CMA1_RAT
ID CMA1_RAT Reviewed; 247 AA.
AC P50339; Q9R2C8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chymase;
DE EC=3.4.21.39;
DE AltName: Full=Alpha-chymase;
DE AltName: Full=Mast cell protease 3;
DE Short=rMCP-3;
DE AltName: Full=Mast cell protease 5;
DE Short=rMCP-5;
DE AltName: Full=Mast cell protease III;
DE Short=rMCP-III;
DE Flags: Precursor;
GN Name=Cma1; Synonyms=Mcpt3;
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 TISSUE=Peritoneal mast cell;
RX PubMed=7487912; DOI=10.1042/bj3110675;
RA Ide H., Itoh H., Tomita M., Murakumo Y., Kobayashi T., Maruyama H.,
RA Osada Y., Nawa Y.;
RT "Cloning of the cDNA encoding a novel rat mast-cell proteinase, rMCP-3, and
RT its expression in comparison with other rat mast-cell proteinases.";
RL Biochem. J. 311:675-680(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-247.
RC STRAIN=Sprague-Dawley;
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).
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. {ECO:0000250}.
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. Cytoplasmic granule. Note=Secretory
CC granules.
CC -!- TISSUE SPECIFICITY: Mast cells.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; D38495; BAA07507.1; -; mRNA.
DR EMBL; U67908; AAB48261.1; -; mRNA.
DR PIR; S59135; S59135.
DR RefSeq; NP_037224.1; NM_013092.1.
DR AlphaFoldDB; P50339; -.
DR SMR; P50339; -.
DR STRING; 10116.ENSRNOP00000061330; -.
DR BindingDB; P50339; -.
DR ChEMBL; CHEMBL3168; -.
DR MEROPS; S01.150; -.
DR GlyGen; P50339; 1 site.
DR PhosphoSitePlus; P50339; -.
DR PaxDb; P50339; -.
DR Ensembl; ENSRNOT00000067539; ENSRNOP00000061330; ENSRNOG00000020563.
DR GeneID; 25627; -.
DR KEGG; rno:25627; -.
DR UCSC; RGD:2365; rat.
DR CTD; 1215; -.
DR RGD; 2365; Cma1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P50339; -.
DR OMA; PQACRHY; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P50339; -.
DR BRENDA; 3.4.21.B5; 5301.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR PRO; PR:P50339; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000020563; Expressed in pancreas and 13 other tissues.
DR Genevisible; P50339; RN.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:RGD.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; NAS:RGD.
DR GO; GO:0042277; F:peptide binding; IMP:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:RGD.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:RGD.
DR GO; GO:0034769; P:basement membrane disassembly; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0140447; P:cytokine precursor processing; ISO:RGD.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:RGD.
DR GO; GO:0030901; P:midbrain development; IEP:RGD.
DR GO; GO:0006518; P:peptide metabolic process; IEP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0016485; P:protein processing; IDA:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..21
FT /note="Activation peptide"
FT /id="PRO_0000027443"
FT CHAIN 22..247
FT /note="Chymase"
FT /id="PRO_0000027444"
FT DOMAIN 22..245
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 144..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 175..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 247 AA; 27569 MW; 6525D7BF1BFDF053 CRC64;
MNLHALCLLL LLLGSSTKAG EIIGGTECIP HSRPYMAYLE IVTSDNYLSA CSGFLIRRNF
VLTAAHCAGR SITVLLGAHN KTYKEDTWQK LEVEKQFIHP NYDKRLVLHD IMLLKLKEKA
KLTLGVGTLP LSANFNFIPP GRMCRAVGWG RTNVNEPASD TLQEVKMRLQ EPQSCKHFTS
FQHKSQLCVG NPKKMQNVYK GDSGGPLLCA GIAQGIASYV HPNAKPPAVF TRISHYRPWI
NKILREN
