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Reviewed, UniProtKB/Swiss-Prot P52195 (CMA1_PAPHA)

Last modified November 24, 2009. Version 54. 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 chymase
Gene names
Name: CMA1
Synonyms: CHM
OrganismPapio hamadryas (Hamadryas baboon)
Taxonomic identifier9557 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

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.

Catalytic activity

Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa.

Subcellular location

Secreted. Cytoplasmic granule. Note: Mast cell granules.

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
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 By similarity
Propeptide20 – 212Activation peptide
PRO_0000027437
Chain22 – 247226Chymase
PRO_0000027438

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

Sequences

Sequence LengthMass (Da)Tools
P52195-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E0EC15E0FA72FD8B

FASTA24727,339
        10         20         30         40         50         60 
MLLLPLPLLL LFLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKS CGGFLIRRNF 

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

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

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


NKILQAN 

« Hide

References

[1]Liao Y., Karnik S., Husain A.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38521 mRNA. Translation: AAA91160.1.
U38463 Genomic DNA. Translation: AAA91159.1.

3D structure databases

SMRP52195. Positions 22-247.
ModBaseSearch...

Protein family/group databases

MEROPSS01.140.

Phylogenomic databases

HOVERGENP52195.

Enzyme and pathway databases

BRENDA3.4.21.39. 39388.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[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_PAPHA
AccessionPrimary (citable) accession number: P52195
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 24, 2009
This is version 54 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