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Neuroendocrine convertase 1 (NEC 1) (EC 3.4.21.93) (Prohormone convertase 1) (Proprotein convertase 1) (PC1)

 NEC1_RAT                Reviewed;         752 AA.
P28840;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
22-NOV-2017, entry version 146.
RecName: Full=Neuroendocrine convertase 1;
Short=NEC 1;
EC=3.4.21.93;
AltName: Full=Prohormone convertase 1;
AltName: Full=Proprotein convertase 1;
Short=PC1;
Flags: Precursor;
Name=Pcsk1; Synonyms=Bdp, Nec-1, Nec1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1791845; DOI=10.1210/mend-5-12-2014;
Bloomquist B.T., Eipper B.A., Mains R.E.;
"Prohormone-converting enzymes: regulation and evaluation of function
using antisense RNA.";
Mol. Endocrinol. 5:2014-2024(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1954888; DOI=10.1210/endo-129-6-3053;
Hakes D.J., Birch N.P., Mezey A., Dixon J.E.;
"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.";
Endocrinology 129:3053-3063(1991).
-!- 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, insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.
-!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
renin from their precursors, generally by hydrolysis of -Lys-
Arg-|- bonds.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
Note=Localized in the secretion granules.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
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EMBL; M76705; AAA40945.1; -; mRNA.
EMBL; M83745; AAA41476.1; -; mRNA.
PIR; A41556; KXRTC1.
RefSeq; NP_058787.1; NM_017091.2.
UniGene; Rn.11384; -.
ProteinModelPortal; P28840; -.
SMR; P28840; -.
STRING; 10116.ENSRNOP00000015185; -.
MEROPS; S08.072; -.
PhosphoSitePlus; P28840; -.
PaxDb; P28840; -.
PRIDE; P28840; -.
Ensembl; ENSRNOT00000015185; ENSRNOP00000015185; ENSRNOG00000011107.
GeneID; 25204; -.
KEGG; rno:25204; -.
UCSC; RGD:3272; rat.
CTD; 5122; -.
RGD; 3272; Pcsk1.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P28840; -.
KO; K01359; -.
OMA; FEPRALK; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; P28840; -.
TreeFam; TF314277; -.
Reactome; R-RNO-209952; Peptide hormone biosynthesis.
Reactome; R-RNO-264876; Insulin processing.
Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
PRO; PR:P28840; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000011107; -.
Genevisible; P28840; RN.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0051087; F:chaperone binding; IPI:RGD.
GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
GO; GO:0043559; F:insulin binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
GO; GO:0022008; P:neurogenesis; IEP:RGD.
GO; GO:0031016; P:pancreas development; IEP:RGD.
GO; GO:0043043; P:peptide biosynthetic process; ISO:RGD.
GO; GO:0016486; P:peptide hormone processing; IDA:RGD.
GO; GO:0021983; P:pituitary gland development; IEP:RGD.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD.
GO; GO:0016540; P:protein autoprocessing; IMP:RGD.
GO; GO:0016485; P:protein processing; ISO:RGD.
GO; GO:0006508; P:proteolysis; IMP:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0010157; P:response to chlorate; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0043278; P:response to morphine; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR022005; Proho_convert.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF12177; Proho_convert; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
Protease; Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 110 {ECO:0000255}.
/FTId=PRO_0000027063.
CHAIN 111 752 Neuroendocrine convertase 1.
/FTId=PRO_0000027064.
DOMAIN 162 451 Peptidase S8.
DOMAIN 460 597 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
ACT_SITE 167 167 Charge relay system. {ECO:0000250}.
ACT_SITE 208 208 Charge relay system. {ECO:0000250}.
ACT_SITE 382 382 Charge relay system. {ECO:0000250}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 225 374 {ECO:0000250}.
DISULFID 317 347 {ECO:0000250}.
DISULFID 467 494 {ECO:0000250}.
CONFLICT 366 366 T -> TT (in Ref. 2; AAA41476).
{ECO:0000305}.
CONFLICT 514 514 E -> A (in Ref. 2; AAA41476).
{ECO:0000305}.
SEQUENCE 752 AA; 84121 MW; F630AD830A076DED CRC64;
MKQRGWTLQC TAFTLFCVWC ALNSVKAKRQ FVNEWAAEIH GGPEAASAIA EELGYDLLGQ
IGSLENHYLF KHKNHPRRSR RSALHITKRL SDDDRVIWAE QQYEKERRKR SVPRDSALNL
FNDPMWNQQW YLQDTRMTAS LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN
YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM
LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECIIK DNNFEPRALK
ANGEVIVEIP TRACEGQENA INSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE
RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK VTDMSGRMQN EGRIVNWKLI LHGTSSQPEH
MKQPRVYTSY NTVQNDRRGV EKMVNVVEEK PTQNSLNGNL LVPKNSSSSS VEDRRDEQVQ
GAPSKAMLRL LQSAFSKNTP SKQSSKIPSA KLSVPYEGLY EALEKLNKPS QLEDSEDSLY
SDYVDVFYNT KPYKHRDDRL LQALMDILNE KN


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