MCPT1_RAT
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 03-AUG-2022, entry version 164.
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.ENSRNOP00000028012; -.
DR MEROPS; S01.149; -.
DR PaxDb; P09650; -.
DR PRIDE; P09650; -.
DR Ensembl; ENSRNOT00000090206; ENSRNOP00000069831; ENSRNOG00000053494.
DR GeneID; 100360872; -.
DR KEGG; rno:100360872; -.
DR UCSC; RGD:3062; rat.
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; SEQIVHP; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P09650; -.
DR TreeFam; TF333630; -.
DR PRO; PR:P09650; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000053494; Expressed in esophagus and 12 other tissues.
DR Genevisible; P09650; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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
