ID   U3JJX3_FICAL            Unreviewed;       735 AA.
AC   U3JJX3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
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};
GN   Name=PCSK1 {ECO:0000313|Ensembl:ENSFALP00000003077.2};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003077.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000003077.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000003077.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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   AlphaFoldDB; U3JJX3; -.
DR   STRING; 59894.ENSFALP00000003077; -.
DR   MEROPS; S08.072; -.
DR   Ensembl; ENSFALT00000003090.2; ENSFALP00000003077.2; ENSFALG00000002956.2.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000157385; -.
DR   HOGENOM; CLU_002976_4_1_1; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000016665; Chromosome Z.
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:UP000016665};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          447..584
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          616..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        369
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   735 AA;  82382 MW;  B28C363960BCDB3E CRC64;
     MSNCREGTAS SHPPARVLCM ASLKTGTLLA LARPRGRGRG HLLSVPPIGS LKNHYLFRHK
     SHPRRSRRSA THMTKRLSDD ERVSWAEQQY EKKRTKRASV RDSAESLFND PMWNQQWYLQ
     DTRITPSLPK LDLHVIPVWQ KGFTGKGVVI TVLDDGLEWN HTDIYANYDP KASYDFNDND
     HDPFPRYDPT NENKHGTRCA GEIAMQANNR KCGVGVAYNS RVGGIRMLDG IVTDAIEASS
     IGFNPEHVDI YSASWGPNDD GKTVEGPGRL AQKAFEYGIN QGRNGKGSIF VWASGNGGRQ
     GDNCDCDGYT DSIYTISISS ASQQGLSPWY AEKCSSTLAT AYSSGDYTDQ RITSVDLHNE
     CTETHTGTSA SAPLAAGIFA LALEANPDLT WRDMQHLVVW TSEYDPLAGN PGWKKNGAGL
     MVNSRFGFGL LNANALVDLA DPKRWKGVPE KRECIVKDKS FEPRLLRADE EVIIEIPTKA
     CEGQENSIAS LEHVQLEATI EYSRRGDLHV TLVSPSGTST VLLAERERDK SPNGFKNWDF
     MSVHTWGENP AGTWILRITD MSRRIQNEGR IVNWKLILHG TTTQPEHMKQ PRVYTSYNAV
     QNDRRGVEKM TDLVEDHTTL ESLSEKPKAT EETSSSSDKA EDKIPSEAML HLLQSAFSRQ
     MDQKQLPKKT ASKKLNIPYE HFYQALKKLN KPSQLRGSEE SLYSDYVDLF YNAKPYKHRD
     DRLLQALVDI INEGN
//