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Reviewed, UniProtKB/Swiss-Prot P85202 (CMA1_RABIT)

Last modified November 3, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chymase
    EC=3.4.21.39
Alternative name(s):
    Alpha-chymase
Gene names
Name: CMA1
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Chymase
PRO_0000312844

Regions

Domain2 – 218217Peptidase S1

Sites

Active site461Charge relay system By similarity UniProtKB P23946
Active site901Charge relay system By similarity UniProtKB P23946
Active site1771Charge relay system By similarity UniProtKB P23946

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 47 By similarity UniProtKB P23946
Disulfide bond124 ↔ 182 By similarity UniProtKB P23946
Disulfide bond155 ↔ 168 By similarity UniProtKB P23946

Sequences

Sequence LengthMass (Da)Tools
P85202-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: D6E7B8C87D57156E

FASTA22024,710
        10         20         30         40         50         60 
EIIGGTESKP HSRPYMAHLK IITKQGTFAY CGGFLISREF VMTAAHCKGR HITVTLGAHD 

        70         80         90        100        110        120 
VVKKESTWQK IDVVKQFVHP NYNSYTIRHD VMLLKLKEKA NLTLTVGTLP LLPQSNFIPP 

       130        140        150        160        170        180 
GRMCRAVGWG KTSVKESHSN VLQEVKLRLL DPPACQHFPD FNHNLQLCMG TVFKGDSGPL 

       190        200        210        220 
LCARVAQGIA SYAHKNAMPP SVFTRISYYR PWINKVLKEN 

« Hide

References

[1]"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.

Cross-references

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP85202.

Phylogenomic databases

OMARKTKSAF.

Enzyme and pathway databases

BRENDA3.4.21.39. 255.

Family and domain databases

InterProIPR018114. 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]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCMA1_RABIT
AccessionPrimary (citable) accession number: P85202
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents