ID G3VXH5_SARHA Unreviewed; 965 AA.
AC G3VXH5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 6 {ECO:0000313|Ensembl:ENSSHAP00000007880.1};
GN Name=PCSK6 {ECO:0000313|Ensembl:ENSSHAP00000007880.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000007880.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000007880.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000007880.1}
RP IDENTIFICATION.
RG Ensembl;
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_003755638.2; XM_003755590.2.
DR AlphaFoldDB; G3VXH5; -.
DR STRING; 9305.ENSSHAP00000007880; -.
DR Ensembl; ENSSHAT00000007943.2; ENSSHAP00000007880.1; ENSSHAG00000006838.2.
DR GeneID; 100921467; -.
DR KEGG; shr:100921467; -.
DR CTD; 5046; -.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000159506; -.
DR InParanoid; G3VXH5; -.
DR OMA; CSTCTGQ; -.
DR OrthoDB; 5474719at2759; -.
DR TreeFam; TF314277; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0048406; F:nerve growth factor binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0032902; P:nerve growth factor production; IEA:Ensembl.
DR GO; GO:0016486; P:peptide hormone processing; IEA:Ensembl.
DR GO; GO:0032940; P:secretion by cell; IEA:Ensembl.
DR GO; GO:0007354; P:zygotic determination of anterior/posterior axis, embryo; IEA:Ensembl.
DR CDD; cd00064; FU; 5.
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:UP000007648};
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 491..631
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 927..965
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 14..34
FT /note="Disordered"
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 965 AA; 106948 MW; 02852784BC2BFB87 CRC64;
MRRSQLLRSL RLLRAGGGEG GGDRGGRDGS CRRGTGSRLQ AMRCLSWLLV LALPTACAAL
RSPTVYTNHW AVEVLGGPAE ADRVASAHGY LNLGQIGNLE NYYHFYHSKT FKRSTFSSRG
THTFLRMDPK VKWLQQQEVK RRVKRHSRSD AHSIYFNDPI WSNMWYMHCG DKHSRCRSEM
NVPAAWKRGY TGKNVVVTIL DDGIERNHPD LAANYDAYAS YDVNGNDYDP SPRYDASNEN
KHGTRCAGEV AASANNSYCI VGIAYNAKIG GIRMLDGDVT DVVEAKSLGI RPNYIDIYSA
SWGPDDDGKT VDGPGRLAKQ AFEYGIKKGR QGLGSIFVWA SGNGGREGDY CSCDGYTNSI
YTISVSSTTE NGYKPWYLEE CASTLATTYS SGAFYEGKIV TTDLRQRCTD GHTGTSVSAP
MVAGIIALAL EANNQLTWRD VQHLLVKTSR PAHLKASDWK VNGAGHKVSH LYGFGLVDAE
GIVVEAKKWK AVPSQHMCIA ASDKRPRIIP IEQTLRTTAL TNACADHFDQ RVVFLEHVVV
RVSISHPRRG DLQIHLISPS GTKSQLLARR LLDHSNDGFT NWEFMTVHCW GEKAEGEWTL
EVHDIPSQVR NPEKTGKLKE WSLILYGTAE HPYNTFSSHQ SRSRMLEIST SELEPSKAAF
FHKQVEATED DEDYTAPSIQ GSPNILQTSV CHPECGDKGC DGPKADQCLN CIHYSLGSIK
TGRKCVNVCP LGYFGDSLSK RCRRCSRGCE TCTGRSQNQC LSCRRGFYYH QELNTCVTLC
PAGFYADESQ KYCFKCHPNC KKCVDEPEKC TICKEGFSLA GGSCILDCAP GTYFNSELIK
CEKCHSTCQT CVGPGKEECI YCVNNFKIHE KKCVPGCNEG FYFAKVPGFL QKVCARCEEN
CLHCEGSSKN CVKCKTGFML LGNTCVANDT CSNAAEMFCE MVKSNNLCER KLFTQLCCRT
CLLAG
//
