ID   MBSP_SAUWA              Reviewed;          10 AA.
AC   P84476;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Myofibril-bound serine protease;
DE            Short=MBSP;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Saurida wanieso (Wanieso lizardfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Aulopa; Aulopiformes;
OC   Aulopoidei; Synodontidae; Harpadontinae; Saurida.
OX   NCBI_TaxID=315323;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Skeletal muscle {ECO:0000269|PubMed:10817913};
RX   PubMed=10817913; DOI=10.1016/s0305-0491(99)00176-5;
RA   Cao M.J., Osatomi K., Hara K., Ishihara T.;
RT   "Identification of a myofibril-bound serine proteinase (MBSP) in the
RT   skeletal muscle of lizard fish Saurida wanieso which specifically cleaves
RT   the arginine site.";
RL   Comp. Biochem. Physiol. 125B:255-264(2000).
CC   -!- FUNCTION: Serine protease which degrades the myosin heavy chain but not
CC       actin or alpha-actinin. Selectively cleaves Arg-|-Xaa bonds.
CC       {ECO:0000269|PubMed:10817913}.
CC   -!- ACTIVITY REGULATION: Inhibited by the serine protease inhibitors
CC       Pefabloc SC, STI, aprotinin, benzamidine, leupeptin and antipain, and
CC       by the cysteine proteinase inhibitors DTNB and pCMB. Not inhibited by
CC       the cysteine protease inhibitor E-64, the aspartic proteinase inhibitor
CC       pepstatin A and the metalloproteinase inhibitor EDTA.
CC       {ECO:0000269|PubMed:10817913}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. Active from pH 5.0 to 11.0.
CC         {ECO:0000269|PubMed:10817913};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. Active from 30 to 65
CC         degrees Celsius. {ECO:0000269|PubMed:10817913};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10817913}.
CC   -!- TISSUE SPECIFICITY: Detected in muscle (at protein level).
CC       {ECO:0000269|PubMed:10817913}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   GO; GO:0005737; C:cytoplasm; 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   Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Serine protease.
FT   CHAIN           1..>10
FT                   /note="Myofibril-bound serine protease"
FT                   /id="PRO_0000088722"
FT   DOMAIN          1..>10
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:10817913"
SQ   SEQUENCE   10 AA;  1007 MW;  22935FCEBB1DD878 CRC64;
     IVGGAECVPY