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P50339 (CMA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymase

EC=3.4.21.39
Alternative name(s):
Alpha-chymase
Mast cell protease 3
Short name=rMCP-3
Mast cell protease 5
Short name=rMCP-5
Mast cell protease III
Short name=rMCP-III
Gene names
Name:Cma1
Synonyms:Mcpt3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 212Activation peptide
PRO_0000027443
Chain22 – 247226Chymase
PRO_0000027444

Regions

Domain22 – 245224Peptidase S1

Sites

Active site661Charge relay system By similarity
Active site1101Charge relay system By similarity
Active site2031Charge relay system By similarity

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 67 By similarity
Disulfide bond144 ↔ 209 By similarity
Disulfide bond175 ↔ 188 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50339 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6525D7BF1BFDF053

FASTA24727,569
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-247.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38495 mRNA. Translation: BAA07507.1.
U67908 mRNA. Translation: AAB48261.1.
PIRS59135.
RefSeqNP_037224.1. NM_013092.1.
UniGeneRn.10182.

3D structure databases

ProteinModelPortalP50339.
SMRP50339. Positions 22-247.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP50339.
ChEMBLCHEMBL3168.

Protein family/group databases

MEROPSS01.150.

Proteomic databases

PRIDEP50339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000067539; ENSRNOP00000061330; ENSRNOG00000020563.
GeneID25627.
KEGGrno:25627.
UCSCRGD:2365. rat.

Organism-specific databases

CTD1215.
RGD2365. Cma1.

Phylogenomic databases

GeneTreeENSGT00740000115279.
HOVERGENHBG013304.
KOK01329.
OMATLHHDIM.
OrthoDBEOG7RRF7Z.
PhylomeDBP50339.

Gene expression databases

GenevestigatorP50339.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607417.

Entry information

Entry nameCMA1_RAT
AccessionPrimary (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: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries