniProtKB
  • neuropeptide processing Source: UniProtKB
  • positive regulation of acetylcholine secretion, neurotransmission Source: UniProtKB
  • positive regulation of backward locomotion Source: UniProtKB
  • positive regulation of digestive system process Source: UniProtKB
  • positive regulation of forward locomotion Source: UniProtKB
  • positive regulation of lipid localization Source: UniProtKB
  • positive regulation of locomotion involved in locomotory behavior Source: UniProtKB
  • positive regulation of oviposition Source: UniProtKB
  • positive regulation of synaptic growth at neuromuscular junction Source: UniProtKB
  • regulation of backward locomotion Source: UniProtKB
  • regulation of eating behavior Source: UniProtKB
  • regulation of locomotion involved in locomotory behavior Source: WormBase
  • regulation of muscle contraction Source: UniProtKB
  • regulation of neuromuscular synaptic transmission Source: UniProtKB
  • regulation of synaptic growth at neuromuscular junction Source: UniProtKB
  • response to mechanical stimulus Source: UniProtKB
  • response to serotonin Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Serine protease

Enzyme and pathway databases

SignaLinkiQ18772.

Protein family/group databases

MEROPSiS08.109.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroendocrine convertase 2By similarity (EC:3.4.21.945 Publications)
Short name:
NEC 2By similarity
Alternative name(s):
Egg-laying defective protein 31 Publication
Kex2-like prohormone convertase 21 Publication
Short name:
CELPC21 Publication
Prohormone convertase 2By similarity
Short name:
PC21 Publication
Proprotein convertase 21 Publication
Gene namesi
Name:egl-3Imported
Synonyms:kpc-2Imported
ORF Names:C51E3.7Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiC51E3.7a; CE08940; WBGene00001172; egl-3.
C51E3.7b; CE08941; WBGene00001172; egl-3.
C51E3.7c; CE45708; WBGene00001172; egl-3.

Subcellular locationi

  • Cell projectionaxon 2 Publications
  • Cytoplasmic vesiclesecretory vesicle lumen 1 Publication
  • Secreted 1 Publication

GO - Cellular componenti

  • axon Source: WormBase
  • cytoplasmic vesicle Source: UniProtKB-KW
  • extracellular region Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell projection, Cytoplasmic vesicle, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117E → Q in n588; loss of nlp and flp neuropeptide production. Egg-laying defects characterized by egg retention and resistance to serotonin and imipramine-induced egg-laying. Coiling behavior. 2 Publications1
Mutagenesisi176G → E in n729; loss of nlp and flp neuropeptide production. Egg-laying defects characterized by egg retention and resistance to serotonin and imipramine-induced egg-laying. Coiling behavior. 2 Publications1
Mutagenesisi496C → Y in n589; temperature-sensitive mutant. Egg-laying defects characterized by egg retention and resistance to serotonin and imipramine-induced egg-laying. Coiling behavior. Increases spontaneous convulsions in an acr-2 n2420 mutant background. 2 Publications1
Mutagenesisi594G → E in n150; temperature-sensitive mutant. Loss of nlp and flp neuropeptide production. Egg-laying defects characterized by egg retention and resistance to serotonin and imipramine-induced egg-laying. Restores sensitivity to nose touch in a glr-1 n2461 mutant background. 3 Publications1
Mutagenesisi621G → R in nu349; egg-laying defects characterized by egg retention and resistance to serotonin and imipramine-induced egg-laying. Loss of localization to secretory vesicles in axons. Loss of FMRFamide-like peptide (FaRP) production in neurons. Resistance to acetylcholine esterase inhibitor aldicarb-induced paralysis. Insensitive to body touch but not to nose touch. Restores sensitivity to nose touch, high osmolarity and volatile repellents in a glr-1 n2461 or lin-10 n1508 mutant background. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000043934323 – 107Sequence analysisAdd BLAST85
ChainiPRO_5008958380108 – 652Neuroendocrine convertase 2Sequence analysisAdd BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi167N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi232 ↔ 382By similarity
Glycosylationi290N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi324 ↔ 354By similarity
Glycosylationi451N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi496 ↔ 522By similarity
Glycosylationi542N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Ubl conjugation, Zymogen

Proteomic databases

EPDiG5ECN9.
PaxDbiG5ECN9.
PeptideAtlasiG5ECN9.

