ID   ASPR_TERCL              Reviewed;          15 AA.
AC   C0HJJ8;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Alkaline serine protease {ECO:0000303|Ref.1};
DE            Short=AkP {ECO:0000303|Ref.1};
DE            EC=3.4.21.- {ECO:0000269|Ref.1};
DE   Flags: Fragment;
OS   Termitomyces clypeatus (White-rot fungus) (Sinotermitomyces taiwanensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Lyophyllaceae; Termitomyces.
OX   NCBI_TaxID=182030;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=MTCC 5091 {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.ijbiomac.2016.05.034;
RA   Majumder R., Banik S.P., Khowala S.;
RT   "AkP from mushroom Termitomyces clypeatus is a proteoglycan specific
RT   protease with apoptotic effect on HepG2.";
RL   Int. J. Biol. Macromol. 0:0-0(2016).
CC   -!- FUNCTION: Protease capable of hydrolyzing gelatin and cell surface
CC       heparan sulfate proteoglycans (HSPGs) in vitro. {ECO:0000269|Ref.1}.
CC   -!- ACTIVITY REGULATION: Inhibited by serine protease inhibitors
CC       phenylmethanesulphonylfluoride (PMSF) and di-iodopropylfluorophosphate
CC       (DFP). {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 mM for azocasein {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 9. Activity is relatively stable between pH 8-10 but
CC         drops at lower pH and is absent at pH 4. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease.
FT   CHAIN           1..>15
FT                   /note="Alkaline serine protease"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000436784"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1585 MW;  2BF00E824DC27BF8 CRC64;
     GTQTNAPWGL ARLIS