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Database: UniProt
Entry: A0A1S3KTJ4_SALSA
LinkDB: A0A1S3KTJ4_SALSA
Original site: A0A1S3KTJ4_SALSA 
ID   A0A1S3KTJ4_SALSA        Unreviewed;      1895 AA.
AC   A0A1S3KTJ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 5-like {ECO:0000313|RefSeq:XP_013982013.1};
GN   Name=LOC106562014 {ECO:0000313|RefSeq:XP_013982013.1};
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_013982013.1};
RN   [1] {ECO:0000313|RefSeq:XP_013982013.1}
RP   IDENTIFICATION.
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_013982013.1; XM_014126538.1.
DR   STRING; 8030.ENSSSAP00000078650; -.
DR   KEGG; sasa:106562014; -.
DR   OrthoDB; 5474719at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa01.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; 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; 14.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SMART; SM00261; FU; 22.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 7.
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; 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:UP000087266};
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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1895
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010324487"
FT   TRANSMEM        1770..1791
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          480..620
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          193..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1796..1833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1871..1895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        405
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1895 AA;  207342 MW;  13CE6699A2E2A334 CRC64;
     MTRNVPLSTG MVVLSAFLWM GSLVPLCQPL IYTNDWAVRI NGAPASADSI AEKYGFHNLG
     QIGDLNNFYS FRHSGTVERS TLSNKDFTDL IAKETKVEWV QQQVVHWRTK RNSRASHIYS
     IDVRTKHIHP GPVQPNQTQT LVFNDPQWCS LWYIHCSEGS QGCPSYMNIE GAWRRGHTGK
     GVVVSVLDDG IEREHPDLRP NYDPFASYDF NGNDDDPTPR YDSSNDNSHG TKCAGMVAAA
     ANNSQCTVGI SFNARIGGIR MLDGDVTDIV EAQSLSFRQQ HIDIYSASWG PEDDGRTVEG
     PGPLARLALD NGIRTGRKGR GSIFVWASGN GGRSRDHCSC DGYTNSIYTI SISSTTHSGA
     RPDYLEPCPS TLASTYSSFS TDRQGAKMVT LDLKQGCSKE HSGTSVSAPM AAGVIALALE
     ANPLLTWRDV QHIIVRTSQA SHLTSPDWHT NGAGYQVSHL YGFGLLDAES MVKEAERWRL
     VPSQHVCKEA PTQQSRTIPP GLVLRSVYES TGCSLHPLQH IVYLEHVVIH VTITHSHRGD
     LSITLTSPTG TKSQLLANRP LDHSTEGFQS WEFMTTHCWG EKASGDWSLE VLDTPSQQRD
     NSETGELREW SLVLYGTSEQ PYSMRREQAR SAELPTDGGD LTEEYNGRCD PECSEDGCEG
     PGPQQCVTCL HLFLKFKNNT RTCVSVCPVG FWGDRRRCKK CFSSCEICTG SRSDQCTTCR
     AGHHLTEGTS SCTASCGDNY YLDHDANMCR KCSENCLRCT SANICTECKS GTSLLGNRCQ
     RSCGPGSYHN EQESTCEPCH EACATCAGAG IESCNQCADG YLMEEWRCVS SCSVGFYATE
     SSPQKTSDGP RICRRCDSSC LTCVGAGKGN CSSCAGGHSL MDKMCMVSTV CGDGEYQDSH
     GKCHACDATC LKCTGPKSEE CISCGPSRSL DQGCCVAQCA RGKYQSGGQC HLCDHTCAMC
     LDGGPANCTS CDTDKFNMDR YLYKGGCVDA CPEGHYHTQE KSCEACPDNC KLCSSATHCL
     RCNSSYYTTD GVCTRLECGE GEVEDPEYDD CMACEEGCKK CVLYNPRHCL SCTDGFYKFQ
     DGCYKNCPAK TFSVEEEMTC VPCDEKCVSC DEHECYWCET DLFLSEGKCV PECPDGFYGD
     EDTQECEECH SDCVTCSGPD SDDCVLCEEG TSREEGECVS KQDSCPVKTF LTGEGECEAC
     HASCDSCSGE EKSQCKTCVK GRFLSAEQVC VLKCPASSFA SRLSGVCEPC PRGCAQCVDE
     HRCTRCQVVR KAPLYLQDGQ CVRQCQSGYA AGQVCRGCAT GCASCEKNAT HCLSCVEPFL
     LYKHHCVEAC PPAHTLRDGE CQHCPTACQE CSPNSECTGC EEYHFLYEGR CVMDCPERFF
     RDSEQDVCVR CHPDCARCDG PDGDDCDSCA DPEATLHNGA CLPNCPSHTY RDSRTGQCKD
     CDGSCLTCSG PHAGSCSSCR EGQKLDAEGQ CDPLVNRCTP RHYTDQDGEC HPCHKYCQQC
     NGPGKSHCLS CNQNHFILNG TCMDFCPTGF YQEESSQRCE GCHPACLTCM GRHSHECLSC
     KDHLFREGKE CVDTCQPSHY GNMTSRTCER CDPSCGECSG GRADGCLNCA DGLLYLRKQG
     RCHSSCPQGH YQDSQHHTCE PCHSSCRTCS GKGSQACDLC HMGYTLSDGM CESHCNMGQY
     PVLQDCEDCD GSCLDCSGPG PYNCTICPAH AILTAGGRCL LCCQNDLPVE GDSTAQQQQE
     CCNCTETRGE CVLSTNLAFR NDEEESTGNM ALFITTSILL LLGLGTIVFL IRRSRSKSPS
     LPDPITAPRG YEKLGGGRHN TTSAGHASSS GHFREAQLVD LTDRYGDKDE EDEDEDEDIV
     YMGQDGTVYR KFRYGQPGND NDDELEYDDE SYTFR
//
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