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Database: UniProt
Entry: A0A455BT43_PHYMC
LinkDB: A0A455BT43_PHYMC
Original site: A0A455BT43_PHYMC 
ID   A0A455BT43_PHYMC        Unreviewed;       994 AA.
AC   A0A455BT43;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 6 isoform X1 {ECO:0000313|RefSeq:XP_028350988.2};
GN   Name=PCSK6 {ECO:0000313|RefSeq:XP_028350988.2};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028350988.2};
RN   [1] {ECO:0000313|RefSeq:XP_028350988.2}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028350988.2};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_028350988.2; XM_028495187.2.
DR   AlphaFoldDB; A0A455BT43; -.
DR   Proteomes; UP000248484; Chromosome 11.
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; 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; 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:UP000248484};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          491..631
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        242
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        416
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   994 AA;  109037 MW;  AEA01B63D074D786 CRC64;
     MPPRAPPGPR PPPRAPAAGG DEDTDTDTGG AGGPGLRPLA PRPWRWLLLL ALPAACSAPP
     PPRPVYTNHW AVQVLGGPAA ADRVAAAHGY LNLGQIGNLE DYYHFYHSKT FKRSALSSRG
     PHTFLRMDPQ VKWLQQQEVK RRVKRQVRSD PQALYFNDPI WSNMWYMHCG DKNSRCRSEM
     NVQAAWKRGY TGKNVVVTIL DDGIERNHPD LAPNYDSYAS YDVNGNDYDP SPRYDASNEN
     KHGTRCAGEV AASANNSYCI VGIAYNAKIG GIRMLDGDVT DVVEAKSLGI RPNYIDIYSA
     SWGPDDDGKT VDGPGRLARQ AFEYGIKKGR QGLGSIFVWA SGNGGREGDH CSCDGYTNSI
     YTISVSSTTE NGYKPWYLEE CASTLATTYS SGAFYERKIV TTDLRQRCTD GHTGTSVSAP
     MVAGIIALAL EANSQLTWRD VQHLLVKTSR PAHLKANDWK VNGAGHKVSH LYGFGLVDAD
     ALVMEAKKWT AVPLQHSCVA VTDKRPRSIP VVQTLRTSAL TTACADHSDQ RVGYLEHVVA
     RITISHPRRG DLQIHLISPS GTKSQLLAKR LLDHSNEGFT NWEFMTVHCW GEKAEGEWTL
     EIQDMPSQVR NPEKQGKLKE WSLILYGTAQ HPYTTFSAHQ SRSRMLELSA PEPEPPMAAL
     SPSQAEVPED EEDYTAPPSH GSPNILQTSV CHPECGDKGC DGPNADQCLN CVHFSLGSVK
     TIRKCVSVCP LGYFGDMASR RCRRCHKGCE TCSGRGPTQC LSCRRGFYHH QEVNTCVTFC
     PAGFYADENQ KNCLKCHPSC KKCMDEPEKC TVCKEGFSLA RGSCIPDCEP GTYFDSELIR
     CGECHPTCQT CVGPSREECI HCAPNFHFQD WKCVPACGEG FYPEEMPGLP HKVCRRCDES
     CLSCEGSSRN CSRCKTGFTQ LGTSCITNHT CSNGARSFRG ISGHPGQVGE GFEEVSAMSS
     HTLLAGSILL ANSQREQNEF QGSTAPASEQ LLGP
//
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