ID G3P2G0_GASAC Unreviewed; 778 AA.
AC G3P2G0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000011783.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000011783.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000011783.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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}.
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DR AlphaFoldDB; G3P2G0; -.
DR STRING; 69293.ENSGACP00000011783; -.
DR MEROPS; S08.072; -.
DR Ensembl; ENSGACT00000011807.1; ENSGACP00000011783.1; ENSGACG00000008926.1.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000157385; -.
DR InParanoid; G3P2G0; -.
DR OMA; VWQKGFT; -.
DR TreeFam; TF314277; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000008926; Expressed in telencephalon and 2 other cell types or tissues.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 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; PS00136; SUBTILASE_ASP; 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:UP000007635};
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..778
FT /note="Neuroendocrine convertase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003449139"
FT DOMAIN 467..604
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 639..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 389
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 778 AA; 86505 MW; 1562CD82B87B8F83 CRC64;
MEMRCRPAMM CCVFAVLLSV VSRSLESSYV DRQYLNEWAV EIPGGLAAAE AIAKELDYKL
VRQIGALEDH FLFKHRNHPG RMKRSANHIT RRLSEDDRVL WAEQQYEKSR NKRASLGGCR
DCPVDKLFDD PMWNQQWYLQ DTRTSPSLPK LDLHVIPVWQ KGITGKGVVI TVLDDGLEWN
HTDIYSNYDA AASYDFNNND PDPFPRYDST NENKHGTRCA GEIAMQADNN KCGVGVAFNS
KVGGIRMLDG IVTDAIEASS IGFNPNHVDI YSASWGPNDD GKTVEGPGRL AQKAFEYGIQ
KGRGGKGSIF VWASGNGGRQ GDNCDCDGYT DSIYTISISS ASQQGLSPWY AEKCSSTLAT
AYSSGDYTDQ RITSADLHNE CTQTHTGTSA SAPLAAGIFA LALEQNPDLN WRDLQHIVVW
TSEFDPLANN PGWKRNGAGL MVNSRFGFGL LNAKALVDLA DPATWKHVPE KKQCIVRDDS
FQPRELKAAG AITIEIPTKA CVGQENAVIS LEHVQVEASI EYSRRGDLHI TLTSPAGTST
VLLAERERDT SANGFKNWDF MSVHTWGEDP AGTWTIKITD TSGRMQNEGR ILSWKLILHG
TSEKPEHMKK PRVYIPYNAV QNDRRGVEHM DDMMEVTQEP TQAYPPPNTE PAHASPPPNP
GKESKKPLNP PASPSLALLR LLQTAFNRQN PALPQPKSAA RASSAWRKLQ PDRSISPPAT
RLPPQMLYQA LDMINKYQGP EDSVYSDYSD GFYSIKPYRH RDDRLLQALF EMIDGDHK
//
