ID   MBSP_SAUUN              Reviewed;          22 AA.
AC   P84478;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Myofibril-bound serine protease;
DE            Short=MBSP;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Saurida undosquamis (Brushtooth lizardfish) (Saurus undosquamis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Aulopa; Aulopiformes;
OC   Aulopoidei; Synodontidae; Harpadontinae; Saurida.
OX   NCBI_TaxID=143315;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Skeletal muscle {ECO:0000269|PubMed:14698920};
RX   PubMed=14698920; DOI=10.1016/j.cbpc.2003.10.015;
RA   Ohkubo M., Miyagawa K., Osatomi K., Hara K., Nozaki Y., Ishihara T.;
RT   "Purification and characterization of myofibril-bound serine protease from
RT   lizard fish (Saurida undosquamis) muscle.";
RL   Comp. Biochem. Physiol. 137B:139-150(2004).
CC   -!- FUNCTION: Serine protease which degrades the myosin heavy chain and
CC       tropomyosin, but not actin. Selectively cleaves Arg-|-Xaa bonds.
CC       {ECO:0000269|PubMed:14698920}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.0. Active from pH 5.0 to 11.0.
CC         {ECO:0000269|PubMed:14698920};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius. Active from 20 to 70
CC         degrees Celsius. {ECO:0000269|PubMed:14698920};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14698920}.
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC       {ECO:0000269|PubMed:14698920}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   AlphaFoldDB; P84478; -.
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..>22
FT                   /note="Myofibril-bound serine protease"
FT                   /id="PRO_0000088721"
FT   DOMAIN          1..>22
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         22
FT                   /evidence="ECO:0000303|PubMed:14698920"
SQ   SEQUENCE   22 AA;  2454 MW;  61FE979A32F10E65 CRC64;
     IVGGYECEAY SKPYQVSINL GY