ID A0A2I2U735_FELCA Unreviewed; 950 AA.
AC A0A2I2U735;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 6 {ECO:0000313|Ensembl:ENSFCAP00000028254.2};
GN Name=PCSK6 {ECO:0000313|Ensembl:ENSFCAP00000028254.2,
GN ECO:0000313|VGNC:VGNC:80878};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000028254.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000028254.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028254.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000028254.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028254.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000028254.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028254.2};
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 EMBL; AANG04000441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2U735; -.
DR Ensembl; ENSFCAT00000033830.3; ENSFCAP00000028254.2; ENSFCAG00000013386.6.
DR VGNC; VGNC:80878; PCSK6.
DR GeneTree; ENSGT00940000159506; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000013386; Expressed in liver and 10 other cell types or tissues.
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; PF08686; PLAC; 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:UP000011712};
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 489..629
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 912..950
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..668
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 199
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 950 AA; 104930 MW; 647693502799CE58 CRC64;
MPPRAPPAPG PRPPPRAAAV DAVDAGGAGG PGLRPLAPRP WRWLLLLALP AACSAPPPPP
RPVYTNHWAV QVLGGPAAAD RVAAAHGYLN LGQIGNLENY YHFYHSKTFK RSTLSSRGPH
TFLRMDPQVK WLQQQEVKRR VKRQVRGDPQ ALYFNDPIWS NMWYMHCGDK NSRCRSEMNV
QAAWKKGYTG KNVVVTILDD GIERNHPDLA PNYDSYASYD VNGNDYDPSP RYDASNENKH
GTRCAGEVAA SANNSYCIVG IAYNAKIGGI RMLDGDVTDV VEAKSLGIRP NYIDIYSASW
GPDDDGKTVD GPGRLAKQAF EYGIKKGRQG LGSIFVWASG NGGREGDHCS CDGYTNSIYT
ISVSSTTENG YKPWYLEECA STLATTYSSG AFYERKIVTT DLRQRCTDGH TGTSVSAPMV
AGIIALALEA NSQLTWRDVQ HLLVKTSRPA HLKANDWKVN GAGHKVSHLY GFGLVDAEAL
VTEAKKWTAV PSQHMCVATT DKRPRSIPVV QTLRTTALTT ACADHSDQRV GYLEHVVARI
SISHPRRGDL QIHLISPSGT KSQLLAKRLL DHSNEGFTNW EFMTVHCWGE KAEGEWTLEI
QDMPSQVRNP EKQGKLKEWS LILYGTAEHP YNTFISHQSR SRMLELSTPE LEPPKAALSP
PQAEVPEDEE DYTGVCHPEC GDKGCDGPNA DQCLNCVHFS LGSAKTSRKC VNTCPPGYFG
DTAARRCRRC YKGCETCSGR SPTQCLSCRR GFYHHQEMNT CVTFCPAGFY ADESQKNCLK
CHPSCRKCVD EPEKCTVCKE GFSFARGSCI PDCEPGTYFD SELIKCGECH HSCQTCVGPS
REECIHCAAN FHFQDWKCVP ACGEGFYPEE MPGLPHKVCR RCDESCLSCE GSSRNCSRCK
TGFTLLGTTC ITNHTCSNAD EMFCEMVKSN RLCERKLFIQ FCCRTCLLAG
//
