ID   CL401_COCLU             Reviewed;         506 AA.
AC   B3V0K8;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Subtilisin-like serine protease Cur l 4.0101 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE   AltName: Full=Subtilisin-like serine protease {ECO:0000303|PubMed:20667621};
DE   AltName: Allergen=Cur l 4.0101 {ECO:0000305};
DE   Flags: Precursor;
OS   Cochliobolus lunatus (Filamentous fungus) (Curvularia lunata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=5503 {ECO:0000312|EMBL:ACF19589.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=20667621; DOI=10.1016/j.imbio.2010.06.009;
RA   Tripathi P., Nair S., Singh B.P., Arora N.;
RT   "Molecular and immunological characterization of subtilisin like serine
RT   protease, a major allergen of Curvularia lunata.";
RL   Immunobiology 216:402-408(2011).
CC   -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 81% of
CC       the 16 patients sensitive to C.lunata. Induces histamine release from
CC       basophils. {ECO:0000269|PubMed:20667621}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC       ECO:0000305}.
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DR   EMBL; EU622631; ACF19589.1; -; mRNA.
DR   AlphaFoldDB; B3V0K8; -.
DR   SMR; B3V0K8; -.
DR   Allergome; 3901; Cur l 4.
DR   Allergome; 8438; Cur l 4.0101.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Glycoprotein; Hydrolase; Protease; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..135
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y755, ECO:0000255"
FT                   /id="PRO_0000446900"
FT   CHAIN           136..458
FT                   /note="Subtilisin-like serine protease Cur l 4.0101"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y755, ECO:0000305"
FT                   /id="PRO_5012203775"
FT   PROPEP          459..506
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000446901"
FT   DOMAIN          43..134
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          147..453
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   REGION          59..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        215
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        381
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            316
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   506 AA;  53762 MW;  3F2E356460625E66 CRC64;
     MKYSLIAALP ALAAASPTFS TETIHKQSAP VLSSTSAKEV PNSYMVVFKK HVKDASKHHD
     WVQSVHSKNT QERMELRKRS SDLPVSNEVF AGLKHTYELS GLKGYSGHFD DETLEAIRNH
     PDVDYIERDS EVRILGGDEP ETENNSPWGL ARISHRDSLS FGTWNKYLYA ADGGEGVDVY
     VIDTGTNVDH VDFEGRAKWG KTIPNGDADE DGNGHGTHCS GTVAGKKYGV AKKAHVYAVK
     VLRSNGSGTM SDVVKGVEFA AKSHSEAVSA AKNGKKKGFK GSTANMSLGG GKSTTLDMAV
     NAAVDAGLHF AVAAGNDNAD SCNYSPAAAE NAVTVGASTL LDERAYFSNY GKCNDIFAPG
     LNILSTWIGS KHATNTISGT SMASPHIAGL LAYMLSLQPA KDSAYAVADI TPKKLKANLI
     AIGTVGALSD VPSNTANVLA WNGGGSSNYT DIIEKGGYTV KKAASKEEEK ESEFRITIPS
     LSELEDDFEK AKESAGRKAH HVGGKL