[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2071582 [NCBI, ExPASy, EBI, Israel, Japan] Caughey G.H., Zerweck E.H., Vanderslice P.; "Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase."; J. Biol. Chem. 266:12956-12963(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Heart; PubMed=1894611 [NCBI, ExPASy, EBI, Israel, Japan] Urata H., Kinoshita A., Perez D.M., Misono K.S., Bumpus F.M., Graham R.M., Husain A.; "Cloning of the gene and cDNA for human heart chymase."; J. Biol. Chem. 266:17173-17179(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 22-247. DOI=10.1016/0014-5793(93)81461-8; PubMed=8495723 [NCBI, ExPASy, EBI, Israel, Japan] Sukenaga Y., Kido H., Neki A., Enomoto M., Ishida K., Takagi K., Katunuma N.; "Purification and molecular cloning of chymase from human tonsils."; FEBS Lett. 323:119-122(1993).
[5]	NUCLEOTIDE SEQUENCE OF 26-60. TISSUE=Placenta; PubMed=2049082 [NCBI, ExPASy, EBI, Israel, Japan] Jenne D.E., Tschopp J.; "Angiotensin II-forming heart chymase is a mast-cell-specific enzyme."; Biochem. J. 276:567-568(1991).
[6]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1021/bi971403n; PubMed=9400368 [NCBI, ExPASy, EBI, Israel, Japan] McGrath M.E., Mirzadegan T., Schmidt B.F.; "Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A."; Biochemistry 36:14318-14324(1997).
[7]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). DOI=10.1006/jmbi.1998.2462; PubMed=9931257 [NCBI, ExPASy, EBI, Israel, Japan] Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M., Strobl S.; "The 2.2-A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity."; J. Mol. Biol. 286:163-173(1999).
[8]	ERRATUM. DOI=10.1006/jmbi.1999.2691; PubMed=10208809 [NCBI, ExPASy, EBI, Israel, Japan] Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M., Strobl S.; J. Mol. Biol. 286:817-817(1999).

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. Cytoplasmic granule. Note=Mast cell granules.
TISSUE SPECIFICITY: Mast cells in lung, heart, skin and placenta.
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

M64269; AAA52020.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M69137; AAA52021.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M69136; AAA52019.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069110; AAH69110.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069370; AAH69370.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069490; AAH69490.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X59072; CAA41796.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S61334; AAB26828.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A40967; KYHUCM.

NP_001827.1; -.

3D structure databases

PDB

1KLT; X-ray; 1.90 A; A=22-247.	[ExPASy / RCSB / EBI]
1NN6; X-ray; 1.75 A; A=20-247.	[ExPASy / RCSB / EBI]
1PJP; X-ray; 2.20 A; A=22-247.	[ExPASy / RCSB / EBI]
1T31; X-ray; 1.90 A; A=22-247.	[ExPASy / RCSB / EBI]
2HVX; X-ray; 2.60 A; A=22-247.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KLT; -.
1NN6; -.
1PJP; -.
1T31; -.
2HVX; -.

ModBase

P23946.

Protein family/group databases

MEROPS

S01.140; -.

PTM databases

PhosphoSite

P23946; -.

Organism-specific databases

HIX0037752; -.

HGNC:2097; CMA1.

CAB000363; -.

118938; gene. [NCBI / EBI]

PharmGKB

PA26623; -.

GeneCards

P23946.

Gene expression databases

ArrayExpress

P23946; -.

CleanEx

HS_CMA1; -.

GermOnline

ENSG00000092009; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
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).

Genome annotation databases

Ensembl

ENSG00000092009; Homo sapiens. [Contig view]

GeneID

1215; -.

KEGG

hsa:1215; -.

Phylogenomic databases

HOVERGEN

P23946; -.

Other

P23946; -.

P23946; -.

5003; -.

CMA1; Homo sapiens.

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

Keywords

3D-structure; Glycoprotein; Hydrolase; Polymorphism; 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_0000027433`
`CHAIN`	`22 247`	`226`	`Chymase.`	`PRO_0000027434`
`DOMAIN`	`22 245`	`224`	`Peptidase S1.`
`ACT_SITE`	`66 66`		`Charge relay system.`
`ACT_SITE`	`110 110`		`Charge relay system.`
`ACT_SITE`	`203 203`		`Charge relay system.`
`CARBOHYD`	`80 80`		`N-linked (GlcNAc...).`
`CARBOHYD`	`103 103`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`51 67`
`DISULFID`	`144 209`
`DISULFID`	`175 188`
`VARIANT`	`46 46`	`1`	`G -> R (in dbSNP:rs5246 [NCBI]).`	`VAR_011770 [3D]`
`VARIANT`	`66 66`	`1`	`H -> R (in dbSNP:rs5247 [NCBI]).`	`VAR_011771 [3D]`
`VARIANT`	`98 98`	`1`	`R -> H (in dbSNP:rs13306252 [NCBI]).`	`VAR_029190 [3D]`
`CONFLICT`	`28 28`		`C -> S (in Ref. 4; AAB26828).`
`STRAND`	`36 42`	`7`
`STRAND`	`44 46`	`3`
`STRAND`	`48 57`	`10`
`STRAND`	`60 63`	`4`
`HELIX`	`65 67`	`3`
`STRAND`	`70 77`	`8`
`STRAND`	`89 98`	`10`
`TURN`	`104 106`	`3`
`STRAND`	`112 118`	`7`
`STRAND`	`143 156`	`14`
`STRAND`	`163 170`	`8`
`HELIX`	`172 175`	`4`
`TURN`	`183 185`	`3`
`STRAND`	`186 190`	`5`
`STRAND`	`206 209`	`4`
`STRAND`	`212 219`	`8`
`STRAND`	`228 232`	`5`
`HELIX`	`233 236`	`4`
`HELIX`	`237 246`	`10`

Sequence information

Length: 247 AA [This is the length of the unprocessed precursor]

Molecular weight: 27325 Da [This is the MW of the unprocessed precursor]

CRC64: DC1464A049ED6B00 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF CGGFLIRRNF 

        70         80         90        100        110        120 
VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA 

       130        140        150        160        170        180 
SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRD 

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


NQILQAN

P23946 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