Expressioni

Tissue specificityi

Expressed in head and tail ganglia (PubMed:7954663, PubMed:11717360, PubMed:12657671, PubMed:24671950). Expressed in neurons including mechanosensory and motor neurons, and interneurons (at protein level) (PubMed:11717360, PubMed:12657671). Expressed in the nerve ring, ventral nerve cord and intestine (PubMed:24671950).4 Publications

Gene expression databases

BgeeiWBGene00001172.
ExpressionAtlasiG5ECN9. baseline and differential.

Interactioni

Subunit structurei

Interacts (via C-terminus) with F-box protein fsn-1 (via SPRY domain); the interaction results in egl-3 proteasomal degradation.1 Publication

GO - Molecular functioni

  • FBXO family protein binding Source: UniProtKB

Protein-protein interaction databases

STRINGi6239.C51E3.7a.

Structurei

3D structure databases

ProteinModelPortaliG5ECN9.
SMRiG5ECN9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini165 – 423Peptidase S8Sequence analysisAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni501 – 652Required for ubiquitination-mediated degradation1 PublicationAdd BLAST152

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
KOG3526. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
KOiK01360.
OMAiIWHSSIT.
OrthoDBiEOG091G05HI.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like.
IPR034182. Kexin/furin.
IPR009020. Peptidase/Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
PfamiView protein in Pfam
PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF16470. S8_pro-domain. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiView protein in PROSITE
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform aImported (identifier: G5ECN9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKNTHVDLIC VFLSIFIGIG EAVDVYTNHF HVHLKEGGGL EDAHRIAKRH
60 70 80 90 100
GFINRGQVAA SDNEYHFVQP ALVHARTRRS AGHHAKLHND DEVLHVEQLK
110 120 130 140 150
GYTRTKRGYR PLEQRLESQF DFSAVMSPSD PLYGYQWYLK NTGQAGGKAR
160 170 180 190 200
LDLNVERAWA MGFTGKNITT AIMDDGVDYM HPDIKNNFNA EASYDFSSND
210 220 230 240 250
PFPYPRYTDD WFNSHGTRCA GEIVAARDNG VCGVGVAYDG KVAGIRMLDQ
260 270 280 290 300
PYMTDLIEAN SMGHEPSKIH IYSASWGPTD DGKTVDGPRN ATMRAIVRGV
310 320 330 340 350
NEGRNGLGSI FVWASGDGGE DDDCNCDGYA ASMWTISINS AINNGENAHY
360 370 380 390 400
DESCSSTLAS TFSNGGRNPE TGVATTDLYG RCTRSHSGTS AAAPEAAGVF
410 420 430 440 450
ALALEANPSL TWRDLQHLTV LTSSRNSLFD GRCRDFPSLG INDNHRDSHG
460 470 480 490 500
NCSHFEWQMN GVGLEYNHLF GFGVLDAAEM VMLAMAWKTS PPRYHCTAGL
510 520 530 540 550
IDTPHEIPAD GNLILEINTD GCAGSQFEVR YLEHVQAVVS FNSTRRGDTT
560 570 580 590 600
LYLISPMGTR TMILSRRPKD DDSKDGFTNW PFMTTHTWGE NPTGKWRLVA
610 620 630 640 650
RFQGPGAHAG TLKKFELMLH GTREAPYNLI EPIVGQTNKK LDTVQKAHKR

