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A7WPL7 (CMA1_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 30. 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
Gene names
Name:CMA1
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 214Activation peptide
PRO_0000312843
Chain22 – 247226Chymase Ref.2
PRO_5000271615

Regions

Domain22 – 245224Peptidase S1

Sites

Active site661Charge relay system By similarity UniProtKB P23946
Active site1101Charge relay system By similarity UniProtKB P23946
Active site2031Charge relay system By similarity UniProtKB P23946

Amino acid modifications

Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 67 By similarity UniProtKB P23946
Disulfide bond144 ↔ 209 By similarity UniProtKB P23946
Disulfide bond175 ↔ 188 By similarity UniProtKB P23946

Experimental info

Sequence conflict521G → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
A7WPL7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 988E69EBAD6AF589

FASTA24727,666
        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 

« Hide

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

EMBL
GenBank
DDBJ
AM851020 mRNA. Translation: CAO99144.1.
RefSeqNP_001166403.1. NM_001172932.1.

3D structure databases

ProteinModelPortalA7WPL7.
SMRA7WPL7. Positions 22-247.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7WPL7.

Protein family/group databases

MEROPSS01.140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000012522; ENSCPOP00000011161; ENSCPOG00000012404.
GeneID100135503.

Organism-specific databases

CTD1215.

Phylogenomic databases

eggNOGroNOG06568.
GeneTreeENSGT00580000081281.
HOVERGENHBG013304.
InParanoidA7WPL7.
OrthoDBEOG4R23VK.

Enzyme and pathway databases

BRENDA3.4.21.39. 1225.

Family and domain databases

InterProIPR009003. Pept_cys/ser_Trypsin-like.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCMA1_CAVPO
AccessionPrimary (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: November 16, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families