ID A0A1L8HR72_XENLA Unreviewed; 741 AA.
AC A0A1L8HR72;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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.S {ECO:0000313|RefSeq:XP_018099852.1,
GN ECO:0000313|Xenbase:XB-GENE-6488900};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018099852.1};
RN [1] {ECO:0000313|RefSeq:XP_018099852.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018099852.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018099852.1};
RG RefSeq;
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 RefSeq; XP_018099852.1; XM_018244363.2.
DR AlphaFoldDB; A0A1L8HR72; -.
DR STRING; 8355.A0A1L8HR72; -.
DR PaxDb; 8355-A0A1L8HR72; -.
DR GeneID; 108707229; -.
DR KEGG; xla:108707229; -.
DR AGR; Xenbase:XB-GENE-6488900; -.
DR CTD; 108707229; -.
DR Xenbase; XB-GENE-6488900; pcsk1.S.
DR OMA; DQEWYLQ; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 108707229; Expressed in zone of skin and 5 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; 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; PS00138; SUBTILASE_SER; 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, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 383
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 741 AA; 83473 MW; D03E996231605B1C CRC64;
MEGGHWQHLC IASVALLCLL CRGLEAALDK HFVNEWAAEI PGGPEEAQLL AEELGYDYMG
QIGSLENHYL FRHRAHPRRS RRSAPHITKR LADDGRVSWA EQQYNKERNK RSAIKEDTKN
LFKDPLWNRQ WYLQDTRSNP SLPKLDLHLL PVWKRGITGK GVVITVLDDG LEWNHTDIYA
NYDPEASYDF NDNDNDPFPR YDITNENRHG TRCVGEIAMI ANNNKCGVGV AYNAKVGGIR
MLDGIVTDAK EASSIGFNPQ HVHIYSASWG PNDDGKTVEG PGRLAQKAFE YGIKQGRNGK
GSIFVWASGN GGRQGDNCDC DGYTDSIYTI SISSASQQGL SPWYAEKCSS TLATAYSSGD
YTDQRIISAD LHNECTETHT GTSASAPLAA GIFALALEFN PDLTWRDMQH LVVWTSEYDP
LSNNPGWKKN GAGLMVNSRF GFGLLNAKAL VDLADPKTWK GVAEKKECIV EDNEFSPRFL
RSDGEVTIQI PTKACEGQDN HIKSLEHLQL EATIEYTRRG DLHITLTSPL GTNTVLLTER
ERDKSPNGFK SWDFMSVHTW GEDPAGTWTV KISDVSGRKN NEGRIVSWKL ILRGTSTQPE
HMKYPRVYTS YNVVQNDRRG VEKMGDTEKE PINESVTTDR SEVTENTPDS QELDERAKSL
AIAHLLKNAF DRGEASFPLE EKDIPKHSYL YALATIKQAE GREKENNLYN EYIDRFYHTR
PYKHRDDRLL QALLNILKKK P
//
