Reviewed, UniProtKB/Swiss-Prot P50339 (CMA1_RAT)

Names and origin

Protein names

Recommended name:
    Chymase
    EC=3.4.21.39
Alternative name(s):
    Alpha-chymase
    Mast cell protease 3
    Mast cell protease III
      Short name=rMCP-3
      Short name=rMCP-III
    Mast cell protease 5
      Short name=rMCP-5

Gene names

Name:	Cma1
Synonyms:	Mcpt3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion By similarity.
Catalytic activity	Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.
Subcellular location	Secreted. Cytoplasmic granule. Note: Secretory granules.
Tissue specificity	Mast cells.
Sequence similarities	Belongs to the peptidase S1 family. Granzyme subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from mutant phenotype. Source: RGD
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide binding Inferred from mutant phenotype. Source: RGD serine-type endopeptidase activity Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 21	2	Activation peptide		PRO_0000027443
	Chain	22 – 247	226	Chymase		PRO_0000027444
Regions
	Domain	22 – 245	224	Peptidase S1
Sites
	Active site	66	1	Charge relay system By similarity
	Active site	110	1	Charge relay system By similarity
	Active site	203	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 67		By similarity
	Disulfide bond	144 ↔ 209		By similarity
	Disulfide bond	175 ↔ 188		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P50339-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6525D7BF1BFDF053	FASTA	247	27,569
	10 20 30 40 50 60 MNLHALCLLL LLLGSSTKAG EIIGGTECIP HSRPYMAYLE IVTSDNYLSA CSGFLIRRNF 70 80 90 100 110 120 VLTAAHCAGR SITVLLGAHN KTYKEDTWQK LEVEKQFIHP NYDKRLVLHD IMLLKLKEKA 130 140 150 160 170 180 KLTLGVGTLP LSANFNFIPP GRMCRAVGWG RTNVNEPASD TLQEVKMRLQ EPQSCKHFTS 190 200 210 220 230 240 FQHKSQLCVG NPKKMQNVYK GDSGGPLLCA GIAQGIASYV HPNAKPPAVF TRISHYRPWI NKILREN

References

[1]	"Cloning of the cDNA encoding a novel rat mast-cell proteinase, rMCP-3, and its expression in comparison with other rat mast-cell proteinases." Ide H., Itoh H., Tomita M., Murakumo Y., Kobayashi T., Maruyama H., Osada Y., Nawa Y. Biochem. J. 311:675-680(1995) [PubMed: 7487912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Peritoneal mast cell.
[2]	"Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations." Lutzelschwab C., Pejler G., Aveskogh M., Hellman L. J. Exp. Med. 185:13-29(1997) [PubMed: 8996238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-247. Strain: Sprague-Dawley.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38495 mRNA. Translation: BAA07507.1. U67908 mRNA. Translation: AAB48261.1.
IPI	IPI00197397.
PIR	S59135.
RefSeq	NP_037224.1.
UniGene	Rn.10182
3D structure databases
HSSP	HSSP built from PDB template 1NN6 based on UniProtKB P23946.
SMR	P50339. Positions 22-247.
ModBase	Search...
Protein family/group databases
MEROPS	S01.150.
Proteomic databases
PRIDE	P50339.
Genome annotation databases
GeneID	25627.
KEGG	rno:25627.
Organism-specific databases
RGD	2365. Cma1.
Phylogenomic databases
HOVERGEN	P50339.
Enzyme and pathway databases
BRENDA	3.4.21.39. 248.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	607417.

Entry information

Entry name

CMA1_RAT

Accession

Primary (citable) accession number: P50339
Secondary accession number(s): Q9R2C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)