ID   FIBC_LUMRU              Reviewed;         242 AA.
AC   P83298;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Fibrinolytic enzyme, isozyme C;
DE            Short=F-II;
DE            EC=3.4.21.-;
OS   Lumbricus rubellus (Humus earthworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Lumbricus.
OX   NCBI_TaxID=35632 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Nakajima N., Sugimoto M.;
RT   "Structural analysis of earthworm serine proteases.";
RL   Submitted (MAR-2002) to UniProtKB.
CC   -!- MISCELLANEOUS: In L.rubellus there are at least three isozymes of
CC       fibrinolytic enzyme. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   PIR; PN0655; PN0655.
DR   AlphaFoldDB; P83298; -.
DR   SMR; P83298; -.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW   Hemostasis; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..242
FT                   /note="Fibrinolytic enzyme, isozyme C"
FT                   /id="PRO_0000088689"
FT   DOMAIN          1..242
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        44
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        191
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        127..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        158..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        187..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   242 AA;  24837 MW;  F912425D2724745D CRC64;
     VIGGTNASPG EFPWQLSQQR QSGSWSHSCG ASLLSSTSAL SASHCVDGVL PNNIRVIAGL
     WQQSDTSGTQ TANVDSYTMH ENYGAGTASY SNDIAILHLA TSISLGGNIQ AAVLPANNNN
     DYAGTTCVIS GWGRTDGTNN LPDILQKSSI PVITTAQCTA AMVGVGGANI WDNHICVQDP
     AGNTGACNGD SGGPLNCPDG GTRVVGVTSW VVSSGLGTCL PDYPSVYTRV SAYLGWIGDN
     SR