ID A0A2I0LQE6_COLLI Unreviewed; 760 AA.
AC A0A2I0LQE6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 7 {ECO:0000313|EMBL:PKK19652.1};
DE Flags: Fragment;
GN Name=PCSK7 {ECO:0000313|EMBL:PKK19652.1};
GN ORFNames=A306_00012245 {ECO:0000313|EMBL:PKK19652.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK19652.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK19652.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK19652.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK19652.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKCR02000141; PKK19652.1; -; Genomic_DNA.
DR STRING; 8932.A0A2I0LQE6; -.
DR InParanoid; A0A2I0LQE6; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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; 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; 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:SF28; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 7; 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; 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; 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:UP000053872};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 439..576
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 158..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKK19652.1"
SQ SEQUENCE 760 AA; 84103 MW; 6DF7C2B200789B81 CRC64;
WLSAAWAPPA AAERGAEPPH RALSWAVSLD APEEQLEQRA EELARSAGLL NMGRVGELRG
HYLFASRPDG RTPEAIRRSV DTLFAQHDSV RWHSEQKLLK RSKRSLRFND PKYPQQWHLN
NHKSPGKDIN VTGVWERNVT GRGVTVVVVD DGVEHTIKDI QPNYSPEGSY DLNSNDPDPM
PHPDEENGNH HGTRXXVPNN SFCTVGVAYG SRIAGIRVLD GPLTDSMEAI AFNKHYQIND
IYSCSWGPDD DGKTVDGPHQ LGKAALQHGV IAGRRGFGSI FVVASGNGGQ HNDNCNYDGY
ANSIYTVTIG AVDETGSMPF YAEECASMLA VTFSGGDKMM RSIVTTDWDL QKGTGCTEGH
TGTSAAAPLA AGMIALMLQV RPCLTWRDVQ HIIVFTATKY EDRHAKWDTN QAGFSHSHQH
GFGLLNAWRL VNAAKIWESV PYLASYVSPA LRAGRSIPLL PRELEVAWNV SAADLQLSGM
KTLEHVAVTV TITHPRRGNL EIRLFCPSGM MSLIGTARSM DSDPNGFADW TFSTVRCWGE
EAQGTYRLVI RDIGDESLRP GTLKQWQLTL YGSSWSPAEM RERQRLLEEA MSGRYLSSDF
SLPCPPGLQI PEEQRYTITA NTLKTLLLLG CFAVFWTFYY MLEVCLSRNN AGLDLSCSGS
AACRWYQQGG KHRALESGLE MESVPLYREK DVEDVEMECE HPQPAQQDEG EEEEGSWTPT
HPELSGRATS FPEAAPVGAG HRGREAPTEL LSEDRERQPC
//