SH
Length:652
Mass (Da):72,046
Last modified:December 14, 2011 - v1
Checksum:i39E378E75C081A2B
GO
Isoform bImported (identifier: G5ECN9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     93-188: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:556
Mass (Da):61,044
Checksum:i7FDB40A393D4BEA2
GO
Isoform cImported (identifier: G5ECN9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:527
Mass (Da):57,785
Checksum:i490BDE56DEC71F11
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0588291 – 125Missing in isoform c. CuratedAdd BLAST125
Alternative sequenceiVSP_05883093 – 188Missing in isoform b. CuratedAdd BLAST96

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04995 mRNA. Translation: AAA56868.1.
BX284605 Genomic DNA. Translation: CAB01635.1.
BX284605 Genomic DNA. Translation: CAB01642.1.
BX284605 Genomic DNA. Translation: CBZ01786.1.
PIRiC89181.
T20131.
RefSeqiNP_001023732.1. NM_001028561.3. [G5ECN9-1]
NP_001256192.1. NM_001269263.1. [G5ECN9-3]
NP_505614.3. NM_073213.6. [G5ECN9-2]
UniGeneiCel.18027.

Genome annotation databases

EnsemblMetazoaiC51E3.7a; C51E3.7a; WBGene00001172. [G5ECN9-1]
C51E3.7b; C51E3.7b; WBGene00001172. [G5ECN9-2]
C51E3.7c.1; C51E3.7c.1; WBGene00001172. [G5ECN9-3]
C51E3.7c.2; C51E3.7c.2; WBGene00001172. [G5ECN9-3]
GeneIDi179412.
KEGGicel:CELE_C51E3.7.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04995 mRNA. Translation: AAA56868.1.
BX284605 Genomic DNA. Translation: CAB01635.1.
BX284605 Genomic DNA. Translation: CAB01642.1.
BX284605 Genomic DNA. Translation: CBZ01786.1.
PIRiC89181.
T20131.
RefSeqiNP_001023732.1. NM_001028561.3. [G5ECN9-1]
NP_001256192.1. NM_001269263.1. [G5ECN9-3]
NP_505614.3. NM_073213.6. [G5ECN9-2]
UniGeneiCel.18027.

3D structure databases

ProteinModelPortaliG5ECN9.
SMRiG5ECN9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.C51E3.7a.

Protein family/group databases

MEROPSiS08.109.

Proteomic databases

EPDiG5ECN9.
PaxDbiG5ECN9.
PeptideAtlasiG5ECN9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC51E3.7a; C51E3.7a; WBGene00001172. [G5ECN9-1]
C51E3.7b; C51E3.7b; WBGene00001172. [G5ECN9-2]
C51E3.7c.1; C51E3.7c.1; WBGene00001172. [G5ECN9-3]
C51E3.7c.2; C51E3.7c.2; WBGene00001172. [G5ECN9-3]
GeneIDi179412.
KEGGicel:CELE_C51E3.7.

Organism-specific databases

CTDi179412.
WormBaseiC51E3.7a; CE08940; WBGene00001172; egl-3.
C51E3.7b; CE08941; WBGene00001172; egl-3.
C51E3.7c; CE45708; WBGene00001172; egl-3.

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
KOG3526. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
KOiK01360.
OMAiIWHSSIT.
OrthoDBiEOG091G05HI.

Enzyme and pathway databases

SignaLinkiQ18772.

Gene expression databases

BgeeiWBGene00001172.
ExpressionAtlasiG5ECN9. baseline and differential.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like.
IPR034182. Kexin/furin.
IPR009020. Peptidase/Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
PfamiView protein in Pfam
PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF16470. S8_pro-domain. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiView protein in PROSITE
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNEC2_CAEEL
AccessioniPrimary (citable) accession number: G5ECN9
Secondary accession number(s): E9P883, Q18772
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2017
Last sequence update: December 14, 2011
Last modified: May 10, 2017
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.