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P28840 (NEC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Prohormone convertase 1
Proprotein convertase 1
Short name=PC1
Gene names
Name:Pcsk1
Synonyms:Bdp, Nec-1, Nec1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
   DomainSignal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processneurogenesis

Inferred from expression pattern PubMed 18781386. Source: RGD

pancreas development

Inferred from expression pattern PubMed 17221210. Source: RGD

peptide hormone processing

Inferred from direct assay PubMed 10087454. Source: RGD

pituitary gland development

Inferred from expression pattern PubMed 15208361. Source: RGD

positive regulation of protein secretion

Inferred from direct assay PubMed 9389490. Source: RGD

protein autoprocessing

Inferred from mutant phenotype PubMed 9556596. Source: RGD

proteolysis

Inferred from mutant phenotype PubMed 16497799. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 18585435. Source: RGD

response to calcium ion

Inferred from expression pattern PubMed 9556596. Source: RGD

response to chlorate

Inferred from expression pattern PubMed 17221210. Source: RGD

response to drug

Inferred from expression pattern PubMed 10971617. Source: RGD

response to fatty acid

Inferred from expression pattern PubMed 18781386. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 11751617. Source: RGD

response to glucose

Inferred from expression pattern PubMed 17283238. Source: RGD

response to inorganic substance

Inferred from expression pattern PubMed 12501973. Source: RGD

response to interleukin-1

Inferred from expression pattern PubMed 17283238. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 10630414. Source: RGD

response to morphine

Inferred from expression pattern PubMed 18771713. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 17584972. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 10971617. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 17584972. Source: RGD

   Cellular_componentaxon terminus

Inferred from direct assay PubMed 10906712. Source: RGD

dendrite

Inferred from direct assay PubMed 10906712. Source: RGD

extracellular space

Inferred from direct assay PubMed 9389490. Source: RGD

neuron projection

Inferred from direct assay PubMed 17543468. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 10906712PubMed 17543468. Source: RGD

perikaryon

Inferred from direct assay PubMed 17543468. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 9389490. Source: RGD

rough endoplasmic reticulum

Inferred from direct assay PubMed 9405499. Source: RGD

secretory granule

Inferred from direct assay PubMed 10806118. Source: RGD

trans-Golgi network

Inferred from direct assay PubMed 10906712. Source: RGD

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchaperone binding

Inferred from physical interaction PubMed 10806118. Source: RGD

endopeptidase activity

Inferred from direct assay PubMed 10087454. Source: RGD

insulin binding

Inferred from physical interaction PubMed 10806118. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 10806118. Source: RGD

serine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 11083 Potential
PRO_0000027063
Chain111 – 752642Neuroendocrine convertase 1
PRO_0000027064

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

Glycosylation1731N-linked (GlcNAc...) Potential
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 conflict3661T → TT in AAA41476. Ref.2
Sequence conflict5141E → A in AAA41476. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28840 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: F630AD830A076DED

FASTA75284,121
        10         20         30         40         50         60 
MKQRGWTLQC TAFTLFCVWC ALNSVKAKRQ FVNEWAAEIH GGPEAASAIA EELGYDLLGQ 

        70         80         90        100        110        120 
IGSLENHYLF KHKNHPRRSR RSALHITKRL SDDDRVIWAE QQYEKERRKR SVPRDSALNL 

       130        140        150        160        170        180 
FNDPMWNQQW YLQDTRMTAS LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN 

       190        200        210        220        230        240 
YDPEASYDFN DNDHDPFPRY DPTNENKHGT 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 
ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECIIK DNNFEPRALK 

       490        500        510        520        530        540 
ANGEVIVEIP TRACEGQENA INSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE 

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

       610        620        630        640        650        660 
MKQPRVYTSY NTVQNDRRGV EKMVNVVEEK PTQNSLNGNL LVPKNSSSSS VEDRRDEQVQ 

       670        680        690        700        710        720 
GAPSKAMLRL LQSAFSKNTP SKQSSKIPSA KLSVPYEGLY EALEKLNKPS QLEDSEDSLY 

       730        740        750 
SDYVDVFYNT KPYKHRDDRL LQALMDILNE KN 

« Hide

References

[1]"Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA."
Bloomquist B.T., Eipper B.A., Mains R.E.
Mol. Endocrinol. 5:2014-2024(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats."
Hakes D.J., Birch N.P., Mezey A., Dixon J.E.
Endocrinology 129:3053-3063(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76705 mRNA. Translation: AAA40945.1.
M83745 mRNA. Translation: AAA41476.1.
PIRKXRTC1. A41556.
RefSeqNP_058787.1. NM_017091.2.
XP_003749285.1. XM_003749237.2.
UniGeneRn.11384.

3D structure databases

ProteinModelPortalP28840.
SMRP28840. Positions 31-103, 122-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015185.

Protein family/group databases

MEROPSS08.072.

Proteomic databases

PaxDbP28840.
PRIDEP28840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015185; ENSRNOP00000015185; ENSRNOG00000011107.
GeneID100911216.
25204.
KEGGrno:100911216.
rno:25204.
UCSCRGD:3272. rat.

Organism-specific databases

CTD5122.
RGD3272. Pcsk1.

Phylogenomic databases

eggNOGCOG4935.
GeneTreeENSGT00750000117689.
HOGENOMHOG000192536.
HOVERGENHBG008705.
InParanoidP28840.
KOK01359.
OMANNPGWKK.
OrthoDBEOG7BW0JD.
PhylomeDBP28840.
TreeFamTF314277.

Gene expression databases

GenevestigatorP28840.

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

NextBio605733.
PROP28840.

Entry information

Entry nameNEC1_RAT
AccessionPrimary (citable) accession number: P28840
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 121 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