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P63239

- NEC1_MOUSE

UniProt

P63239 - NEC1_MOUSE

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Protein

Neuroendocrine convertase 1

Gene

Pcsk1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 and insulin.

Catalytic activityi

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

Cofactori

Calcium.

pH dependencei

Optimum pH is 5.5-6.5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671Charge relay systemBy similarity
Active sitei208 – 2081Charge relay systemBy similarity
Active sitei382 – 3821Charge relay systemBy similarity

GO - Molecular functioni

  1. endopeptidase activity Source: BHF-UCL
  2. serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

  1. peptide biosynthetic process Source: BHF-UCL
  2. peptide hormone processing Source: BHF-UCL
  3. protein processing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_206713. NGF processing.
REACT_207837. Insulin processing.

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
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:97511. Pcsk1.

Subcellular locationi

Cytoplasmic vesiclesecretory vesicle
Note: Localized in the secretion granules.

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. Golgi apparatus Source: RefGenome
  4. secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Propeptidei28 – 11083Sequence AnalysisPRO_0000027059Add
BLAST
Chaini111 – 753643Neuroendocrine convertase 1PRO_0000027060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi225 ↔ 374By similarity
Disulfide bondi317 ↔ 347By similarity
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi467 ↔ 494By similarity
Glycosylationi645 – 6451N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

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

Proteomic databases

MaxQBiP63239.
PaxDbiP63239.
PRIDEiP63239.

PTM databases

PhosphoSiteiP63239.

Miscellaneous databases

PMAP-CutDBP63239.

Expressioni

Gene expression databases

BgeeiP63239.
CleanExiMM_PCSK1.
ExpressionAtlasiP63239. baseline and differential.
GenevestigatoriP63239.

Interactioni

Protein-protein interaction databases

DIPiDIP-48841N.

Structurei

Secondary structure

1
753
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 384Combined sources
Helixi43 – 5311Combined sources
Beta strandi62 – 654Combined sources
Beta strandi67 – 715Combined sources
Beta strandi77 – 793Combined sources
Helixi89 – 946Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi713 – 7164Combined sources
Beta strandi718 – 7214Combined sources
Helixi722 – 7265Combined sources
Turni727 – 7304Combined sources
Helixi741 – 7488Combined sources
Turni749 – 7513Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KN6NMR-A28-110[»]
2KDTNMR-A711-753[»]
2KE3NMR-A711-753[»]
ProteinModelPortaliP63239.
SMRiP63239. Positions 31-103, 123-595, 711-753.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini162 – 451290Peptidase S8Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4935.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP63239.
KOiK01359.
OMAiNNPGWKK.
OrthoDBiEOG7BW0JD.
PhylomeDBiP63239.
TreeFamiTF314277.

Family and domain databases

Gene3Di2.60.120.260. 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. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF12177. Proho_convert. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121V → F in CAA40368. (PubMed:1657897)Curated
Sequence conflicti117 – 1171A → P in CAA40368. (PubMed:1657897)Curated
Sequence conflicti122 – 1221N → T in CAA40368. (PubMed:1657897)Curated
Sequence conflicti128 – 1281Q → H in CAA40368. (PubMed:1657897)Curated
Sequence conflicti282 – 2821R → K in CAA40368. (PubMed:1657897)Curated
Sequence conflicti330 – 3301S → L in AAA39375. (PubMed:2017186)Curated
Sequence conflicti732 – 7321K → E in CAA40368. (PubMed:1657897)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006517153.1.
XP_006517217.1. XM_006517154.1.
XP_006517218.1. XM_006517155.1.
UniGeneiMm.1333.
Mm.394672.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M69196 mRNA. Translation: AAA39732.1 .
X57088 mRNA. Translation: CAA40368.1 .
M58589 mRNA. Translation: AAA39894.1 .
M55668 mRNA. Translation: AAA39375.1 . Sequence problems.
CCDSi CCDS26649.1.
PIRi JX0171. KXMSC1.
RefSeqi NP_038656.1. NM_013628.2.
XP_006517216.1. XM_006517153.1.
XP_006517217.1. XM_006517154.1.
XP_006517218.1. XM_006517155.1.
UniGenei Mm.1333.
Mm.394672.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KN6 NMR - A 28-110 [» ]
2KDT NMR - A 711-753 [» ]
2KE3 NMR - A 711-753 [» ]
ProteinModelPortali P63239.
SMRi P63239. Positions 31-103, 123-595, 711-753.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48841N.

Protein family/group databases

MEROPSi S08.072.

PTM databases

PhosphoSitei P63239.

Proteomic databases

MaxQBi P63239.
PaxDbi P63239.
PRIDEi P63239.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022075 ; ENSMUSP00000022075 ; ENSMUSG00000021587 .
GeneIDi 18548.
KEGGi mmu:18548.
UCSCi uc007rfs.1. mouse.

Organism-specific databases

CTDi 5122.
MGIi MGI:97511. Pcsk1.

Phylogenomic databases

eggNOGi COG4935.
HOGENOMi HOG000192536.
HOVERGENi HBG008705.
InParanoidi P63239.
KOi K01359.
OMAi NNPGWKK.
OrthoDBi EOG7BW0JD.
PhylomeDBi P63239.
TreeFami TF314277.

Enzyme and pathway databases

Reactomei REACT_206713. NGF processing.
REACT_207837. Insulin processing.

Miscellaneous databases

EvolutionaryTracei P63239.
NextBioi 294338.
PMAP-CutDB P63239.
PROi P63239.
SOURCEi Search...

Gene expression databases

Bgeei P63239.
CleanExi MM_PCSK1.
ExpressionAtlasi P63239. baseline and differential.
Genevestigatori P63239.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProi IPR008979. 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 ]
PANTHERi PTHR10795. PTHR10795. 1 hit.
Pfami PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF12177. Proho_convert. 1 hit.
[Graphical view ]
PRINTSi PR00723. SUBTILISIN.
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. "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.

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: October 29, 2014
This is version 99 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

External Data

Dasty 3