ID   MCPT1_RAT               Reviewed;         260 AA.
AC   P09650;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Mast cell protease 1;
DE            Short=rMCP-1;
DE            EC=3.4.21.39;
DE   AltName: Full=Chymase;
DE   AltName: Full=Chymotrypsin-like protease;
DE            Short=CLIP protein;
DE   AltName: Full=Mast cell protease I;
DE            Short=rMCP-I;
DE   Flags: Precursor;
GN   Name=Mcpt1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Mast cell;
RX   PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA   Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT   "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT   serine proteases and a carboxypeptidase A from various rat mast cell
RT   populations.";
RL   J. Exp. Med. 185:13-29(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-260.
RX   PubMed=8135800; DOI=10.1006/bbrc.1994.1270;
RA   Rouleau A., Garbarg M., Schwartz J.C., Ruat M.;
RT   "Molecular cloning of rat mast cell protease 1 and development of specific
RT   probes for its gene transcript.";
RL   Biochem. Biophys. Res. Commun. 199:593-602(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-247.
RX   PubMed=3122823; DOI=10.1021/bi00396a020;
RA   le Trong H., Parmelee D.C., Walsh K.A., Neurath H., Woodbury R.G.;
RT   "Amino acid sequence of rat mast cell protease I (chymase).";
RL   Biochemistry 26:6988-6994(1987).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-73.
RX   PubMed=103093; DOI=10.1073/pnas.75.11.5311;
RA   Woodbury R.G., Everitt M., Sanada Y., Katunuma N., Lagunoff D., Neurath H.;
RT   "A major serine protease in rat skeletal muscle: evidence for its mast cell
RT   origin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:5311-5313(1978).
RN   [5]
RP   PROTEIN SEQUENCE OF 21-34; 91-101 AND 232-238, AND FUNCTION.
RX   PubMed=8336143; DOI=10.1111/j.1471-4159.1993.tb02160.x;
RA   Nelson R.B., Siman R., Iqbal M.A., Potter H.;
RT   "Identification of a chymotrypsin-like mast cell protease in rat brain
RT   capable of generating the N-terminus of the Alzheimer amyloid beta-
RT   protein.";
RL   J. Neurochem. 61:567-577(1993).
CC   -!- FUNCTION: Major secreted protease of mast cells with suspected roles in
CC       vasoactive peptide generation, extracellular matrix degradation, and
CC       regulation of gland secretion. May participate in generating
CC       perivascular beta-protein which ultimately aggregates into amyloid-beta
CC       deposits. {ECO:0000269|PubMed:8336143}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa >
CC         Leu-|-Xaa.; EC=3.4.21.39;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasmic granule
CC       {ECO:0000250}. Note=Mast cell granules. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; U67915; AAB48268.1; -; mRNA.
DR   EMBL; S69206; AAB30269.1; -; mRNA.
DR   PIR; JC2125; JC2125.
DR   RefSeq; NP_001264597.1; NM_001277668.1.
DR   AlphaFoldDB; P09650; -.
DR   SMR; P09650; -.
DR   STRING; 10116.ENSRNOP00000069831; -.
DR   MEROPS; S01.149; -.
DR   PaxDb; 10116-ENSRNOP00000028012; -.
DR   Ensembl; ENSRNOT00000090206.2; ENSRNOP00000069831.1; ENSRNOG00000053494.2.
DR   Ensembl; ENSRNOT00055020565; ENSRNOP00055016566; ENSRNOG00055012101.
DR   Ensembl; ENSRNOT00060043142; ENSRNOP00060035701; ENSRNOG00060024940.
DR   Ensembl; ENSRNOT00065053951; ENSRNOP00065044384; ENSRNOG00065031282.
DR   GeneID; 100360872; -.
DR   KEGG; rno:100360872; -.
DR   UCSC; RGD:3062; rat.
DR   AGR; RGD:2321286; -.
DR   CTD; 100360872; -.
DR   RGD; 3062; Mcpt1.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   HOGENOM; CLU_006842_1_0_1; -.
DR   InParanoid; P09650; -.
DR   OMA; CVGSPRK; -.
DR   OrthoDB; 2540265at2759; -.
DR   PhylomeDB; P09650; -.
DR   TreeFam; TF333630; -.
DR   PRO; PR:P09650; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000053494; Expressed in esophagus and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24271:SF23; CHYMASE 2, MAST CELL-RELATED; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   Genevisible; P09650; RN.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..20
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:103093,
FT                   ECO:0000269|PubMed:3122823, ECO:0000269|PubMed:8336143"
FT                   /id="PRO_0000027439"
FT   CHAIN           21..260
FT                   /note="Mast cell protease 1"
FT                   /id="PRO_0000027440"
FT   DOMAIN          21..244
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        65
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CONFLICT        56..58
FT                   /note="TRQ -> NRN (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70..71
FT                   /note="ET -> NE (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91..94
FT                   /note="KVEK -> ALEI (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  28617 MW;  076278089C1F8A96 CRC64;
     MQALLFLMAL LLPSGAGAEE IIGGVESRPH SRPYMAHLEI TTERGYKATC GGFLVTRQFV
     MTAAHCKGRE TTVTLGVHDV SKTESTQQKI KVEKQIVHPN YNFYSNLHDI MLLKLQKKAK
     VTPAVDVIPL PQPSDFLKPG KMCRAAGWGQ TGVTKPTSNT LREVKQRIMD KEACKNYFHY
     NYNFQVCVGS PRKIRSAYKG DSGGPLVCAG VAHGIVSYGR GDAKPPAVFT RISPYVPWIN
     KVIKGKDLTS LSLHESESPS
//