Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Furin-like protease kpc-1

Gene

kpc-1

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

Functioni

Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif (PubMed:24671950). During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341). Promotes the formation, extension and self-avoidance of dendritic branches of PVD and FLP mechanosensory neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341). In PVD neurons, regulates plasma membrane levels of branching receptor dma-1 by targeting it to late endosomes and thus promotes normal dendrite branching and dendrite self-avoidance (PubMed:26974341). Also controls dendrite extension in AIY and D-type motoneurons, dendrite branching in AQR sensory neurons and VC4/5 motoneurons, the normal number of dendritic branches in AVL neurons and the positioning of HSN and ALM/PLM neurons (PubMed:25232734). Dispensable for maintaining dendrite branching in adults (PubMed:25232734). Also regulates dauer-specific dendritic branching of IL2 neurons and dauer-specific nictation behavior (PubMed:23932402). Under adverse environmental conditions, may promote dauer formation by processing insulin-like proteins ins-1 and ins-18, two daf-2/InsR antagonists (PubMed:24671950).4 Publications

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi176Calcium 1By similarity1
Active sitei221Charge relay systemPROSITE-ProRule annotation1
Metal bindingi230Calcium 1By similarity1
Active sitei262Charge relay systemPROSITE-ProRule annotation1
Metal bindingi276Calcium 1By similarity1
Metal bindingi326Calcium 2By similarity1
Metal bindingi369Calcium 2By similarity1
Metal bindingi399Calcium 2By similarity1
Active sitei436Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • serine-type endopeptidase activity Source: WormBase

GO - Biological processi

  • dendrite morphogenesis Source: WormBase
  • insulin processing Source: WormBase

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

SignaLinkiO17798.

Protein family/group databases

MEROPSiS08.047.

Names & Taxonomyi

Protein namesi
Recommended name:
Furin-like protease kpc-11 Publication (EC:3.4.21.-1 Publication)
Alternative name(s):
CelfurPC protein1 Publication
Gene namesi
Name:kpc-1Imported
ORF Names:F11A6.1Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF11A6.1a; CE17653; WBGene00002232; kpc-1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini140 – 670LumenalCuratedAdd BLAST531
Transmembranei671 – 692HelicalSequence analysisAdd BLAST22

GO - Cellular componenti

  • axon Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: WormBase
  • perikaryon Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

Several defects in neuron development (PubMed:25232734, PubMed:26974341). In PVD mechanosensory neurons, tertiary and quaternary branching is decreased, secondary and ectopic tertiary branching is increased, the length of dendritic branches is also reduced and branches tend to overlap (PubMed:25232734, PubMed:26974341). Secondary dendrite branches are trapped next to primary branches (PubMed:26974341). In a sax-7 (nj48) or dma-1 (wy686) mutant background, significantly less secondary dendrites are trapped (PubMed:26974341). Increased dma-1 protein levels in PVD neuron dendrites (PubMed:26974341). In addition, abnormal dendrite branches in FLP neurons, reduced axonal extension in AIY interneurons, abnormal positioning of touch receptor ALM and HSN motoneuron, formation of ectopic branching in AVL, loss of sensory AQR branching in the nerve ring, and impaired extension and formation of branches near the vulva in VC4/5 motoneurons (PubMed:26974341). RNAi-mediated knockdown at the L1 larval stage but not at the L4 larval stage causes defects in the dendritic branching of PVD neurons (PubMed:26974341).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi136R → A in wy1060; loss of propeptide cleavage, trapped secondary dendrite branches and loss of tertiary and quaternary dendrite branches; when associated with A-143. 1 Publication1
Mutagenesisi143R → A in wy1060; loss of propeptide cleavage, trapped secondary dendrite branches and loss of tertiary and quaternary dendrite branches; when associated with A-136. 1 Publication1
Mutagenesisi263G → R in gk(779937); increased secondary dendritic branches in PVD neurons. 1 Publication1
Mutagenesisi265R → Q in gk(333538); normal secondary dendritic branches in PVD neurons. 1 Publication1
Mutagenesisi265R → W in dz185; increased secondary dendritic branches in PVD neurons. 1 Publication1
Mutagenesisi440P → L in my24; highly disorganized and truncated dauer-specific branching of the IL2Q neuron and disorganized and truncated branching of the PVD and FLP neurons in adults. 1 Publication1
Mutagenesisi440P → S in xr58; partial trapping of secondary dendrite branches next to primary dendrite branches. Forms tertiary and quaternary branches but with substantial overlap between tertiary dendrite branches. Increased dma-1 protein levels in PVD neuron dendrites. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
PropeptideiPRO_000043049034 – 139By similarityAdd BLAST106
ChainiPRO_0000430491140 – 692Furin-like protease kpc-1By similarityAdd BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi3N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi275N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi279 ↔ 428By similarity
Disulfide bondi371 ↔ 401By similarity
Glycosylationi455N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi487N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi518 ↔ 544By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiO17798.
PeptideAtlasiO17798.

