ID Q0P4Q8_XENTR Unreviewed; 911 AA.
AC Q0P4Q8;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 5 {ECO:0000313|EMBL:AAI21946.1, ECO:0000313|RefSeq:XP_031746758.1};
GN Name=pcsk5 {ECO:0000313|RefSeq:XP_031746758.1,
GN ECO:0000313|Xenbase:XB-GENE-959596};
GN Synonyms=fur2 {ECO:0000313|EMBL:AAI21946.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI21946.1};
RN [1] {ECO:0000313|EMBL:AAI21946.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testes {ECO:0000313|EMBL:AAI21946.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_031746758.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031746758.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031746758.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; BC121945; AAI21946.1; -; mRNA.
DR RefSeq; XP_031746758.1; XM_031890898.1.
DR Xenbase; XB-GENE-959596; pcsk5.
DR HOGENOM; CLU_002976_3_0_1; -.
DR Proteomes; UP000008143; Chromosome 1.
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; 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; 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:SF7; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 5; 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; 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 2: Evidence at transcript level;
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:UP000008143};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..911
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041199305"
FT DOMAIN 457..597
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 867..911
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 167
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 911 AA; 101424 MW; AC56B74E8A4C9318 CRC64;
MASKWLPRRC PLVALTVLLG ILIPPCRARM FTNHWAVRIA GGETEANRIA SKYGYTNMGQ
IGALQDYYHF FHSKTIKRSI LSSRGTHSFI SMEPKVEWIQ QQVVKKRIKR DYKPTNTQST
FFNDPKWPSM WYMHCSENVH HCQSDMNIVG AWKRGYTGKN VVVTILDDGI ERNHPDLMQN
YDAQASTDIN GNDFDPMPRY DASNENKHGT RCAGEVAATA NNSHCTVGIA FNAKIGGVRM
LDGDVTDMVE AKSLSLNPQH VHIYSASWGP DDDGKTVDGP ASLAREAFEN GIRTGRRGFG
SVYVWASGNG GRSRDHCSCD GYTNSIYTIS ISSTTESGKK PWYLEECAST LATTYSSGES
YDRKVITTDL RQRCTDSHTG TSASAPMAAG IIALALEANP FLTWRDVQHI IVRTSRQRHL
NAPDWKTNAA GYKVSHLYGF GLMDAEAMVI EAEKWTTVPA QHICVENTDR QIKTIRPDNV
VRSVYKATGC ADNTNHHVVY LEHVVVRVSI THPRRGDLAI YLTSPSGTRS QLLANRLFDH
SMEGFKNWEF MTTHCWGERA SGDWTLEIYD TPSQLRNFKT PGKLKEWSLV LYGTSVHPYS
PRNDVPKVER VRSSPIDEPS EDYSMDDYTG PCDVECSNVG CDGPGPDHCT DCLHFYYKAK
NNTRICVSDC PAGHYLADKK RCKKCFLHCE SCVGSRSDQC TACKPGYYLN EESNSCIINC
PEGFYLNENK VLCRKCNENC KSCTSEQTCT ECKPGLSLQG SKCAMSCEDG KYYSALKKEC
DPCHRSCATC SGPGIDNCIN CTDGTLFEDG KCVHMCSSGY YLTQSKTNAY KICKKCDASC
LTCSGPGDRN CTSCLDNYVL ESSVCVVGTI CKDATEEAWA EGGFCMLVKK NNLCIRKVLQ
QLCCRTCTLK V
//
