ID A0A1S3KPG7_SALSA Unreviewed; 845 AA.
AC A0A1S3KPG7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Furin-like isoform X2 {ECO:0000313|RefSeq:XP_013980578.1};
GN Name=LOC106561302 {ECO:0000313|RefSeq:XP_013980578.1};
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_013980578.1};
RN [1] {ECO:0000313|RefSeq:XP_013980578.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013980578.1};
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 RefSeq; XP_013980578.1; XM_014125103.1.
DR AlphaFoldDB; A0A1S3KPG7; -.
DR GeneID; 106561302; -.
DR CTD; 566591; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
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; 1.
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; 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:SF11; FURIN PRECURSOR; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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; SM00261; FU; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
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}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..845
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010208236"
FT TRANSMEM 733..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..581
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 100..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 845 AA; 91829 MW; 08FB53B1CC23B646 CRC64;
MDARLALLQL GTLLGLLYLA LELTAELTAA EEVYTNTWAV HIEGGPQEAD RIARKHGFIN
HGNVFGGYYH FRHHTVVKRS LSGHRGTHVR LQKEPQVRWA EQQVSRRRKK RDVYTEPSDP
KFPQQWYLSN PSQADLNAKG AWSQGYTGRG VVVTILDDGI EKDHPDLATN YDPEASYDVN
DGDSDPQPRY TQRNENRHGT RCAGEVAAAA NNNVCGVGVA YNTKIGGVRM LDGEVTDMVE
AHSLSLNSQH IHIYSASWGP EDDGKTVDGP AKLAKEAFLR GVTEGRGGLG SIFVWASGNG
GREKDSCNCD GYTNSIYTLS ISSTTQYGMV PWYSEACSST LATTFSSGNP NEKQIVTTDL
RQKCTDSHTG TSASAPLAAG IIALALEANM NLTWRDMQHL VVRTSHPAHL STDDWSTNGV
GRRVSHSYGY GLLDAGAMVA LAQNWTSVDP QHQCVLTMLS EPRDISSRLL FSKTLDACWG
KPEYVSSLEH VQARLTLSYN HRGNLAIHLI SPLGTRSTLL APRPKDYSSE GFNDWAFMTT
HSWDEDPRGE WTLEIENVSE QGHDYGVLSQ FTLILYGTGS SSINPLSPDF PRPSNNSCKT
FDAQQICIEC SPGFSLFLQG CVKLCPPGFT TGPQLLNLSL DNWVDLSSVQ ACLPCHPACL
TCSGSGPNDC LSCPPHSHLV LTACLHQNQV QRKSPTGQVL QGERSGPGES PVGSEQGEEG
EPPGPNLGLS SPLVTLLAVL SCAFILAAFA GVFLLLQLRS GGAPWVRRTK LHSVETGGGV
SGGIRVGFGF GLGLGWERQG RVSYKGIPTV WRDEDQVTLG GSESDIEDLD CHSERTAFIR
TQSSL
//
