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Database: UniProt
Entry: A0A2K5I9W0_COLAP
LinkDB: A0A2K5I9W0_COLAP
Original site: A0A2K5I9W0_COLAP 
ID   A0A2K5I9W0_COLAP        Unreviewed;       928 AA.
AC   A0A2K5I9W0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Proprotein convertase subtilisin/kexin type 6 {ECO:0008006|Google:ProtNLM};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000013428.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000013428.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   AlphaFoldDB; A0A2K5I9W0; -.
DR   STRING; 336983.ENSCANP00000013428; -.
DR   Ensembl; ENSCANT00000036342.1; ENSCANP00000013428.1; ENSCANG00000030011.1.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00064; FU; 4.
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; IPR000742; EGF-like_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR032778; GF_recep_IV.
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; IPR010909; PLAC.
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:SF8; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 6; 1.
DR   Pfam; PF14843; GF_recep_IV; 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   SMART; SM00181; EGF; 5.
DR   SMART; SM00261; FU; 5.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS50900; PLAC; 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:UP000233080};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          454..594
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          890..928
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          617..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        205
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   928 AA;  102956 MW;  1D454B58DF5B3D81 CRC64;
     VSTGAEPAPG VDSVRGHSQA AATQDVQAAE IIWDFVFRPF WKLFVRLLID GILLLVLQIG
     NLEDYYHFYH SKTFKRSTLS SRGPHTFLRM DPQVKWLQQQ EVKRRVKRQV RSDPQALYFN
     DPIWSNMWYL HCGDKNSRCR SEMNVQAAWK RGYTGKNVVV TILDDGIERN HPDLAPNYDS
     YASYDVNGND YDPSPRYDAS NENKHGTRCA GEVAASANNS YCIVGIAYNA KIGGIRMLDG
     DVTDVVEAKS LGIRPNYIDI YSASWGPDDD GKTVDGPGRL AKQAFEYGIK KGRQGLGSIF
     VWASGNGGRE GDYCSCDGYT NSIYTISVSS ATENGYKPWY LEECASTLAT TYSSGAFYER
     KIVTTDLRQR CTDGHTGTSV SAPMVAGIIA LALEANGQLT WRDVQHLLVK TSRPAHLKAS
     DWKVNGAGHK VSHFYGFGLV DAEALVVEAK KWTAVPSQHM CVAASDKRPR SIPLVQVLRT
     TALTSACAEH SDQRVVYLEH VVVRISISHP RRGDLQIYLI SPSGTKSQLL AKRLLDLSNE
     GFTNWEFMTV HCWGEKAEGQ WTLEIQDLPS QVRNPEKQGK LKEWSLILYG TAEHPYHTFS
     AHQSRSRMLE LSAPELEPPK AALSPSQVEV PEDEEDYTAH STPGSANILQ TSVCHPECGD
     KGCDGPNADQ CLNCIHFSLG SVKTSRKCVS VCPLGYFGDT AARRCRRCHK GCETCSGRGA
     TQCLSCRRGF YHHQEMNTCV TLCPAGFYAD ESQKNCLKCH PSCKKCVDEP EKCTVCKEGF
     SLARGSCIPD CEPGTYFDSE LIRCGECHHT CGTCVGPGRE ECIHCAKNFH FQDWKCVPAC
     GEGFYPEEMP GLPHKVCRRC DENCLSCAGS SRNCSRCKTG FTQLGTSCIT NHTCSNADET
     FCEMVKSNRL CERKLFIQFC CRTCLLAG
//
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