ID A0A1S3PJW2_SALSA Unreviewed; 919 AA.
AC A0A1S3PJW2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 5 isoform X3 {ECO:0000313|RefSeq:XP_014027664.1};
GN Name=pcsk5 {ECO:0000313|RefSeq:XP_014027664.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014027664.1};
RN [1] {ECO:0000313|RefSeq:XP_014027664.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014027664.1};
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_014027664.1; XM_014172189.1.
DR AlphaFoldDB; A0A1S3PJW2; -.
DR GeneID; 106585692; -.
DR CTD; 559556; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR Bgee; ENSSSAG00000068019; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 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: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; 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:UP000087266};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..919
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010259164"
FT DOMAIN 468..608
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 875..919
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 178
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 219
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 393
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 919 AA; 102271 MW; F941E9018BFAE097 CRC64;
MVWNAALRRG LMCVLALWLG FTSAPCKARI YTNHWAVRIN GGPVFADRIA DKYGYKNMGQ
IGDLKDHYHF FHSRTIKRST LSSRGGHSFI SMESKVEWIQ QQVVKRRIKR DYKAAPPPLT
SPAQTSPAQS IFFNDAKWSS MWYIHCNDDI HNCQSDMNIV GAWKRGYTGK DVVITILDDG
IERNHPDLIQ NYDNQASYDV NGNDMDPMPR YDASNENKHG TRCAGEVAAS ANNSHCTVGI
AYNARIGGVR MLDGDVTDMV EAKSLSLQPQ HIDIYSASWG PDDDGKTVDG PASLARQAFE
NGIRMGRKGR GSIFVWASGN GGRSRDHCSC DGYTNSIYTI SISSTAESGR KPWYLEECSS
TLTTTYSSGE NYDRKIITTD LRQRCTDSHT GTSASAPMAA GIIALALEAN PLLSWRDVQH
IIVKTSRAGH LNAPDWKTNA AGYNVSHLYG FGLMDAEAMV KEAERWKQVP AQHICVESAD
RQIRTIRPEH VVRSVYKATG CIDNSNHHVI YLEHVVVRIT ITHPRRGDLS INLTSPSGTK
SQLLGNRLFD HSMEGFKNWE FMTTHCWGEK AAGDWILEIH DSPSQLRSQK VPGKLKEWSL
VLYGTSVHPY SSLRSDKPRS AEPPADEEFT EEYNGLCNSE CNENGCEGPG PHQCINCLHY
FLKFKNNTRT CVSECPSGFF RDDRKRCKKC SSLCEMCVGS RSDQCSTCRP GFHLNEGSNN
CVASCVDGFY LDHDSNMCRR CNENCKKCTT SNICTECKPG MSLQGNKCQM TCDPGTYYNG
HRRTCEQCHR ACATCAGTGM EACNKCAEGY FLEEWRCVST CSVGYYMSEQ TSDNGDVNKS
CRKCDHSCYA CTGPGETNCS TCVNGYNLEA GVCVVSTICK DANEESWAEG SFCVLVKKNN
LCQRKVLQQL CCRTCSLKG
//
