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P21812 (MCPT4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Mast cell protease 4

Short name=mMCP-4
EC=3.4.21.-
Alternative name(s):
MSMCP
Myonase
Serosal mast cell protease
Gene names
Name:Mcpt4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing. Ref.4 Ref.7

Enzyme regulation

Completely inhibited by serine protease inhibitors such as chymostatin, diisopropylfluorophosphate and phenylmethylsulfonyl fluoride, but not by p-tosyl-L-phenylalanine chloromethyl ketone, p-tosyl-L-lysine chloromethyl ketone, pepstatin, E-64, EDTA or o-phenanthroline. Also inhibited by lima bean trypsin inhibitor, soy bean trypsin inhibitor and human plasma alpha1-antichymotrypsin.

Subunit structure

Monomer. Ref.4

Tissue specificity

Submucosal mast cells. In femoral muscle, detected in myocytes but not in mast cells. Ref.4

Disruption phenotype

Mice display an impaired ability to inactivate thrombin or degrade fibronectin in peritoneal cells. Ref.7

Sequence similarities

Belongs to the peptidase S1 family. Granzyme subfamily.

Contains 1 peptidase S1 domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 9 at high salt concentrations.

Mass spectrometry

Molecular mass is 25187 Da from positions 21 - 246. Determined by MALDI. Ref.4

Sequence caution

The sequence BAB18732.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 202Activation peptide
PRO_0000027453
Chain21 – 246226Mast cell protease 4
PRO_0000027454

Regions

Domain21 – 244224Peptidase S1

Sites

Active site651Charge relay system By similarity
Active site1091Charge relay system By similarity
Active site2021Charge relay system By similarity

Amino acid modifications

Disulfide bond50 ↔ 66 By similarity
Disulfide bond143 ↔ 208 By similarity
Disulfide bond174 ↔ 187 By similarity

Natural variations

Natural variant611M → L in strain: C57BL/6 and Leaden X A1.
Natural variant1601T → I in strain: C57BL/6 and Leaden X A1.
Natural variant2461E → KK in strain: C57BL/6 and Leaden X A1.

Sequences

Sequence LengthMass (Da)Tools
P21812 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 0887A1C71ACE2698

FASTA24627,204
        10         20         30         40         50         60 
MQALLFLMAL LLPSGAGAEE IIGGVESRPH SRPYMAHLEI TTERGFTATC GGFLITRQFV 

        70         80         90        100        110        120 
MTAAHCSGRE ITVTLGAHDV SKTESTQQKI KVEKQIVHPK YNFYSNLHDI MLLKLQKKAK 

       130        140        150        160        170        180 
ETPSVNVIPL PRPSDFIKPG KMCRAAGWGR TGVTEPTSDT LREVKLRIMD KEACKNYWHY 

       190        200        210        220        230        240 
DYNLQVCVGS PRKKRSAYKG DSGGPLLCAG VAHGIVSYGR GDAKPPAVFT RISSYVPWIN 


RVIKGE 

« Hide

References

[1]"Cloning of the cDNA and gene for mouse mast cell protease 4. Demonstration of its late transcription in mast cell subclasses and analysis of its homology to subclass-specific neutral proteases of the mouse and rat."
Serafin W.E., Sullivan T.P., Conder G.A., Ebrahimi A., Marcham P., Johnson S.S., Austen K.F., Reynolds D.S.
J. Biol. Chem. 266:1934-1941(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: BALB/c.
[2]"Independent influence of strain difference and mi transcription factor on the expression of mouse mast cell chymases."
Ge Y., Jippo T., Lee Y.-M., Adachi S., Kitamura Y.
Am. J. Pathol. 158:281-292(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[3]"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(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 7-246.
Strain: Leaden X A1.
Tissue: Mastocytoma.
[4]"Purification and characterization of myonase from X-chromosome linked muscular dystrophic mouse skeletal muscle."
Hori S., Ohtani S., Hori C., Nokihara K.
J. Biochem. 123:650-658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 7-246, PROTEIN SEQUENCE OF 21-66; 76-84; 86-93; 96-106; 126-143; 146-155; 178-180; 197-207 AND 231-238, FUNCTION, SUBUNIT, TISSUE SPECIFICITY, MASS SPECTROMETRY.
Tissue: Skeletal muscle.
[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(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-43.
[6]"Biochemical and immunological characterization of multiple glycoforms of mouse mast cell protease 1: comparison with an isolated murine serosal mast cell protease (MMCP-4)."
Newlands G.F.J., Knox D.P., Pirie-Shepherd S.R., Miller H.R.P.
Biochem. J. 294:127-135(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-40.
[7]"The chymase, mouse mast cell protease 4, constitutes the major chymotrypsin-like activity in peritoneum and ear tissue. A role for mouse mast cell protease 4 in thrombin regulation and fibronectin turnover."
Tchougounova E., Pejler G., Abrink M.
J. Exp. Med. 198:423-431(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55617 mRNA. Translation: AAA39989.1.
M55616 Genomic DNA. Translation: AAA72939.1.
AY007569 mRNA. Translation: AAG24503.1.
X68804 mRNA. Translation: CAA48704.1.
AB051900 mRNA. Translation: BAB18732.1. Different initiation.
CCDSCCDS27140.1.
PIRB38678.
JE0151.
S26042.
RefSeqNP_034909.2. NM_010779.2.
UniGeneMm.439684.

3D structure databases

ProteinModelPortalP21812.
SMRP21812. Positions 21-243.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.149.

Proteomic databases

MaxQBP21812.
PRIDEP21812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17227.
KEGGmmu:17227.

Organism-specific databases

CTD17227.
MGIMGI:96940. Mcpt4.

Phylogenomic databases

HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP21812.
KOK01362.
PhylomeDBP21812.

Gene expression databases

GenevestigatorP21812.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291644.
PROP21812.
SOURCESearch...

Entry information

Entry nameMCPT4_MOUSE
AccessionPrimary (citable) accession number: P21812
Secondary accession number(s): Q9EPQ9, Q9EQT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot