ID W5NGE3_LEPOC Unreviewed; 641 AA.
AC W5NGE3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 2 {ECO:0000313|Ensembl:ENSLOCP00000019702.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019702.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; AHAT01001627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006638648.1; XM_006638585.2.
DR AlphaFoldDB; W5NGE3; -.
DR STRING; 7918.ENSLOCP00000019702; -.
DR MEROPS; S08.073; -.
DR Ensembl; ENSLOCT00000019734.1; ENSLOCP00000019702.1; ENSLOCG00000015998.1.
DR GeneID; 102684877; -.
DR KEGG; loc:102684877; -.
DR CTD; 5126; -.
DR eggNOG; KOG3526; Eukaryota.
DR GeneTree; ENSGT00940000156965; -.
DR HOGENOM; CLU_002976_4_4_1; -.
DR InParanoid; W5NGE3; -.
DR OMA; LAKQWHS; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000018468; Linkage group LG16.
DR Bgee; ENSLOCG00000015998; Expressed in brain and 9 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 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; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:UP000018468};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..641
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004867593"
FT DOMAIN 464..600
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 641 AA; 71058 MW; 9CCE523069124364 CRC64;
MMLGLNRDGT TVVLVLLNAI IVAKGATEKP VYTNQFLVEL HEGDHDVASQ VAADHGFNNV
RKLSFGQGLF HFYHNAIPKT RRRRNLQHKQ RLEKDHRVKS ILQQEGFERM KRGYRDINEI
EVNMNDPLFT KQWYLINTGQ ADGTPGLDLN VAEAWDLGFT GKGVTIAIMD DGIDYLHPDL
ASNYNAEASY DFSSNDPYPY PRYTDDWFNS HGTRCAGEVS AAANNNICGV GVAYNSKVAG
IRMLDQPFMT DIIEASSISH MPQVIDIYSA SWGPTDDGKT VDGPRELTLQ AMADGVNKGR
AGKGSIYVWA SGDGGSYDDC NCDGYASSMW TISINSAIND GRTALYDESC SSTLASTFSN
GRKRNPEAGV ATTDLYGNCT LRHSGTSAAA PEAAGVFALA LEANPNLTWR DMQHLTVLTS
KRNQLHDEVH QWRRNGVGLE FNHLFGYGVL DAGGMVKMAK DWKTVPERFH CVGGSVQETH
KIPSDGKLML TITTDACEGK DNFVRYLEHV QAVITVNSSR RGDLNINMTS PMGTKSILLS
RRPRDDDSKV GFDKWPFMTT HTWGEDPRGT WVLEVGFTGA VPQKGVLKEW TLMLHGTQSA
PYIDQIVRDY QSKLAMSKKE ELEEELDEAV ERSLKSLLSK N
//
