• secretory granule lumen • transport vesicle • cytoplasmic vesicle • extracellular space • membrane • neuron projection
Biological process
• peptide biosynthetic process • cell-cell signaling • peptide hormone processing • proteolysis • protein processing
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
5122
18548
Ensembl
ENSG00000175426
ENSMUSG00000021587
UniProt
P29120
P63239
RefSeq (mRNA)
NM_001177876 NM_000439 NM_001177875
NM_013628
RefSeq (protein)
NP_000430 NP_001171346
NP_038656
Location (UCSC)
Chr 5: 96.39 – 96.43 Mb
Chr 13: 75.09 – 75.13 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
proprotein convertase 1
Identifiers
EC number
3.4.21.93
CAS number
99676-46-7
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
PMC
articles
PubMed
articles
NCBI
proteins
Proprotein convertase 1, also known as prohormone convertase, prohormone convertase 3, or neuroendocrine convertase 1 and often abbreviated as PC1/3 is an enzyme that in humans is encoded by the PCSK1 gene.[5] PCSK1 and PCSK2 differentially cleave proopiomelanocortin and they act together to process proinsulin and proglucagon in pancreatic islets.[6]
Contents
1Function
2Clinical significance
3See also
4References
5External links
Function
PC1/3 is an enzyme that performs the proteolytic cleavage of prohormones to their intermediate (or sometimes completely cleaved) forms.[6] It is present only in neuroendocrine cells such as brain, pituitary and adrenal, and most often cleaves after a pair of basic residues within prohormones but can occasionally cleave after a single arginine. It binds to a protein known as proSAAS, which also represents its endogenous inhibitor. PC1 is synthesized as a 99 kDa proform quickly converted to an 87 kDa major active form, which itself is nearly completely cleaved to a 66 kDa active form within neuroendocrine cells.
Proprotein convertase 1 is the enzyme largely responsible for the first step in the biosynthesis of insulin. Following the action of proprotein convertase 1, a carboxypeptidase is required to remove the basic residues from the processing intermediate and generate the bioactive form of insulin. Another prohormone convertase, proprotein convertase 2 plays a more minor role in the first step of insulin biosynthesis, but a greater role in the first step of glucagon biosynthesis. The knockout of proprotein convertase 1 is not lethal in mice or humans, most likely due to the presence of the second convertase, although mice lacking proprotein convertase 1 activity show a number of defects including slow growth.[citation needed]
Proprotein convertase 1 is a calcium (Ca2+) activated serine endoprotease (meaning that a serine residue is part of the active site that hydrolyzes the peptide bond within the substrate). It is related to the bacterial enzyme known as subtilisin. There are nine subtilisin homologs in mammals; in addition to proprotein convertase 1 and 2, other members of this enzyme family include furin, PACE4, PC4, PC5/6, PC7/8, PCSK9, and SKI1/S1P.
Clinical significance
Variants in the PCSK1 gene may be associated with obesity.[7]
See also
Proprotein convertase subtilisin/kexin type 1 inhibitor
References
^ abcGRCh38: Ensembl release 89: ENSG00000175426 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000021587 - Ensembl, May 2017
^Seidah NG, Mattei MG, Gaspar L, Benjannet S, Mbikay M, Chrétien M (September 1991). "Chromosomal assignments of the genes for neuroendocrine convertase PC1 (NEC1) to human 5q15-21, neuroendocrine convertase PC2 (NEC2) to human 20p11.1-11.2, and furin (mouse 7[D1-E2] region)". Genomics. 11 (1): 103–7. doi:10.1016/0888-7543(91)90106-O. PMID 1765368.
^ abJansen E, Ayoubi TA, Meulemans SM, Van de Ven WJ (June 1995). "Neuroendocrine-specific expression of the human prohormone convertase 1 gene. Hormonal regulation of transcription through distinct cAMP response elements". J. Biol. Chem. 270 (25): 15391–7. doi:10.1074/jbc.270.25.15391. PMID 7797529.
^Renström F, Payne F, Nordström A, et al. (April 2009). "Replication and extension of genome-wide association study results for obesity in 4923 adults from northern Sweden". Hum. Mol. Genet. 18 (8): 1489–96. doi:10.1093/hmg/ddp041. PMC 2664142. PMID 19164386.
External links
Proprotein+Convertase+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
6
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word knowledge letters chemistry
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I am trying to run a scheduled task with User Group (not a single user). This is working fine when I in the field "when running a task, use the following user account:" insert BUILTIN User Group (for example: Administrators or Users). But when I try it with the created Local User Group (example: TestGroup) it is not working. The Users in the TestGroup are the same as in the Administrators group. What could be the problem? Are there some restrictions to the Created User Group compared to BUILTINUsers?
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For ports in the country of Spain, see List of ports in Spain. City in City of Port of Spain, Trinidad and Tobago Port of Spain City City of Port of Spain Top to bottom (left to right): Skyline of Port of Spain from Gulf of Paria; National Academy for the Performing Arts, Independence Square, Eric Williams Plaza; MovieTowne, Port of Port of Spain Motto(s): "We Gather Strength As We Go Along" Port of Spain Coordinates: 10°40′N 61°31′W / 10.667°N 61.517°W / 10.667; -61.517 Coordinates: 10°40′N 61°31′W / 10.667°N 61.517°W / 10.667; -61.517 Country Trinidad and Tobago Jurisdiction City of Port of Spain Settled 1560 Incorporated (town) 1853 Incorporated (city) 1914 Government • Mayor Joel Martinez • Governing body City Corporation Area [1] • City 12 km 2 (5 sq mi) Elevation [2] 66 m (217 ft) Population (2011) [1] • City 37,074 • Rank 3rd • Density 3,090/km 2 (8,000/sq mi)...
