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Database: UniProt/SWISS-PROT
Entry: NEC1_RAT
LinkDB: NEC1_RAT
Original site: NEC1_RAT 
ID   NEC1_RAT                Reviewed;         752 AA.
AC   P28840;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-APR-2018, entry version 150.
DE   RecName: Full=Neuroendocrine convertase 1;
DE            Short=NEC 1;
DE            EC=3.4.21.93;
DE   AltName: Full=Prohormone convertase 1;
DE   AltName: Full=Proprotein convertase 1;
DE            Short=PC1;
DE   Flags: Precursor;
GN   Name=Pcsk1; Synonyms=Bdp, Nec-1, Nec1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1791845; DOI=10.1210/mend-5-12-2014;
RA   Bloomquist B.T., Eipper B.A., Mains R.E.;
RT   "Prohormone-converting enzymes: regulation and evaluation of function
RT   using antisense RNA.";
RL   Mol. Endocrinol. 5:2014-2024(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1954888; DOI=10.1210/endo-129-6-3053;
RA   Hakes D.J., Birch N.P., Mezey A., Dixon J.E.;
RT   "Isolation of two complementary deoxyribonucleic acid clones from a
RT   rat insulinoma cell line based on similarities to Kex2 and furin
RT   sequences and the specific localization of each transcript to
RT   endocrine and neuroendocrine tissues in rats.";
RL   Endocrinology 129:3053-3063(1991).
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid
CC       residues. Substrates include POMC, renin, enkephalin, dynorphin,
CC       somatostatin, insulin and AGRP. {ECO:0000250|UniProtKB:P63239}.
CC   -!- CATALYTIC ACTIVITY: Release of protein hormones, neuropeptides and
CC       renin from their precursors, generally by hydrolysis of -Lys-
CC       Arg-|- bonds.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Localized in the secretion granules.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
DR   EMBL; M76705; AAA40945.1; -; mRNA.
DR   EMBL; M83745; AAA41476.1; -; mRNA.
DR   PIR; A41556; KXRTC1.
DR   RefSeq; NP_058787.1; NM_017091.2.
DR   UniGene; Rn.11384; -.
DR   ProteinModelPortal; P28840; -.
DR   SMR; P28840; -.
DR   STRING; 10116.ENSRNOP00000015185; -.
DR   MEROPS; S08.072; -.
DR   PhosphoSitePlus; P28840; -.
DR   PaxDb; P28840; -.
DR   PRIDE; P28840; -.
DR   Ensembl; ENSRNOT00000015185; ENSRNOP00000015185; ENSRNOG00000011107.
DR   GeneID; 25204; -.
DR   KEGG; rno:25204; -.
DR   UCSC; RGD:3272; rat.
DR   CTD; 5122; -.
DR   RGD; 3272; Pcsk1.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   GeneTree; ENSGT00750000117358; -.
DR   HOGENOM; HOG000192536; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; P28840; -.
DR   KO; K01359; -.
DR   OMA; FEPRALK; -.
DR   OrthoDB; EOG091G05HI; -.
DR   PhylomeDB; P28840; -.
DR   TreeFam; TF314277; -.
DR   Reactome; R-RNO-209952; Peptide hormone biosynthesis.
DR   Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   PRO; PR:P28840; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000011107; -.
DR   Genevisible; P28840; RN.
DR   GO; GO:0043679; C:axon terminus; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR   GO; GO:0030141; C:secretory granule; IDA:RGD.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR   GO; GO:0043559; F:insulin binding; IPI:RGD.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
DR   GO; GO:0022008; P:neurogenesis; IEP:RGD.
DR   GO; GO:0031016; P:pancreas development; IEP:RGD.
DR   GO; GO:0043043; P:peptide biosynthetic process; ISO:RGD.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:RGD.
DR   GO; GO:0021983; P:pituitary gland development; IEP:RGD.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD.
DR   GO; GO:0016540; P:protein autoprocessing; IMP:RGD.
DR   GO; GO:0016485; P:protein processing; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; IMP:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR   GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR   GO; GO:0010157; P:response to chlorate; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IEP:RGD.
DR   GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR   GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0043278; P:response to morphine; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   CDD; cd04059; Peptidases_S8_Protein_converta; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.30.70.850; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022005; Proho_convert.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12177; Proho_convert; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Complete proteome;
KW   Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   PROPEP       28    110       {ECO:0000255}.
FT                                /FTId=PRO_0000027063.
FT   CHAIN       111    752       Neuroendocrine convertase 1.
FT                                /FTId=PRO_0000027064.
FT   DOMAIN      162    451       Peptidase S8.
FT   DOMAIN      460    597       P/Homo B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01173}.
FT   ACT_SITE    167    167       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    208    208       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    382    382       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    225    374       {ECO:0000250}.
FT   DISULFID    317    347       {ECO:0000250}.
FT   DISULFID    467    494       {ECO:0000250}.
FT   CONFLICT    366    366       T -> TT (in Ref. 2; AAA41476).
FT                                {ECO:0000305}.
FT   CONFLICT    514    514       E -> A (in Ref. 2; AAA41476).
FT                                {ECO:0000305}.
SQ   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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