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Database: UniProt
Entry: A0A0D9RHX4_CHLSB
LinkDB: A0A0D9RHX4_CHLSB
Original site: A0A0D9RHX4_CHLSB 
ID   A0A0D9RHX4_CHLSB        Unreviewed;       681 AA.
AC   A0A0D9RHX4;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 4 {ECO:0000313|Ensembl:ENSCSAP00000008213.1};
GN   Name=PCSK4 {ECO:0000313|Ensembl:ENSCSAP00000008213.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000008213.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000008213.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000008213.1}
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; AQIB01152653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01152654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01152655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9RHX4; -.
DR   STRING; 60711.ENSCSAP00000008213; -.
DR   Ensembl; ENSCSAT00000010114.1; ENSCSAP00000008213.1; ENSCSAG00000012070.1.
DR   eggNOG; KOG3525; Eukaryota.
DR   GeneTree; ENSGT00940000161989; -.
DR   OMA; PQKKCAI; -.
DR   Proteomes; UP000029965; Chromosome 6.
DR   Bgee; ENSCSAG00000012070; Expressed in pituitary gland.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
DR   CDD; cd00064; FU; 1.
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; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   PANTHER; PTHR42884:SF16; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 4; 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; SSF57184; Growth factor receptor domain; 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:UP000029965};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..681
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002345096"
FT   DOMAIN          446..578
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        155
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        370
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   681 AA;  75402 MW;  BA266016A9BC1430 CRC64;
     VPIALWLLWV LALALLRPRA VGWASVRVPI YVSSWAVRVS QGNREVERLA RKFGFVNLGP
     IFPDGQYFHL RHRGVVQQSL TPHWGHRLHL KKDPKVQWFQ QQTLRRRVKR SVVVPTDPWF
     SKQWYMNSEA QPDLSVLQAW GQGLSGQGIV VSVLDDGIEK DHPDLWANYD PLASYDFNDY
     DPDPQPRYTP SDENRHGTRC AGEVAAMANN GFCGVGVAFN ARIGGVRMLD GTITDVIEAQ
     SLSLQPQHIH IYSASWGPED DGRTVDGPGI LTREAFRRGV TKGRGGLGTL FIWASGNGGL
     HYDDCNCDGY TNSIHTLSVG STTQQGRVPW YSEACASTLT TTYSSGVATD PQIVTTDLHH
     QCTDQHTGTS ASAPLAAGMI ALALEANPFL TWRDMQHLVV RASKPAHLQA EDWRTNGVGR
     QVSHHYGYGL LDAGLLVDTA RTWLRTQPQR KCAVRVQNRP TPILPLIYIR KNVSACAGRH
     NSIRSLEHVQ AQLTLSYSRR GDLEISLTSP MGTRSTLVAI RPLDVSTEGY NNWVFMSTHF
     WDENPQGVWT LGLENKGYYF NTGMLYRYTL LLYGTAEDMT ARPTGPQVTS SACVQRDTEG
     LCQAVCDGAA YILGRLCLAY CPPRFFNHTR LVTPRPGHTA ALTLRVCSSC HSSCYTCRGG
     SLKDCTSCPP SSTLDQQQGS C
//
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