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

Neuroendocrine convertase 1

Gene

Pcsk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP.1 Publication

Catalytic activityi

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

Cofactori

pH dependencei

Optimum pH is 5.5-6.5.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei167Charge relay systemBy similarity1
Active sitei208Charge relay systemBy similarity1
Active sitei382Charge relay systemBy similarity1

GO - Molecular functioni

  • endopeptidase activity Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

  • nerve growth factor processing Source: Reactome
  • peptide biosynthetic process Source: BHF-UCL
  • peptide hormone processing Source: BHF-UCL
  • protein processing Source: BHF-UCL
  • regulation of insulin secretion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.4.21.93. 3474.
ReactomeiR-MMU-167060. NGF processing.
R-MMU-209952. Peptide hormone biosynthesis.
R-MMU-264876. Insulin processing.
R-MMU-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-MMU-400511. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
R-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.

Protein family/group databases

MEROPSiS08.072.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroendocrine convertase 1 (EC:3.4.21.93)
Short name:
NEC 1
Alternative name(s):
Furin homolog
PC3
Prohormone convertase 1
Propeptide-processing protease
Proprotein convertase 1
Short name:
PC1
Gene namesi
Name:Pcsk1
Synonyms:Att-1, Nec-1, Nec1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:97511. Pcsk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Disruption phenotypei

Increase in unprocessed AGRP.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
PropeptideiPRO_000002705928 – 110Sequence analysisAdd BLAST83
ChainiPRO_0000027060111 – 753Neuroendocrine convertase 1Add BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi225 ↔ 374By similarity
Disulfide bondi317 ↔ 347By similarity
Glycosylationi401N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi467 ↔ 494By similarity
Glycosylationi645N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

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

Proteomic databases

PaxDbiP63239.
PeptideAtlasiP63239.
PRIDEiP63239.

PTM databases

iPTMnetiP63239.
PhosphoSitePlusiP63239.

Miscellaneous databases

PMAP-CutDBP63239.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021587.
CleanExiMM_PCSK1.
ExpressionAtlasiP63239. baseline and differential.
GenevisibleiP63239. MM.

Interactioni

Protein-protein interaction databases

DIPiDIP-48841N.
STRINGi10090.ENSMUSP00000022075.

Structurei

Secondary structure

1753
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 38Combined sources4
Helixi43 – 53Combined sources11
Beta strandi62 – 65Combined sources4
Beta strandi67 – 71Combined sources5
Beta strandi77 – 79Combined sources3
Helixi89 – 94Combined sources6
Beta strandi97 – 100Combined sources4
Beta strandi713 – 716Combined sources4
Beta strandi718 – 721Combined sources4
Helixi722 – 726Combined sources5
Turni727 – 730Combined sources4
Helixi741 – 748Combined sources8
Turni749 – 751Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KN6NMR-A28-110[»]
2KDTNMR-A711-753[»]
2KE3NMR-A711-753[»]
ProteinModelPortaliP63239.
SMRiP63239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini162 – 451Peptidase S8Add BLAST290

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP63239.
KOiK01359.
OMAiGVKQGRQ.
OrthoDBiEOG091G05HI.
PhylomeDBiP63239.
TreeFamiTF314277.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.30.70.850. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
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.
IPR022005. Proho_convert.
IPR009020. Propept_inh.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF12177. Proho_convert. 1 hit.
PF16470. S8_pro-domain. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P63239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA
60 70 80 90 100
EELGYDLLGQ IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE
110 120 130 140 150
QQYEKERSKR SVQKDSALDL FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP
160 170 180 190 200
VWEKGITGKG VVITVLDDGL EWNHTDIYAN YDPEASYDFN DNDHDPFPRY
210 220 230 240 250
DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM LDGIVTDAIE
260 270 280 290 300
ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
310 320 330 340 350
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST
360 370 380 390 400
LATSYSSGDY TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP
410 420 430 440 450
NLTWRDMQHL VVWTSEYDPL ASNPGWKKNG AGLMVNSRFG FGLLNAKALV
460 470 480 490 500
DLADPRTWRN VPEKKECVVK DNNFEPRALK ANGEVIVEIP TRACEGQENA
510 520 530 540 550
IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE RDTSPNGFKN
560 570 580 590 600
WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH
610 620 630 640 650
MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN
660 670 680 690 700
VEGRRDEQVQ GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF
710 720 730 740 750
YEALEKLNKP SKLEGSEDSL YSDYVDVFYN TKPYKHRDDR LLQALMDILN

