CMA1_CANLF
ID CMA1_CANLF Reviewed; 249 AA.
AC P21842;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chymase;
DE EC=3.4.21.39;
DE AltName: Full=Alpha-chymase;
DE AltName: Full=Mast cell protease I;
DE Flags: Precursor;
GN Name=CMA1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2378872; DOI=10.1021/bi00473a024;
RA Caughey G.H., Raymond W.W., Vanderslice P.;
RT "Dog mast cell chymase: molecular cloning and characterization.";
RL Biochemistry 29:5166-5171(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Beagle;
RX PubMed=9379034;
RA Caughey G.H., Blount J.L., Koerber K.L., Kitamura M., Fang K.C.;
RT "Cloning and expression of the dog mast cell alpha-chymase gene.";
RL J. Immunol. 159:4367-4375(1997).
RN [3]
RP PROTEIN SEQUENCE OF 22-46.
RX PubMed=3122835; DOI=10.1016/0167-4838(88)90109-4;
RA Caughey G.H., Viro N.F., Lazarus S.C., Nadel J.A.;
RT "Purification and characterization of dog mastocytoma chymase:
RT identification of an octapeptide conserved in chymotryptic leukocyte
RT proteinases.";
RL Biochim. Biophys. Acta 952:142-149(1988).
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: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; J02904; AAA30835.1; -; mRNA.
DR EMBL; U89607; AAB94641.1; -; Genomic_DNA.
DR PIR; A35842; A35842.
DR RefSeq; NP_001013442.1; NM_001013424.1.
DR AlphaFoldDB; P21842; -.
DR SMR; P21842; -.
DR STRING; 9612.ENSCAFP00000018316; -.
DR MEROPS; S01.140; -.
DR PaxDb; P21842; -.
DR Ensembl; ENSCAFT00030022936; ENSCAFP00030020008; ENSCAFG00030012378.
DR Ensembl; ENSCAFT00040015211; ENSCAFP00040013176; ENSCAFG00040008127.
DR Ensembl; ENSCAFT00845014479; ENSCAFP00845011218; ENSCAFG00845008224.
DR GeneID; 490628; -.
DR KEGG; cfa:490628; -.
DR CTD; 1215; -.
DR VEuPathDB; HostDB:ENSCAFG00845008224; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P21842; -.
DR OMA; PQACRHY; -.
DR OrthoDB; 1076876at2759; -.
DR TreeFam; TF333630; -.
DR Reactome; R-CFA-1433557; Signaling by SCF-KIT.
DR Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CFA-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Proteomes; UP000002254; Chromosome 8.
DR Bgee; ENSCAFG00000012443; Expressed in blood and 41 other tissues.
DR GO; GO:0005615; C:extracellular space; 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; -; 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..19
FT PROPEP 20..21
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3122835"
FT /id="PRO_0000027431"
FT CHAIN 22..249
FT /note="Chymase"
FT /id="PRO_0000027432"
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 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 29
FT /note="K -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="H -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="R -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27812 MW; 3BBD0A6C2855F540 CRC64;
MHCLPLTLLL LLLCSRAEAE EIIGGTESKP HSRPYMAHLE ILTLRNHLAS CGGFLIRRNF
VLTAAHCAGR FIMVTLGAHN IQKKEDTWQK LEVIKQFPHP KYDDLTLRHD IMLLKLKEKA
NLTLAVGTLP LSPQFNFVPP GRMCRVAGWG KRQVNGSGSD TLQEVKLRLM DPQACRHYMA
FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG QNDAKPPAVF TRISHYRPWI
NKVLKQNKA
