CMA1_MOUSE
ID CMA1_MOUSE Reviewed; 247 AA.
AC P21844; Q9R1F0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Chymase;
DE EC=3.4.21.39;
DE AltName: Full=Alpha-chymase;
DE AltName: Full=Mast cell chymase 1;
DE AltName: Full=Mast cell protease 5;
DE Short=mMCP-5;
DE AltName: Full=Mast cell protease I;
DE Flags: Precursor;
GN Name=Cma1; Synonyms=Mcpt5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1939089; DOI=10.1016/s0021-9258(18)54925-5;
RA McNeil H.P., Austen K.F., Somerville L.L., Gurish M.F., Stevens R.L.;
RT "Molecular cloning of the mouse mast cell protease-5 gene. A novel
RT secretory granule protease expressed early in the differentiation of
RT serosal mast cells.";
RL J. Biol. Chem. 266:20316-20322(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Leaden X A1; TISSUE=Mastocytoma;
RX PubMed=2060576; DOI=10.1002/eji.1830210706;
RA Huang R., Blom T., Hellman L.;
RT "Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three mouse
RT mast cell-specific serine proteases.";
RL Eur. J. Immunol. 21:1611-1621(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1376147; DOI=10.1016/0167-4838(92)90340-j;
RA Chu W., Johnson D.A., Musich P.R.;
RT "Molecular cloning and characterization of mouse mast cell chymases.";
RL Biochim. Biophys. Acta 1121:83-87(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=129/Sv;
RX PubMed=11398967; DOI=10.1007/s002510100316;
RA Lunderius C., Hellman L.;
RT "Characterization of the gene encoding mouse mast cell protease 8 (mMCP-8),
RT and a comparative analysis of hematopoietic serine protease genes.";
RL Immunogenetics 53:225-232(2001).
RN [5]
RP PROTEIN SEQUENCE OF 22-51.
RX PubMed=2326280; DOI=10.1073/pnas.87.8.3230;
RA Reynolds D.S., Stevens R.L., Lane W.S., Carr M.H., Austen K.F.,
RA Serafin W.E.;
RT "Different mouse mast cell populations express various combinations of at
RT least six distinct mast cell serine proteases.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3230-3234(1990).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=1527387;
RA McNeil H.P., Frenkel D.P., Austen F., Friend D.S., Stevens R.L.;
RT "Translation and granule localization of mouse mast cell protease-5.
RT Immunodetection with specific antipeptide Ig.";
RL J. Immunol. 149:2466-2472(1992).
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.
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:0000269|PubMed:1527387}.
CC Cytoplasmic granule {ECO:0000269|PubMed:1527387}. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48705.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M73759; AAA40105.1; -; mRNA.
DR EMBL; M73760; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X68805; CAA48705.1; ALT_INIT; mRNA.
DR EMBL; M68898; AAA39492.1; -; mRNA.
DR EMBL; AF119364; AAD43901.1; -; Genomic_DNA.
DR CCDS; CCDS27135.2; -.
DR PIR; S23504; S23504.
DR PIR; S26043; S26043.
DR RefSeq; NP_034910.1; NM_010780.3.
DR AlphaFoldDB; P21844; -.
DR SMR; P21844; -.
DR STRING; 10090.ENSMUSP00000022834; -.
DR MEROPS; S01.150; -.
DR GlyGen; P21844; 1 site.
DR iPTMnet; P21844; -.
DR PhosphoSitePlus; P21844; -.
DR MaxQB; P21844; -.
DR PaxDb; P21844; -.
DR PRIDE; P21844; -.
DR ProteomicsDB; 285499; -.
DR Antibodypedia; 3125; 409 antibodies from 39 providers.
DR DNASU; 17228; -.
DR Ensembl; ENSMUST00000226280; ENSMUSP00000154406; ENSMUSG00000022225.
DR GeneID; 17228; -.
DR KEGG; mmu:17228; -.
DR CTD; 1215; -.
DR MGI; MGI:96941; Cma1.
DR VEuPathDB; HostDB:ENSMUSG00000022225; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR InParanoid; P21844; -.
DR OMA; PQACRHY; -.
DR OrthoDB; 1076876at2759; -.
DR BRENDA; 3.4.21.B5; 3474.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR BioGRID-ORCS; 17228; 0 hits in 72 CRISPR screens.
DR PRO; PR:P21844; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P21844; protein.
DR Bgee; ENSMUSG00000022225; Expressed in dermis and 122 other tissues.
DR ExpressionAtlas; P21844; baseline and differential.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
DR GO; GO:0034769; P:basement membrane disassembly; ISO:MGI.
DR GO; GO:0140447; P:cytokine precursor processing; ISO:MGI.
DR GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI.
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; Glycoprotein; Hydrolase;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..21
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2326280"
FT /id="PRO_0000027455"
FT CHAIN 22..247
FT /note="Chymase"
FT /id="PRO_0000027456"
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"
FT CONFLICT 5
FT /note="T -> A (in Ref. 1; AAA40105)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="C -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> R (in Ref. 3; AAA39492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27586 MW; 24C290CF61237DC7 CRC64;
MHLLTLHLLL LLLGSSTKAG EIIGGTECIP HSRPYMAYLE IVTSENYLSA CSGFLIRRNF
VLTAAHCAGR SITVLLGAHN KTSKEDTWQK LEVEKQFLHP KYDENLVVHD IMLLKLKEKA
KLTLGVGTLP LSANFNFIPP GRMCRAVGWG RTNVNEPASD TLQEVKMRLQ EPQACKHFTS
FRHNSQLCVG NPKKMQNVYK GDSGGPLLCA GIAQGIASYV HRNAKPPAVF TRISHYRPWI
NKILREN
