UniProt: A0A3Q7SLE6

Database: UniProt
Entry: A0A3Q7SLE6_VULVU

LinkDB:  A0A3Q7SLE6_VULVU 
Original site:  A0A3Q7SLE6_VULVU

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (28)   
   InterPro (15)   
   Pfam (4)   
   PROSITE (6)   
   SMART (3)   
All databases (33)   

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ID   A0A3Q7SLE6_VULVU        Unreviewed;      1885 AA.
AC   A0A3Q7SLE6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 5 isoform X1 {ECO:0000313|RefSeq:XP_025857318.1};
GN   Name=PCSK5 {ECO:0000313|RefSeq:XP_025857318.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025857318.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025857318.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857318.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025857318.1};
RG   RefSeq;
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_025857318.1; XM_026001533.1.
DR   KEGG; vvp:112922097; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 17.
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; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   Pfam; PF14843; GF_recep_IV; 2.
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; 14.
DR   SMART; SM01411; Ephrin_rec_like; 4.
DR   SMART; SM00261; FU; 22.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 6.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1885
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018790532"
FT   TRANSMEM        1770..1790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          461..601
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        386
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1885 AA;  209382 MW;  B0634F1E1635C37E CRC64;
     MGWGSRGCGP GRLDLLCVLA LLGGCLLPVC RTRVYTNHWA VKIAGGFPEA DRIASKYGFI
     NIGQIGALKD YYHFYHSRTI KRSVLSSRGT HSFISMEPKV EWIQQQVVKK RTKRDYDFSR
     AQPTYFNDPK WPSMWYMHCS DNTHPCQSDM NIEGAWKRGY TGKNIVVTIL DDGIERTHPD
     LMQNYDALAS CDVNGNDLDP MPRYDASNEN KHGTRCAGEV AAAANNSHCT VGIAFNAKIG
     GVRMLDGDVT DMVEAKSVSF NPQHVHIYSA SWGPDDDGKT VDGPAPLTRQ AFENGVRMGR
     RGLGSVFVWA SGNGGRSKDH CSCDGYTNSI YTISISSTAE SGKKPWYLEE CSSTLATTYS
     SGESYDKKII TTDLRQRCTD NHTGTSASAP MAAGIIALAL EANPFLTWRD VQHVIVRTSR
     AGHLNANDWK TNAAGFKVSH LYGFGLMDAE AMVMEAEKWT TVPQQRVCVE STDRQIKTIR
     PNSAVRSIYK ASGCSDNPNH HVNYLEHVVV RITITHPRRG DLAIYLTSPS GTRSQLLANR
     LFDHSMEGFK NWEFMTIHCW GERATGDWIL EVYDTPSQLR NFKTPGKLKE WSLVLYGTSV
     QPYSPTNEFP KVERVRYSRV EDPTDDYGTE DYAGPCDPEC SEVGCDGPGP DHCNDCLNYY
     YKLKNNTRIC VSSCPSGHYH ADKKRCRKCA LNCESCFGSH ADQCLSCKYG YFLNEEINSC
     VIHCPDGSYP DTKKNLCRKC SENCKTCTEF QNCTECRDGL SLQGSRCSIT CEDGQYFNGQ
     DCQPCHRFCA TCAGPGADGC INCTEGYFME DGRCVQSCSL SYYFDHSSEN GYKSCKKCDA
     SCLTCNGPGF KNCTSCLSGY LLDLGTCQMG AICKDGEYID EHGHCQICEA SCATCWGPTQ
     EDCTSCPITR ILDKGRCVFK CPSGKFEFQN QCHLCHYTCQ ECQGNEPSNC TSCGVDNQGQ
     ERFLYQGECW ESCPAGHYPA EGHTCLPCSD NCELCHSAPI CVRCMSGYFV VPTNHTCQKL
     QCGQGQIQDP DYEECVPCEE GCLGCSLDDP GTCTSCTMGY YMFDHHCYKT CPEKTYSEEF
     ECKACDTNCS NCDQHECYWC EEGFFLLGGT CVRRCGPGFY GNPEVGECEP CHPACKSCVG
     LGPHQCSSCQ EGLQLQHGTC VGPAQPHVEG KFWNEPVPTA SPSLVKSLPQ KPRRKFQIKR
     DILRGHQPCH PSCKTCGESA TQCTSCPKGT YLLAQACVSS CPEGTWPSAR NGSCENCTED
     CASCSGANLC TKCQTWPDFP VFLHKGRCYT TCPEGFYAED SMCTPCSSPC RTCEGNATNC
     HSCQGSLILH QGACWEACPE RHVAMEGVCK HCPEMCQDCI HEKTCKECMP QSFLYKDMCH
     QSCPQSFYAD LGQCIPCHED CLECSGPSAD DCDLCAEPSL VFYDGQCLDE CPAGTYYEKE
     TKDCRDCHKS CQTCLSPGTC TTCQEGLQIN SHGTCMPHKE CTHSEYWDVQ ALKCKPCHAK
     CFRCTGPTEE QCHSCPRDSL LLNTICVPDC PEGYYTDEDS HQCVPCHNSC RTCEGRRSTQ
     CLSCQPGLFQ LEKECLLYCR EGYYAEISTG RCERCSKSCK TCRGPGPTDC LSCDTFFFLL
     RSKGECHPTC PEHYYAEQKN KTCERCHPTC DKCEGKGAWN CLSCVWSYHL MGGICASDCL
     VGEYRVGKGD NFTCEKCHES CVECKGPGTK NCTVCPASLL LLMDDGRCLH CCNVSDPSHT
     QECCDCRDTT EECILQSSEI GPAGEHTKTA LLITSSVMLV LLLGAAVIVW KKSRGRGEPV
     AKPGYEKLAD PNKSYVSYKS SHHQSTSFEE DQVIEYRDRD YDEDDDDDIV YMGQDGTVYR
     KFKYGLLDDD EEDELEYDDE SYSYQ
//

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