Reviewed, UniProtKB/Swiss-Prot A7WPL7 (CMA1_CAVPO)

Names and origin

Protein names

Recommended name:
    Chymase
    EC=3.4.21.39
Alternative name(s):
    Alpha-chymase

Gene names

Name:

CMA1

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

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 protein 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. UniProtKB P23946
Catalytic activity	Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa. UniProtKB P23946
Subcellular location	Secreted By similarity. Cytoplasmic granule By similarity. Note: Mast cell granules By similarity. UniProtKB P23946
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 21	4	Activation peptide Ref.2		PRO_0000312843
	Chain	22 – 247	226	Chymase Ref.2		PRO_5000271615
Regions
	Domain	22 – 245	224	Peptidase S1
Sites
	Active site	66	1	Charge relay system By similarity UniProtKB P23946
	Active site	110	1	Charge relay system By similarity UniProtKB P23946
	Active site	203	1	Charge relay system By similarity UniProtKB P23946
Amino acid modifications
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 67		By similarity UniProtKB P23946
	Disulfide bond	144 ↔ 209		By similarity UniProtKB P23946
	Disulfide bond	175 ↔ 188		By similarity UniProtKB P23946
Experimental info
	Sequence conflict	52	1	G → S AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	A7WPL7-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 988E69EBAD6AF589	FASTA	247	27,666
	10 20 30 40 50 60 MCLLSLPLLL FLQYTRAKAG EVIGGTECKP HSRPYMAYLE IVSSEGYEKD CGGFLIRRNF 70 80 90 100 110 120 VLTAAHCAGR SLTVNLGVHN KKMKEDTWQR LKVIKQFLHP NYNSSVLLHD IMLLKLEKKA 130 140 150 160 170 180 NLTLAVGTLP LPPECNFLTS GRMCRAAGWG RTNVEEPASD TLQEVKLRLM DPQACKHFPN 190 200 210 220 230 240 FNHNLQLCVG NPRKRKSVFK GDSGGPLLCA GIAQGIVSYA HRNAKPPVVF TRISHYRPWI NKILKAN

References

[1]	"Guinea pig chymase is leucine-specific: a novel example of functional plasticity in the chymase/granzyme family of immune cell serine peptidases." Beauchamp J.C., Caughey G.H., Fingerle J., Schliemann K. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Structural basis for elastolytic substrate specificity in rodent alpha-chymases." Kervinen J., Abad M., Crysler C., Kolpak M., Mahan A.D., Masucci J.A., Bayoumy S., Cummings M.D., Yao X., Olson M., de Garavilla L., Kuo L., Deckman I., Spurlino J. J. Biol. Chem. 283:427-436(2008) [PubMed: 17981788] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-247.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM851020 mRNA. Translation: CAO99144.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S01.140.
Genome annotation databases
Ensembl	ENSCPOG00000012404. Cavia porcellus. [Contig view]
Enzyme and pathway databases
BRENDA	3.4.21.39. 44.
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...

Entry information

Entry name

CMA1_CAVPO

Accession

Primary (citable) accession number: A7WPL7
Secondary accession number(s): P85201

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)