Expressioni

Tissue specificityi

Expressed in the nervous system including the ventral nerve cord, the nerve ring and the retrovesicular ganglion, and in epithelial cells (PubMed:23932402, PubMed:24671950, PubMed:25232734). Expressed in IL2 neurons (PubMed:23932402). Expressed in PVD mechanosensory neurons (PubMed:25232734). Expressed in pharynx with strong expression in the g2 pharyngeal gland cells and vpi pharyngeal intestinal valve cells (PubMed:23932402, PubMed:25232734). Expressed in intestine (PubMed:24671950).3 Publications

Developmental stagei

Expressed in embryos, larvae and adults (PubMed:25232734). Expressed broadly in neuronal and epithelial cells throughout the head during the dauer stage (PubMed:23932402).2 Publications

Gene expression databases

BgeeiWBGene00002232.

Interactioni

Subunit structurei

Interacts (via extracellular domain) with receptor dma-1 (via extracellular domain); the interaction promotes dma-1 internalization.1 Publication

Protein-protein interaction databases

STRINGi6239.F11A6.1b.

Structurei

3D structure databases

ProteinModelPortaliO17798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini216 – 503Peptidase S8Sequence analysisAdd BLAST288
Domaini512 – 646P/Homo BPROSITE-ProRule annotationAdd BLAST135

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi570 – 572Cell attachment sitePROSITE-ProRule annotation3

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Sequence analysis

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
HOGENOMiHOG000192536.
InParanoidiO17798.
KOiK01349.
OMAiINEKPED.
OrthoDBiEOG091G05HI.
PhylomeDBiO17798.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.30.70.850. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like.
IPR034182. Kexin/furin.
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.
IPR009020. Propept_inh.
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
PS51829. P_HOMO_B. 1 hit.
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O17798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNISWYRHC SVRLQLVTLA LFLLLGSASL GSAHIDEEFE DDVTTTISSI
60 70 80 90 100
ASPMRRTYTN EWAVRIAGGK VEEANRLANK YGYTNLGPII PGDEYYLFRD
110 120 130 140 150
DRKKSRSSRK TRSLSANQLQ HEEDVMWMEQ QVAKRRVKRG YRRIRRHTDD
160 170 180 190 200
NDIFEEDDDG TQISKSRNRK HPDPNDPLWT DMWYLNRGEH HSDSTTRMDH
210 220 230 240 250
NVKEAWDLGY TGKGVVVTIL DDGLERTHPD ISPNYDERAS YDVNDRDNDP
260 270 280 290 300
MPRYEFSDEN RHGTRCAGEV AAIFNNSLCI VGIAYNANIG GIRMLDGDVT
310 320 330 340 350
DAVEAASVGH NADYIDIYSA SWGPDDDGRT VDGPAKLTRS AFEKGITMGR
360 370 380 390 400
KGKGSIFVWA SGNGGKDADS CNCDGYTNSI YTLSISSATE NGNIPWYSEA
410 420 430 440 450
CSSTLATTYS SGATGEKMIL TTDLHHACTN MHTGTSASAP LAAGIVALAL
460 470 480 490 500
EANPNLTWRD LQHIVIRTAK PINLRAGDWT TNGVGRNVSH SFGYGLMDAG
510 520 530 540 550
AMVKLAKIWK KVDEQHRCRQ FYPSRYKNIP NGNRLQLQLY SDGCYGGADE
560 570 580 590 600
NKVSYVEHVQ AIVTLKAPKR GDLQIYLTSP SGTKSTLLTK RARDTSRSGF
610 620 630 640 650
TDWAFMTTHN WGEQAAGLWI LEIDNDGWDD AELVKWELVL YGTDRETGDF
660 670 680 690
GGQHASPLAV RSVQMEATSS GTQYSIFHVI TLVILTFSQI LY
Length:692
Mass (Da):77,125
Last modified:April 12, 2017 - v3
Checksum:iB5F17DDF22BA3311
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti205A → V in AAB63525 (PubMed:9174171).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12682 mRNA. Translation: AAB63525.1.
BX284601 Genomic DNA. Translation: CAB04086.1.
PIRiT20759.
T20760.
UniGeneiCel.22630.

Genome annotation databases

GeneIDi173051.
KEGGicel:CELE_F11A6.1.
UCSCiF11A6.1a.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12682 mRNA. Translation: AAB63525.1.
BX284601 Genomic DNA. Translation: CAB04086.1.
PIRiT20759.
T20760.
UniGeneiCel.22630.

3D structure databases

ProteinModelPortaliO17798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F11A6.1b.

Protein family/group databases

MEROPSiS08.047.

Proteomic databases

PaxDbiO17798.
PeptideAtlasiO17798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi173051.
KEGGicel:CELE_F11A6.1.
UCSCiF11A6.1a.2. c. elegans.

Organism-specific databases

CTDi173051.
WormBaseiF11A6.1a; CE17653; WBGene00002232; kpc-1.

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
HOGENOMiHOG000192536.
InParanoidiO17798.
KOiK01349.
OMAiINEKPED.
OrthoDBiEOG091G05HI.
PhylomeDBiO17798.

Enzyme and pathway databases

SignaLinkiO17798.

Miscellaneous databases

PROiPR:O17798.

Gene expression databases

BgeeiWBGene00002232.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.30.70.850. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like.
IPR034182. Kexin/furin.
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.
IPR009020. Propept_inh.
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
PS51829. P_HOMO_B. 1 hit.
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFKPC1_CAEEL
AccessioniPrimary (citable) accession number: O17798
Secondary accession number(s): O17797, Q17325
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 2014
Last sequence update: April 12, 2017
Last modified: April 12, 2017
This is version 135 of the entry and version 3 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.