EEN
Length:753
Mass (Da):84,174
Last modified:October 11, 2004 - v1
Checksum:i04239C7B6385382E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112V → F in CAA40368 (PubMed:1657897).Curated1
Sequence conflicti117A → P in CAA40368 (PubMed:1657897).Curated1
Sequence conflicti122N → T in CAA40368 (PubMed:1657897).Curated1
Sequence conflicti128Q → H in CAA40368 (PubMed:1657897).Curated1
Sequence conflicti282R → K in CAA40368 (PubMed:1657897).Curated1
Sequence conflicti330S → L in AAA39375 (PubMed:2017186).Curated1
Sequence conflicti732K → E in CAA40368 (PubMed:1657897).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69196 mRNA. Translation: AAA39732.1.
X57088 mRNA. Translation: CAA40368.1.
M58589 mRNA. Translation: AAA39894.1.
M55668 mRNA. Translation: AAA39375.1. Sequence problems.
CCDSiCCDS26649.1.
PIRiJX0171. KXMSC1.
RefSeqiNP_038656.1. NM_013628.2.
XP_006517216.1. XM_006517153.2.
XP_006517217.1. XM_006517154.3.
XP_006517218.1. XM_006517155.2.
UniGeneiMm.1333.
Mm.394672.

Genome annotation databases

EnsembliENSMUST00000022075; ENSMUSP00000022075; ENSMUSG00000021587.
GeneIDi18548.
KEGGimmu:18548.
UCSCiuc007rfs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69196 mRNA. Translation: AAA39732.1.
X57088 mRNA. Translation: CAA40368.1.
M58589 mRNA. Translation: AAA39894.1.
M55668 mRNA. Translation: AAA39375.1. Sequence problems.
CCDSiCCDS26649.1.
PIRiJX0171. KXMSC1.
RefSeqiNP_038656.1. NM_013628.2.
XP_006517216.1. XM_006517153.2.
XP_006517217.1. XM_006517154.3.
XP_006517218.1. XM_006517155.2.
UniGeneiMm.1333.
Mm.394672.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KN6NMR-A28-110[»]
2KDTNMR-A711-753[»]
2KE3NMR-A711-753[»]
ProteinModelPortaliP63239.
SMRiP63239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48841N.
STRINGi10090.ENSMUSP00000022075.

Protein family/group databases

MEROPSiS08.072.

PTM databases

iPTMnetiP63239.
PhosphoSitePlusiP63239.

Proteomic databases

PaxDbiP63239.
PeptideAtlasiP63239.
PRIDEiP63239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022075; ENSMUSP00000022075; ENSMUSG00000021587.
GeneIDi18548.
KEGGimmu:18548.
UCSCiuc007rfs.1. mouse.

Organism-specific databases

CTDi5122.
MGIiMGI:97511. Pcsk1.

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP63239.
KOiK01359.
OMAiGVKQGRQ.
OrthoDBiEOG091G05HI.
PhylomeDBiP63239.
TreeFamiTF314277.

Enzyme and pathway databases

BRENDAi3.4.21.93. 3474.
ReactomeiR-MMU-167060. NGF processing.
R-MMU-209952. Peptide hormone biosynthesis.
R-MMU-264876. Insulin processing.
R-MMU-381771. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
R-MMU-400511. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
R-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.

Miscellaneous databases

EvolutionaryTraceiP63239.
PMAP-CutDBP63239.
PROiP63239.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021587.
CleanExiMM_PCSK1.
ExpressionAtlasiP63239. baseline and differential.
GenevisibleiP63239. MM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.30.70.850. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
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.
IPR022005. Proho_convert.
IPR009020. Propept_inh.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF12177. Proho_convert. 1 hit.
PF16470. S8_pro-domain. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEC1_MOUSE
AccessioniPrimary (citable) accession number: P63239
Secondary accession number(s): P21662, P22546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.