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Reviewed, UniProtKB/Swiss-Prot P21842 (CMA1_CANFA)

Last modified June 16, 2009. Version 65. 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
    Mast cell protease I
Gene names
Name: CMA1
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length249 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.

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.

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
Zymogen
   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

Signal peptide1 – 1919
Propeptide20 – 212Activation peptide Ref.3
PRO_0000027431
Chain22 – 249228Chymase
PRO_0000027432

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

Disulfide bond51 ↔ 67 By similarity
Disulfide bond144 ↔ 209 By similarity
Disulfide bond175 ↔ 188 By similarity

Experimental info

Sequence conflict291K → R AA sequence Ref.3
Sequence conflict381H → Q AA sequence Ref.3
Sequence conflict451R → T AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P21842-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 3BBD0A6C2855F540

FASTA24927,812
        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 

« Hide

References

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

Cross-references

Sequence databases

J02904 mRNA. Translation: AAA30835.1.
U89607 Genomic DNA. Translation: AAB94641.1.
PIRA35842.
RefSeqNP_001013442.1.
XP_855610.1.
UniGeneCfa.16336

3D structure databases

HSSPHSSP built from PDB template 1NN6 based on UniProtKB P23946.
SMRP21842. Positions 22-247.
ModBaseSearch...

Protein family/group databases

MEROPSS01.140.

Genome annotation databases

EnsemblENSCAFG00000012443. Canis familiaris. [Contig view]
GeneID490628.
KEGGcfa:490628.

Phylogenomic databases

HOVERGENP21842.

Enzyme and pathway databases

BRENDA3.4.21.39. 463.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCMA1_CANFA
AccessionPrimary (citable) accession number: P21842
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 65 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