LOCUS NP_058787 752 aa linear ROD 12-NOV-2023
DEFINITION neuroendocrine convertase 1 precursor [Rattus norvegicus].
ACCESSION NP_058787
VERSION NP_058787.1
DBSOURCE REFSEQ: accession NM_017091.2
KEYWORDS RefSeq; RefSeq Select.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (residues 1 to 752)
AUTHORS Duhamel M, Rodet F, Murgoci AN, Desjardins R, Gagnon H, Wisztorski
M, Fournier I, Day R and Salzet M.
TITLE The proprotein convertase PC1/3 regulates TLR9 trafficking and the
associated signaling pathways
JOURNAL Sci Rep 6, 19360 (2016)
PUBMED 26778167
REMARK GeneRIF: macrophages from PC1/3 KO mice and rat PC1/3-KD NR8383
macrophages secreted more pro-inflammatory cytokines such as
TNF-alpha, IL6, IL1alpha and CXCL2.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 752)
AUTHORS Gagnon H, Refaie S, Gagnon S, Desjardins R, Salzet M and Day R.
TITLE Proprotein convertase 1/3 (PC1/3) in the rat alveolar macrophage
cell line NR8383: localization, trafficking and effects on cytokine
secretion
JOURNAL PLoS One 8 (4), e61557 (2013)
PUBMED 23637853
REMARK GeneRIF: PC1/3 as an important regulator of vesicle trafficking and
secretion in macrophages.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 752)
AUTHORS Navarro M, Cubero I and Thiele TE.
TITLE Decreased immunoreactivity of the polypeptide precursor
pro-opiomelanocortin (POMC) and the prohormone convertase pc1/3
after chronic ethanol exposure in Sprague-Dawley rats
JOURNAL Alcohol Clin Exp Res 37 (3), 399-406 (2013)
PUBMED 23050949
REMARK GeneRIF: Chronic ethanol exposure decreases prohormone convertase
(pc1/3) immunoreactivity in brain.
REFERENCE 4 (residues 1 to 752)
AUTHORS Takahashi T, Ida T, Sato T, Nakashima Y, Nakamura Y, Tsuji A and
Kojima M.
TITLE Production of n-octanoyl-modified ghrelin in cultured cells
requires prohormone processing protease and ghrelin
O-acyltransferase, as well as n-octanoic acid
JOURNAL J Biochem 146 (5), 675-682 (2009)
PUBMED 19628676
REMARK GeneRIF: The presence of PC and GOAT in the cells, as well as
n-octanoic acid in the culture medium, was necessary to produce
n-octanoyl ghrelin.
REFERENCE 5 (residues 1 to 752)
AUTHORS Dikeakos JD, Di Lello P, Lacombe MJ, Ghirlando R, Legault P,
Reudelhuber TL and Omichinski JG.
TITLE Functional and structural characterization of a dense core
secretory granule sorting domain from the PC1/3 protease
JOURNAL Proc Natl Acad Sci U S A 106 (18), 7408-7413 (2009)
PUBMED 19376969
REFERENCE 6 (residues 1 to 752)
AUTHORS Malide D, Seidah NG, Chretien M and Bendayan M.
TITLE Electron microscopic immunocytochemical evidence for the
involvement of the convertases PC1 and PC2 in the processing of
proinsulin in pancreatic beta-cells
JOURNAL J Histochem Cytochem 43 (1), 11-19 (1995)
PUBMED 7822759
REFERENCE 7 (residues 1 to 752)
AUTHORS Rhodes CJ, Lincoln B and Shoelson SE.
TITLE Preferential cleavage of des-31,32-proinsulin over intact
proinsulin by the insulin secretory granule type II endopeptidase.
Implication of a favored route for prohormone processing
JOURNAL J Biol Chem 267 (32), 22719-22727 (1992)
PUBMED 1429623
REFERENCE 8 (residues 1 to 752)
AUTHORS Hakes DJ, Birch NP, Mezey A and Dixon JE.
TITLE 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
JOURNAL Endocrinology 129 (6), 3053-3063 (1991)
PUBMED 1954888
REFERENCE 9 (residues 1 to 752)
AUTHORS Bloomquist BT, Eipper BA and Mains RE.
TITLE Prohormone-converting enzymes: regulation and evaluation of
function using antisense RNA
JOURNAL Mol Endocrinol 5 (12), 2014-2024 (1991)
PUBMED 1791845
REFERENCE 10 (residues 1 to 752)
AUTHORS Davidson HW, Rhodes CJ and Hutton JC.
