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P21812

- MCPT4_MOUSE

UniProt

P21812 - MCPT4_MOUSE

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Protein

Mast cell protease 4

Gene

Mcpt4

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

Functioni

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.2 Publications

Enzyme regulationi

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.

pH dependencei

Optimum pH is 9 at high salt concentrations.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Charge relay systemBy similarity
Active sitei109 – 1091Charge relay systemBy similarity
Active sitei202 – 2021Charge relay systemBy similarity

GO - Molecular functioni

  1. peptidase activity Source: MGI
  2. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. proteolysis Source: UniProtKB
  2. regulation of angiotensin levels in blood Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.149.

Names & Taxonomyi

Protein namesi
Recommended name:
Mast cell protease 4 (EC:3.4.21.-)
Short name:
mMCP-4
Alternative name(s):
MSMCP
Myonase
Serosal mast cell protease
Gene namesi
Name:Mcpt4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:96940. Mcpt4.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: MGI
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mice display an impaired ability to inactivate thrombin or degrade fibronectin in peritoneal cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 202Activation peptide3 PublicationsPRO_0000027453
Chaini21 – 246226Mast cell protease 4PRO_0000027454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 66PROSITE-ProRule annotation
Disulfide bondi143 ↔ 208PROSITE-ProRule annotation
Disulfide bondi174 ↔ 187PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

MaxQBiP21812.
PRIDEiP21812.

Expressioni

Tissue specificityi

Submucosal mast cells. In femoral muscle, detected in myocytes but not in mast cells.1 Publication

Gene expression databases

GenevestigatoriP21812.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP21812.
SMRiP21812. Positions 21-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 244224Peptidase 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

HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP21812.
KOiK01362.
PhylomeDBiP21812.

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.

P21812-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQALLFLMAL LLPSGAGAEE IIGGVESRPH SRPYMAHLEI TTERGFTATC
60 70 80 90 100
GGFLITRQFV MTAAHCSGRE ITVTLGAHDV SKTESTQQKI KVEKQIVHPK
110 120 130 140 150
YNFYSNLHDI MLLKLQKKAK ETPSVNVIPL PRPSDFIKPG KMCRAAGWGR
160 170 180 190 200
TGVTEPTSDT LREVKLRIMD KEACKNYWHY DYNLQVCVGS PRKKRSAYKG
210 220 230 240
DSGGPLLCAG VAHGIVSYGR GDAKPPAVFT RISSYVPWIN RVIKGE
Length:246
Mass (Da):27,204
Last modified:May 1, 1991 - v1
Checksum:i0887A1C71ACE2698
GO

Sequence cautioni

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

Mass spectrometryi

Molecular mass is 25187 Da from positions 21 - 246. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611M → L in strain: C57BL/6 and Leaden X A1.
Natural varianti160 – 1601T → I in strain: C57BL/6 and Leaden X A1.
Natural varianti246 – 2461E → KK in strain: C57BL/6 and Leaden X A1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27140.1.
PIRiB38678.
JE0151.
S26042.
RefSeqiNP_034909.2. NM_010779.2.
UniGeneiMm.439684.

Genome annotation databases

GeneIDi17227.
KEGGimmu:17227.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS27140.1.
PIRi B38678.
JE0151.
S26042.
RefSeqi NP_034909.2. NM_010779.2.
UniGenei Mm.439684.

3D structure databases

ProteinModelPortali P21812.
SMRi P21812. Positions 21-243.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.149.

Proteomic databases

MaxQBi P21812.
PRIDEi P21812.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 17227.
KEGGi mmu:17227.

Organism-specific databases

CTDi 17227.
MGIi MGI:96940. Mcpt4.

Phylogenomic databases

HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P21812.
KOi K01362.
PhylomeDBi P21812.

Miscellaneous databases

NextBioi 291644.
PROi P21812.
SOURCEi Search...

Gene expression databases

Genevestigatori P21812.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMCPT4_MOUSE
AccessioniPrimary (citable) accession number: P21812
Secondary accession number(s): Q9EPQ9, Q9EQT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 109 of the entry and version 1 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