ID A0A091QN03_MERNU Unreviewed; 501 AA.
AC A0A091QN03;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
DE Flags: Fragment;
GN ORFNames=N331_12861 {ECO:0000313|EMBL:KFQ28598.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ28598.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ28598.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ28598.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KK703153; KFQ28598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QN03; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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; 3.40.50.200; 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; IPR022005; Proho_convert.
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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 213..350
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ28598.1"
FT NON_TER 501
FT /evidence="ECO:0000313|EMBL:KFQ28598.1"
SQ SEQUENCE 501 AA; 56006 MW; ADE6BBD2B2312A9D CRC64;
GIRMLDGIVT DAIEASSIGF NPEHVDIYSA SWGPNDDGKT VEGPGRLAQK AFEYGIKQGR
NGKGSIFVWA SGNGGRQGDN CDCDGYTDSI YTISISSASQ QGLSPWYAEK CSSTLATAYS
SGDYTDQRIT SADLHNECTE THTGTSASAP LAPNLTWRDM QHLVVWTSEY DPLAGNPGWK
KNGAGLMVNS RFGFGLLNAN ALVDLADPKR WKGVPEKREC IVKDKSFEPR LLRANEEVII
EIPTTACKGQ ENSIVSLEHV QLEATIEYSR RGDLHVTLVS PSGTNTVLLA QRERDKSPNG
FKNWDFMSVH TWGENPTGTW VLRITDVSRR IQNEGRIVNW KLILHGTAAQ PEHMKQPRVY
TSYNAVQNDR RGVEKMTDSA EEHTTQENVR EKLRVMEEPS SSSDKAEDKI PSEAMLHLLQ
SAFSRQMAPK RLPKKTASEK SNIPYEHFYQ ALEKLNKPSQ LRDSEESLYS DYVDLFYNAK
PYKHRDDRLL QALVDIVNEG N
//
