ID A0A2K6G0G6_PROCO Unreviewed; 788 AA.
AC A0A2K6G0G6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 7 {ECO:0000313|Ensembl:ENSPCOP00000019716.1};
GN Name=PCSK7 {ECO:0000313|Ensembl:ENSPCOP00000019716.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000019716.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000019716.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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DR RefSeq; XP_012513787.1; XM_012658333.1.
DR RefSeq; XP_012513789.1; XM_012658335.1.
DR AlphaFoldDB; A0A2K6G0G6; -.
DR STRING; 379532.ENSPCOP00000019716; -.
DR Ensembl; ENSPCOT00000030367.1; ENSPCOP00000019716.1; ENSPCOG00000021815.1.
DR GeneID; 105821599; -.
DR KEGG; pcoq:105821599; -.
DR CTD; 9159; -.
DR GeneTree; ENSGT00940000157676; -.
DR OMA; NGRMPFY; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
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; 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: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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 481..618
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 197..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 406
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 788 AA; 86592 MW; DBDEE2F5C9AEB349 CRC64;
MPKGRQRVPH LDAPLGLPTC FWLELAGLFL LVPWVMCLAG TGGPEAQGPG GLSWAVHLDS
LEGEGAEETL EQQADALAHA AGLVNAGRIG ELRGHYLLVQ PAGRGQALEV EAIRQQAEAV
LARHETVRWH SEQRLLKRAK RSVHFNDPKY PQQWHLYNRR SPGRDINVTG VWERNVTGRG
VTVVVVDDGV EHTIQDIAPN YSPEGSYDLN SNDPDPMPHP DVENGNHHGT RCAGEIAAVP
NNSFCAVGVA YGSRIAGIRV LDGPLTDSME AVAFNKHYQI NDIYSCSWGP DDDGKTVDGP
HQLGKAALQH GVIAGRQGFG SIFVVASGNG GQHNDNCNYD GYANSIYTVT IGAVDEEGRM
PFYAEECASM LAVTFSGGDK MLRSIVTTDW DLQKGTGCTE GHTGTSAAAP LAAGMIALML
QVRPCLTWRD VQHIIVFTAT QYEDRHADWV TNEAGFSHSH QHGFGLLNAW RLVNAAKIWT
SVPYLASYVG PVLKENKAIP QSPRSLEVLW NVSRMDLEMS GLKTLEHVAV TVSITHPRRG
SLELKLVCPS GMMSLIGAPR SMDSDPNGFN DWTFSTVRCW GERAKGVYRL VVRDVGDESL
QVGILRQWQL TLYGSVWSPV DIRDRQRLIE SAMSGKYLHD SFALPCPPGL KIPEEDGYTI
TPNTLKTLVL IGFFTVFWTI YYMLEIYLSQ RHVASKPLCR SGPCHWPQRS RKAREEGTEL
ESVPLCNRKD VDGVEAESGG LPTTSGLLAP DLLDEGDWTL SQNNRSALDC PHQHRPIDLL
QGKEEQIC
//
