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Protein

Chymase

Gene

Cma1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661Charge relay systemBy similarity
Active sitei110 – 1101Charge relay systemBy similarity
Active sitei203 – 2031Charge relay systemBy similarity

GO - Molecular functioni

  1. peptide binding Source: Ensembl
  2. serine-type endopeptidase activity Source: MGI

GO - Biological processi

  1. cellular response to glucose stimulus Source: Ensembl
  2. interleukin-1 beta biosynthetic process Source: MGI
  3. midbrain development Source: Ensembl
  4. peptide metabolic process Source: Ensembl
  5. positive regulation of angiogenesis Source: Ensembl
  6. protein processing Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.B5. 3474.
ReactomeiREACT_281604. Metabolism of Angiotensinogen to Angiotensins.
REACT_327841. Signaling by SCF-KIT.
REACT_332323. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiS01.150.

Names & Taxonomyi

Protein namesi
Recommended name:
Chymase (EC:3.4.21.39)
Alternative name(s):
Alpha-chymase
Mast cell chymase 1
Mast cell protease 5
Short name:
mMCP-5
Mast cell protease I
Gene namesi
Name:Cma1
Synonyms:Mcpt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:96941. Cma1.

Subcellular locationi

Secreted 1 Publication. Cytoplasmic granule 1 Publication
Note: Secretory granules.

GO - Cellular componenti

  1. extracellular matrix Source: Ensembl
  2. extracellular space Source: GO_Central
  3. intracellular Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 212Activation peptide1 PublicationPRO_0000027455
Chaini22 – 247226ChymasePRO_0000027456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 67PROSITE-ProRule annotation
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi144 ↔ 209PROSITE-ProRule annotation
Disulfide bondi175 ↔ 188PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP21844.
PRIDEiP21844.

PTM databases

PhosphoSiteiP21844.

Expressioni

Tissue specificityi

Mast cells.

Gene expression databases

BgeeiP21844.
CleanExiMM_CMA1.
ExpressionAtlasiP21844. baseline and differential.
GenevestigatoriP21844.

Structurei

3D structure databases

ProteinModelPortaliP21844.
SMRiP21844. Positions 22-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 245224Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG293191.
HOVERGENiHBG013304.
InParanoidiP21844.
KOiK01329.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLTLHLLL LLLGSSTKAG EIIGGTECIP HSRPYMAYLE IVTSENYLSA
60 70 80 90 100
CSGFLIRRNF VLTAAHCAGR SITVLLGAHN KTSKEDTWQK LEVEKQFLHP
110 120 130 140 150
KYDENLVVHD IMLLKLKEKA KLTLGVGTLP LSANFNFIPP GRMCRAVGWG
160 170 180 190 200
RTNVNEPASD TLQEVKMRLQ EPQACKHFTS FRHNSQLCVG NPKKMQNVYK
210 220 230 240
GDSGGPLLCA GIAQGIASYV HRNAKPPAVF TRISHYRPWI NKILREN
Length:247
Mass (Da):27,586
Last modified:November 30, 1992 - v2
Checksum:i24C290CF61237DC7
GO

Sequence cautioni

The sequence CAA48705.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51T → A in AAA40105 (PubMed:1939089).Curated
Sequence conflicti51 – 511C → R AA sequence (PubMed:2326280).Curated
Sequence conflicti224 – 2241A → R in AAA39492 (PubMed:1376147).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73759 mRNA. Translation: AAA40105.1.
M73760 mRNA. No translation available.
X68805 mRNA. Translation: CAA48705.1. Different initiation.
M68898 mRNA. Translation: AAA39492.1.
AF119364 Genomic DNA. Translation: AAD43901.1.
PIRiS23504.
S26043.
RefSeqiNP_034910.1. NM_010780.2.
UniGeneiMm.1252.

Genome annotation databases

GeneIDi17228.
KEGGimmu:17228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73759 mRNA. Translation: AAA40105.1.
M73760 mRNA. No translation available.
X68805 mRNA. Translation: CAA48705.1. Different initiation.
M68898 mRNA. Translation: AAA39492.1.
AF119364 Genomic DNA. Translation: AAD43901.1.
PIRiS23504.
S26043.
RefSeqiNP_034910.1. NM_010780.2.
UniGeneiMm.1252.

3D structure databases

ProteinModelPortaliP21844.
SMRiP21844. Positions 22-247.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.150.

PTM databases

PhosphoSiteiP21844.

Proteomic databases

PaxDbiP21844.
PRIDEiP21844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi17228.
KEGGimmu:17228.

Organism-specific databases

CTDi1215.
MGIiMGI:96941. Cma1.

Phylogenomic databases

eggNOGiNOG293191.
HOVERGENiHBG013304.
InParanoidiP21844.
KOiK01329.

Enzyme and pathway databases

BRENDAi3.4.21.B5. 3474.
ReactomeiREACT_281604. Metabolism of Angiotensinogen to Angiotensins.
REACT_327841. Signaling by SCF-KIT.
REACT_332323. Activation of Matrix Metalloproteinases.

Miscellaneous databases

NextBioi291648.
PROiP21844.
SOURCEiSearch...

Gene expression databases

BgeeiP21844.
CleanExiMM_CMA1.
ExpressionAtlasiP21844. baseline and differential.
GenevestigatoriP21844.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of the mouse mast cell protease-5 gene. A novel secretory granule protease expressed early in the differentiation of serosal mast cells."
    McNeil H.P., Austen K.F., Somerville L.L., Gurish M.F., Stevens R.L.
    J. Biol. Chem. 266:20316-20322(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three mouse mast cell-specific serine proteases."
    Huang R., Blom T., Hellman L.
    Eur. J. Immunol. 21:1611-1621(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Leaden X A1.
    Tissue: Mastocytoma.
  3. "Molecular cloning and characterization of mouse mast cell chymases."
    Chu W., Johnson D.A., Musich P.R.
    Biochim. Biophys. Acta 1121:83-87(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Characterization of the gene encoding mouse mast cell protease 8 (mMCP-8), and a comparative analysis of hematopoietic serine protease genes."
    Lunderius C., Hellman L.
    Immunogenetics 53:225-232(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
    Strain: 129/Sv.
  5. "Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases."
    Reynolds D.S., Stevens R.L., Lane W.S., Carr M.H., Austen K.F., Serafin W.E.
    Proc. Natl. Acad. Sci. U.S.A. 87:3230-3234(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-51.
  6. "Translation and granule localization of mouse mast cell protease-5. Immunodetection with specific antipeptide Ig."
    McNeil H.P., Frenkel D.P., Austen F., Friend D.S., Stevens R.L.
    J. Immunol. 149:2466-2472(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCMA1_MOUSE
AccessioniPrimary (citable) accession number: P21844
Secondary accession number(s): Q9R1F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 1991
Last sequence update: November 30, 1992
Last modified: March 31, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.