Neuroendocrine convertase 1 precursor

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Reviewed, UniProtKB/Swiss-Prot P63239 (NEC1_MOUSE)

Last modified June 16, 2009. Version 52. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Neuroendocrine convertase 1
      Short name=NEC 1
    EC=3.4.21.93
Alternative name(s):
    Prohormone convertase 1
    Proprotein convertase 1
      Short name=PC1
    PC3
    Furin homolog
    Propeptide-processing protease

Gene names

Name:	Pcsk1
Synonyms:	Att-1, Nec-1, Nec1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 vesicle › secretory 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.

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Ontologies

Keywords
Cellular component	Cytoplasmic vesicle
Domain	Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Uncategorized	proprotein convertase 1 activity Inferred from direct assay. Source: UniProtKB
Biological process	peptide biosynthetic process Inferred from direct assay. Source: UniProtKB peptide hormone processing Inferred from direct assay. Source: UniProtKB protein maturation by peptide bond cleavage Inferred from direct assay. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB secretory granule Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Potential

Propeptide

28 – 110

Potential

PRO_0000027059

Chain

111 – 753

643

Neuroendocrine convertase 1

PRO_0000027060

Regions

Region

122 – 410

289

Catalytic

Region

739 – 751

Amphipathic Potential

Sites

Active site

167

Charge relay system By similarity

Active site

208

Charge relay system By similarity

Active site

382

Charge relay system By similarity

Amino acid modifications

Glycosylation

401

N-linked (GlcNAc...) Potential

Glycosylation

645

N-linked (GlcNAc...) Potential

Disulfide bond

225 ↔ 374

By similarity

Disulfide bond

317 ↔ 347

By similarity

Disulfide bond

467 ↔ 494

By similarity

Experimental info

Sequence conflict

112

V → F in CAA40368. Ref.2

Sequence conflict

117

A → P in CAA40368. Ref.2

Sequence conflict

122

N → T in CAA40368. Ref.2

Sequence conflict

128

Q → H in CAA40368. Ref.2

Sequence conflict

282

R → K in CAA40368. Ref.2

Sequence conflict

330

S → L in AAA39375. Ref.3

Sequence conflict

732

K → E in CAA40368. Ref.2

Secondary structure

753

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P63239-1 [UniParc].

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

753

84,174

        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

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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: 1862107] [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: 1657897] [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: 2017186] [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: 8449925] [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: 2169760] [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: 2264933] [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: 12095256] [Abstract] Cited for: STRUCTURE BY NMR OF 28-110.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M69196 mRNA. Translation: AAA39732.1.
X57088 mRNA. Translation: CAA40368.1.
M58589 mRNA. Translation: AAA39894.1.
M55668 mRNA. Translation: AAA39375.1. Sequence problems.

IPI

IPI00470989.

PIR

KXMSC1. JX0171.

RefSeq

NP_038656.1.

UniGene

Mm.1333

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KN6	NMR	-	A	28-110	[»]
2KDT	NMR	-	A	711-753	[»]
2KE3	NMR	-	A	711-753	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S08.072.

Genome annotation databases

Ensembl

ENSMUSG00000021587. Mus musculus. [Contig view]

GeneID

18548.

KEGG

mmu:18548.

Organism-specific databases

MGI

MGI:97511. Pcsk1.

Phylogenomic databases

HOGENOM

P63239.

HOVERGEN

P63239.

OMA

P63239. HDPFPRY.

Enzyme and pathway databases

BRENDA

3.4.21.93. 244.

Gene expression databases

ArrayExpress

P63239.

Bgee

P63239.

CleanEx

MM_PCSK1.

GermOnline

ENSMUSG00000021587. Mus musculus.

Family and domain databases

InterPro

IPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

ProDom

PD000717. PrprotnconvertsP. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

294338.

PMAP-CutDB

P63239.

SOURCE

Search...

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Entry information

Entry name

NEC1_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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