ID A0A1I7W4K9_LOALO Unreviewed; 472 AA.
AC A0A1I7W4K9; A0A1S0TWG0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ctsf protein {ECO:0000313|EMBL:EFO21301.2, ECO:0000313|WBParaSite:EN70_9599};
GN ORFNames=LOAG_07188 {ECO:0000313|EMBL:EFO21301.2,
GN ECO:0000313|WBParaSite:EN70_9599};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_9599};
RN [1] {ECO:0000313|EMBL:EFO21301.2, ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_9599}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; JH712331; EFO21301.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7W4K9; -.
DR STRING; 7209.A0A1I7W4K9; -.
DR EnsemblMetazoa; EFO21301.2; EFO21301.2; LOAG_07188.
DR WBParaSite; EN70_9599; EN70_9599; EN70_9599.
DR eggNOG; KOG1542; Eukaryota.
DR InParanoid; A0A1I7W4K9; -.
DR OMA; KNDCDAG; -.
DR OrthoDB; 2872670at2759; -.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00042; CY; 1.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.10.450.10; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF959; CATHEPSIN F; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00031; Cystatin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00043; CY; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54403; Cystatin/monellin; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010392391"
FT DOMAIN 13..123
FT /note="Cystatin"
FT /evidence="ECO:0000259|SMART:SM00043"
FT DOMAIN 170..227
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 259..470
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 472 AA; 53542 MW; A8024B23422A635F CRC64;
MLAKCWIILL GLHVLLAIKK HDPSTEKYED LLSLAMAEYN KGRDDKYWWI PVKVLDIGTI
HNTGMHFSIK IAIALSNCTK IAYTNFNSKD CIAKKATGLK TCTFEMFQPS WKIAGKMKLL
ACSDYVSPEQ LAEMKSHDES DTVNMKVTDP VIDLQNWQEG KKTEMLWNSF LDFIKKFKRE
YSSVAEQLDR FKKYMQNLHF VEKLQHEEKG TAIYGVTQFS DMSPEEFQKT MLPSLWWDRV
VSNGVEYDLK KFNLTFNNLP EQFDWRTKGV VTPVKNQGSC GSCWAFSVTG NIEGLWAIKT
GKLISLSEQE LIDCDRIDKG CNGGLPINAF REIQRMGGLE PEDQYPYKAR NGTCHLIRSA
IAVTIDDAVE IPRNETVMKA WIVQRGPLSV GIDAKLLAYY KSGILHPSRS RCPPSGIDHG
VLITGYGVEN GLPYWTIKNS WGDQWGEDGY FRLMLGKDVC GVSDLVSSAI IY
//