TITLE Intraorganellar calcium and pH control proinsulin cleavage in the
pancreatic beta cell via two distinct site-specific endopeptidases
JOURNAL Nature 333 (6168), 93-96 (1988)
PUBMED 3283564
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
M76705.1, M83745.1 and JACYVU010000063.1.
Sequence Note: This RefSeq record was created using sequences from
two different strains, Sprague-Dawley and BN/SsNHsdMCW, because no
single transcript from the same strain was available for the full
length of the gene.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: M76705.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA5760393, SAMEA5760396
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on single protein-coding transcript
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..752
/organism="Rattus norvegicus"
/strain="Sprague-Dawley"
/db_xref="taxon:10116"
/chromosome="2"
/map="2q11"
Protein 1..752
/product="neuroendocrine convertase 1 precursor"
/EC_number="3.4.21.93"
/note="prohormone convertase 3; neuroendocrine convertase
1; NEC 1; prohormone convertase 1; proprotein convertase
1; Protein convertase subtilisin / kexin, type I"
/calculated_mol_wt=81032
sig_peptide 1..27
/inference="COORDINATES: ab initio prediction:SignalP:4.0"
/calculated_mol_wt=3107
Region 34..110
/region_name="S8_pro-domain"
/note="Peptidase S8 pro-domain; pfam16470"
/db_xref="CDD:435357"
mat_peptide 111..752
/product="Neuroendocrine convertase 1. /id=PRO_0000027064"
/note="propagated from UniProtKB/Swiss-Prot (P28840.1)"
/calculated_mol_wt=71241
Region 121..415
/region_name="Peptidases_S8_Protein_convertases_Kexins_Fur
in-lik"
/note="Peptidase S8 family domain in Protein convertases;
cd04059"
/db_xref="CDD:173789"
Site order(123,176,222)
/site_type="other"
/note="calcium binding site 1 [ion binding]"
/db_xref="CDD:173789"
Site order(167..168,203,208,250,268,278,309,320,382)
/site_type="active"
/db_xref="CDD:173789"
Site order(167,208,382)
/site_type="active"
/note="catalytic triad [active]"
/db_xref="CDD:173789"
Site 173
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P28840.1)"
Site order(315,345)
/site_type="other"
/note="calcium binding site 2 [ion binding]"
/db_xref="CDD:173789"
Site order(323,325,328,330)
/site_type="other"
/note="calcium binding site 3 [ion binding]"
/db_xref="CDD:173789"
Site 401
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P28840.1)"
Region 504..591
/region_name="P_proprotein"
/note="Proprotein convertase P-domain; pfam01483"
/db_xref="CDD:426283"
Region 631..662
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (P28840.1)"
Site 645
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P28840.1)"
Region 712..750
/region_name="Proho_convert"
/note="Prohormone convertase enzyme; pfam12177"
/db_xref="CDD:432385"
CDS 1..752
/gene="Pcsk1"
/gene_synonym="BDP; PC1; PC3"
/coded_by="NM_017091.2:220..2478"
/db_xref="GeneID:25204"
/db_xref="RGD:3272"
ORIGIN
1 mkqrgwtlqc taftlfcvwc alnsvkakrq fvnewaaeih ggpeaasaia eelgydllgq
61 igslenhylf khknhprrsr rsalhitkrl sdddrviwae qqyekerrkr svprdsalnl
121 fndpmwnqqw ylqdtrmtas lpkldlhvip vwqkgitgkg vvitvlddgl ewnhtdiyan
181 ydpeasydfn dndhdpfpry dptnenkhgt rcageiamqa nnhkcgvgva ynskvggirm
241 ldgivtdaie assigfnpgh vdiysaswgp nddgktvegp grlaqkafey gvkqgrqgkg
301 sifvwasgng grqgdncdcd gytdsiytis issasqqgls pwyaekcsst latsyssgdy
361 tdqritsadl hndctethtg tsasaplaag ifalaleanp nltwrdmqhl vvwtseydpl
421 annpgwkkng aglmvnsrfg fgllnakalv dladprtwrn vpekkeciik dnnfepralk
481 angeviveip tracegqena inslehvqfe atieysrrgd lhvtltsaag tstvllaere
541 rdtspngfkn wdfmsvhtwg enpvgtwtlk vtdmsgrmqn egrivnwkli lhgtssqpeh
601 mkqprvytsy ntvqndrrgv ekmvnvveek ptqnslngnl lvpknsssss vedrrdeqvq
661 gapskamlrl lqsafskntp skqsskipsa klsvpyegly ealeklnkps qledsedsly
721 sdyvdvfynt kpykhrddrl lqalmdilne kn
//
