ID A0A1S3HCF5_LINUN Unreviewed; 1024 AA.
AC A0A1S3HCF5;
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=Proprotein convertase subtilisin/kexin type 7-like isoform X1 {ECO:0000313|RefSeq:XP_013383685.1};
GN Name=LOC106154020 {ECO:0000313|RefSeq:XP_013383685.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013383685.1};
RN [1] {ECO:0000313|RefSeq:XP_013383685.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013383685.1};
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_013383685.1; XM_013528231.2.
DR AlphaFoldDB; A0A1S3HCF5; -.
DR STRING; 7574.A0A1S3HCF5; -.
DR EnsemblMetazoa; XM_013528231.2; XP_013383685.1; LOC106154020.
DR GeneID; 106154020; -.
DR KEGG; lak:106154020; -.
DR InParanoid; A0A1S3HCF5; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_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 PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR PANTHER; PTHR42884:SF28; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 7; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 641..777
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 149..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 388
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 565
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1024 AA; 113740 MW; 7645092DDB601637 CRC64;
MDCELQGIKA IMKMLIIKSN NMQVRSKGAL CAWLCIFTLL QHTMNADAME KHVKHHIDTK
YHSAKIHSWA VKLQDSEHFY YYSSRCEHIK NIANSVSRAI ADRLNGGLLS NSKIRASVVF
YPMEYLQHFD IYMLELRLNN IPVSNVKETG ASDAETKPSL GKVSRSQNAK VSQFDSSQKP
LKKETFLYPK SVIKLTKHDS QGVFPESSQK SYIENTFLFL HSKTFKKQTM DMDSKSHKYQ
LIGDNIRTEN EDILSKPGSR EDLYLNSSTY LREVIQTVHH IMDVSPEVLW YSQQVIRPRV
KRGWNFKDPA YPRQWHLHNE VNPQMDINVQ EVWSRNISGR GVTVVVVDDG LEWTNPDIQD
NYSPQGSWDL NSHDSDPMPA INKDKNHHGT RCAGEIGAVA NSVCAVGVAF QAKVAGIRVL
DGPMTDSLEA TAFNKNMEVN DIYSCSWGPD DDGKTVDGPH ILAQTAMEKG VNFGRQGYGS
IYVVASGNGG FHGDNCNFDG YANSVYTVTI GAVDELGNMP YYAEECASML AVTFSSGGPG
LRNVVTTDWM VRGGTGCTDE HSGTSAAAPL AAGMIALMLQ ARSCLTWRDV QHIIVMTAVK
VDEQAGHFTT NQAGLHHSHK HGFGLLDAWR LVNAAKVWDP VPWMSTYSSQ EVTVHTKIPR
HPQVLELNMT VSEEVLAGYN LFLLEHVQVT VTLSHPHRGS LDIHVTCPSG TDSVIATPRP
KDSSSDGFQG WTFSTVRCWG ENPVGIWKLK VTDRGNHIFP FGIFEKWQLV LFGSQMNRGN
FEARKRLISD AVSGRYLYDN FTKPCPPPPA NQGPEASIPP KTLKIILLIG VFCFLVALYD
TFEYMFCYND EKKAALVQPG SAGSMATSGS HVNNSHVNNP GNRGSEYARL LSNIEENIPM
VEMPRNIPDR TSADRQSSFH DNSSYDSTRE ADSGQNSHHN FSQYQHNSNA DSSVLYDSEV
DGDLGLGSTG QNTKSVGAFS QAANIERSGK ETGIQKWKKT MSKLSMGKFE EVSLLSSPDG
DVSE
//
