ID   G5BU25_HETGA            Unreviewed;       755 AA.
AC   G5BU25;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Neuroendocrine convertase 1 {ECO:0000256|ARBA:ARBA00015312};
DE            EC=3.4.21.93 {ECO:0000256|ARBA:ARBA00013234};
DE   AltName: Full=Prohormone convertase 1 {ECO:0000256|ARBA:ARBA00031320};
DE   AltName: Full=Proprotein convertase 1 {ECO:0000256|ARBA:ARBA00032862};
GN   Name=PCSK1 {ECO:0000313|EMBL:JAN98005.1};
GN   ORFNames=GW7_03746 {ECO:0000313|EMBL:EHB12786.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB12786.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB12786.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
RN   [2] {ECO:0000313|EMBL:JAN98005.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pituitary {ECO:0000313|EMBL:JAN98005.1};
RA   Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA   Platzer M., Szafranski K.;
RT   "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid residues.
CC       Substrates include POMC, renin, enkephalin, dynorphin, somatostatin,
CC       insulin and AGRP. {ECO:0000256|ARBA:ARBA00002975}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of protein hormones, neuropeptides and renin from
CC         their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.;
CC         EC=3.4.21.93; Evidence={ECO:0000256|ARBA:ARBA00000779};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000256|ARBA:ARBA00004398}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000256|ARBA:ARBA00005325}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH171888; EHB12786.1; -; Genomic_DNA.
DR   EMBL; GEBF01005627; JAN98005.1; -; Transcribed_RNA.
DR   RefSeq; XP_004841764.1; XM_004841707.2.
DR   AlphaFoldDB; G5BU25; -.
DR   STRING; 10181.G5BU25; -.
DR   MEROPS; S08.072; -.
DR   Ensembl; ENSHGLT00100024876; ENSHGLP00100024623; ENSHGLG00100018081.
DR   GeneID; 101704290; -.
DR   KEGG; hgl:101704290; -.
DR   CTD; 5122; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   InParanoid; G5BU25; -.
DR   OMA; VWQKGFT; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000007524; Expressed in pituitary gland and 3 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030070; P:insulin processing; IEA:Ensembl.
DR   GO; GO:0043043; P:peptide biosynthetic process; IEA:Ensembl.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 6.10.250.3320; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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; 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   PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
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; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..755
FT                   /note="Neuroendocrine convertase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007660985"
FT   DOMAIN          460..597
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          622..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        167
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        208
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        382
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   755 AA;  84179 MW;  5717C74F5A6D62B5 CRC64;
     MERRAWSLQG AAFALFCSWC ALNSVKAKRQ FVNEWAAEVP GGPEAASAIA EELGYDLLGQ
     IGSLENYYLF KHKNHPQRSR RSASHITKRL SDDDRVIWAE QQYEKKRSKR SALRDSALNL
     FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVLTILDDGL EWNHTDIYAN
     YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNRKCGVGVA YNSKVGGIRM
     LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG
     SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY
     TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL
     ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRSWSS VPEKKQCVVK DNDFEPRALK
     ANGEVIIEIP TRACEGQENS IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TNTVLLAERE
     RDTSPNGFKN WDFMSVHTWG ENPVGTWTLR ITDMSGRVQN EGRIVNWKLI LHGTSSQPEH
     MKQPRVYTSY NTVQNDRRGV EKMADAGEEQ PTQQNLNEDP LVSKSASSSS SSVGDRWDEQ
     AEGAPSQAML RLLQSAFSKN STPKQSPKKS PSAKLNIPYE NFYKALEKLN KPFQLKDSED
     SLYNDYVDVF YNTKPYKHRD DRLLQALVDI LNEEN
//