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P63239 (NEC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuroendocrine convertase 1

Short name=NEC 1
EC=3.4.21.93
Alternative name(s):
Furin homolog
PC3
Prohormone convertase 1
Propeptide-processing protease
Proprotein convertase 1
Short name=PC1
Gene names
Name:Pcsk1
Synonyms:Att-1, Nec-1, Nec1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 and insulin.

Catalytic activity

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

Cofactor

Calcium.

Subcellular location

Cytoplasmic vesiclesecretory vesicle. Note: Localized in the secretion granules.

Sequence similarities

Belongs to the peptidase S8 family. Furin subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 11083 Potential
PRO_0000027059
Chain111 – 753643Neuroendocrine convertase 1
PRO_0000027060

Regions

Region122 – 410289Catalytic
Region739 – 75113Amphipathic Potential

Sites

Active site1671Charge relay system By similarity
Active site2081Charge relay system By similarity
Active site3821Charge relay system By similarity

Amino acid modifications

Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Disulfide bond225 ↔ 374 By similarity
Disulfide bond317 ↔ 347 By similarity
Disulfide bond467 ↔ 494 By similarity

Experimental info

Sequence conflict1121V → F in CAA40368. Ref.2
Sequence conflict1171A → P in CAA40368. Ref.2
Sequence conflict1221N → T in CAA40368. Ref.2
Sequence conflict1281Q → H in CAA40368. Ref.2
Sequence conflict2821R → K in CAA40368. Ref.2
Sequence conflict3301S → L in AAA39375. Ref.3
Sequence conflict7321K → E in CAA40368. Ref.2

Secondary structure

........................ 753
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63239 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 04239C7B6385382E

FASTA75384,174
        10         20         30         40         50         60 
MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ 

        70         80         90        100        110        120 
IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL 

       130        140        150        160        170        180 
FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN 

       190        200        210        220        230        240 
YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM 

       250        260        270        280        290        300 
LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG 

       310        320        330        340        350        360 
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY 

       370        380        390        400        410        420 
TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL 

       430        440        450        460        470        480 
ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK 

       490        500        510        520        530        540 
ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE 

       550        560        570        580        590        600 
RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH 

       610        620        630        640        650        660 
MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ 

       670        680        690        700        710        720 
GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL 

       730        740        750 
YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN 

« Hide

References

[1]"Isolation and functional expression of a mammalian prohormone processing enzyme, murine prohormone convertase 1."
Korner J., Chun J., Harter D., Axel R.
Proc. Natl. Acad. Sci. U.S.A. 88:6834-6838(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
[2]"Cloning and functional expression of a novel endoprotease involved in prohormone processing at dibasic sites."
Nakayama K., Hosaka M., Hatsuzawa K., Murakami K.
J. Biochem. 109:803-806(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: LAF1.
[3]"Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2."
Seidah N.G., Marcinkiewicz M., Benjannet S., Gaspar L., Beaubien G., Mattei M.-G., Lazure C., Mbikay M., Chretien M.
Mol. Endocrinol. 5:111-122(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Pituitary.
[4]"Purification and characterization of the prohormone convertase PC1(PC3)."
Zhou Y., Lindberg I.
J. Biol. Chem. 268:5615-5623(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 111-120.
Tissue: Ovary.
[5]"cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases."
Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M., Chretien M.
DNA Cell Biol. 9:415-424(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-478.
Tissue: Pituitary.
[6]Erratum
Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M., Chretien M.
DNA Cell Biol. 9:789-789(1990) [PubMed] [Europe PMC] [Abstract]
[7]"Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus."
Tangrea M.A., Bryan P.N., Sari N., Orban J.
J. Mol. Biol. 320:801-812(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M69196 mRNA. Translation: AAA39732.1.
X57088 mRNA. Translation: CAA40368.1.
M58589 mRNA. Translation: AAA39894.1.
M55668 mRNA. Translation: AAA39375.1. Sequence problems.
CCDSCCDS26649.1.
PIRKXMSC1. JX0171.
RefSeqNP_038656.1. NM_013628.2.
XP_006517216.1. XM_006517153.1.
XP_006517217.1. XM_006517154.1.
XP_006517218.1. XM_006517155.1.
UniGeneMm.1333.
Mm.394672.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KN6NMR-A28-110[»]
2KDTNMR-A711-753[»]
2KE3NMR-A711-753[»]
ProteinModelPortalP63239.
SMRP63239. Positions 31-103, 123-597, 711-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48841N.

Protein family/group databases

MEROPSS08.072.

PTM databases

PhosphoSiteP63239.

Proteomic databases

MaxQBP63239.
PaxDbP63239.
PRIDEP63239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022075; ENSMUSP00000022075; ENSMUSG00000021587.
GeneID18548.
KEGGmmu:18548.
UCSCuc007rfs.1. mouse.

Organism-specific databases

CTD5122.
MGIMGI:97511. Pcsk1.

Phylogenomic databases

eggNOGCOG4935.
HOGENOMHOG000192536.
HOVERGENHBG008705.
InParanoidP63239.
KOK01359.
OMANNPGWKK.
OrthoDBEOG7BW0JD.
PhylomeDBP63239.
TreeFamTF314277.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

BgeeP63239.
CleanExMM_PCSK1.
GenevestigatorP63239.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProIPR008979. 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. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF12177. Proho_convert. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63239.
NextBio294338.
PMAP-CutDBP63239.
PROP63239.
SOURCESearch...

Entry information

Entry nameNEC1_MOUSE
AccessionPrimary (citable) accession number: P63239
Secondary accession number(s): P21662, P22546
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot