[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00473a024; PubMed=2378872 [NCBI, ExPASy, EBI, Israel, Japan] Caughey G.H., Raymond W.W., Vanderslice P.; "Dog mast cell chymase: molecular cloning and characterization."; Biochemistry 29:5166-5171(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Beagle; PubMed=9379034 [NCBI, ExPASy, EBI, Israel, Japan] Caughey G.H., Blount J.L., Koerber K.L., Kitamura M., Fang K.C.; "Cloning and expression of the dog mast cell alpha-chymase gene."; J. Immunol. 159:4367-4375(1997).
[3]	PROTEIN SEQUENCE OF 22-46. PubMed=3122835 [NCBI, ExPASy, EBI, Israel, Japan] Caughey G.H., Viro N.F., Lazarus S.C., Nadel J.A.; "Purification and characterization of dog mastocytoma chymase: identification of an octapeptide conserved in chymotryptic leukocyte proteinases."; Biochim. Biophys. Acta 952:142-149(1988).

Comments

FUNCTION: Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.
CATALYTIC ACTIVITY: Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.
SUBCELLULAR LOCATION: Secreted (By similarity). Cytoplasmic granule (By similarity). Note=Mast cell granules (By similarity).
SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J02904; AAA30835.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U89607; AAB94641.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A35842; A35842.

RefSeq

NP_001013442.1; -.
XP_855610.1; -.

UniGene

Cfa.16336

3D structure databases

HSSP

P23946; 1NN6. [HSSP ENTRY / PDB]

SMR

P21842; 22-247.

ModBase

P21842.

Protein family/group databases

MEROPS

S01.140; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P21842.

Genome annotation databases

Ensembl

ENSCAFG00000012443; Canis familiaris. [Contig view]

GeneID

490628; -.

KEGG

cfa:490628; -.

Phylogenomic databases

HOVERGEN

P21842; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Protease; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`PROPEP`	`20 21`	`2`	`Activation peptide.`	`PRO_0000027431`
`CHAIN`	`22 249`	`228`	`Chymase.`	`PRO_0000027432`
`DOMAIN`	`22 245`	`224`	`Peptidase S1.`
`ACT_SITE`	`66 66`		`Charge relay system (By similarity).`
`ACT_SITE`	`110 110`		`Charge relay system (By similarity).`
`ACT_SITE`	`203 203`		`Charge relay system (By similarity).`
`DISULFID`	`51 67`		`By similarity.`
`DISULFID`	`144 209`		`By similarity.`
`DISULFID`	`175 188`		`By similarity.`
`CONFLICT`	`29 29`		`K -> R (in Ref. 3; AA sequence).`
`CONFLICT`	`38 38`		`H -> Q (in Ref. 3; AA sequence).`
`CONFLICT`	`45 45`		`R -> T (in Ref. 3; AA sequence).`

Sequence information

Length: 249 AA [This is the length of the unprocessed precursor]

Molecular weight: 27812 Da [This is the MW of the unprocessed precursor]

CRC64: 3BBD0A6C2855F540 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHCLPLTLLL LLLCSRAEAE EIIGGTESKP HSRPYMAHLE ILTLRNHLAS CGGFLIRRNF 

        70         80         90        100        110        120 
VLTAAHCAGR FIMVTLGAHN IQKKEDTWQK LEVIKQFPHP KYDDLTLRHD IMLLKLKEKA 

       130        140        150        160        170        180 
NLTLAVGTLP LSPQFNFVPP GRMCRVAGWG KRQVNGSGSD TLQEVKLRLM DPQACRHYMA 

       190        200        210        220        230        240 
FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG QNDAKPPAVF TRISHYRPWI 


NKVLKQNKA

P21842 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools