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Protein

Mast cell protease 1

Gene

Mcpt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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. May participate in generating perivascular beta-protein which ultimately aggregates into beta-amyloid deposits.1 Publication

Catalytic activityi

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

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. serine-type endopeptidase activity Source: GO_Central

GO - Biological processi

  1. protein processing Source: GO_Central
  2. regulation of angiotensin levels in blood Source: Ensembl
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 1 (EC:3.4.21.39)
Short name:
rMCP-1
Alternative name(s):
Chymase
Chymotrypsin-like protease
Short name:
CLIP protein
Mast cell protease I
Short name:
rMCP-I
Gene namesi
Name:Mcpt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi3062. Mcpt1.

Subcellular locationi

Secreted By similarity. Cytoplasmic granule By similarity
Note: Mast cell granules.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 202Activation peptide3 PublicationsPRO_0000027439
Chaini21 – 260240Mast cell protease 1PRO_0000027440Add
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

PaxDbiP09650.
PRIDEiP09650.

Expressioni

Gene expression databases

ExpressionAtlasiP09650. baseline.
GenevestigatoriP09650.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028012.

Structurei

3D structure databases

ProteinModelPortaliP09650.
SMRiP09650. 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

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP09650.
OMAiYMAQLEI.
PhylomeDBiP09650.
TreeFamiTF333630.

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.

P09650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQALLFLMAL LLPSGAGAEE IIGGVESRPH SRPYMAHLEI TTERGYKATC
60 70 80 90 100
GGFLVTRQFV MTAAHCKGRE TTVTLGVHDV SKTESTQQKI KVEKQIVHPN
110 120 130 140 150
YNFYSNLHDI MLLKLQKKAK VTPAVDVIPL PQPSDFLKPG KMCRAAGWGQ
160 170 180 190 200
TGVTKPTSNT LREVKQRIMD KEACKNYFHY NYNFQVCVGS PRKIRSAYKG
210 220 230 240 250
DSGGPLVCAG VAHGIVSYGR GDAKPPAVFT RISPYVPWIN KVIKGKDLTS
260
LSLHESESPS
Length:260
Mass (Da):28,617
Last modified:November 1, 1997 - v3
Checksum:i076278089C1F8A96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 583TRQ → NRN AA sequence (PubMed:3122823).Curated
Sequence conflicti70 – 712ET → NE AA sequence (PubMed:3122823).Curated
Sequence conflicti91 – 944KVEK → ALEI AA sequence (PubMed:8336143).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67915 mRNA. Translation: AAB48268.1.
S69206 mRNA. Translation: AAB30269.1.
PIRiJC2125.
RefSeqiNP_001264597.1. NM_001277668.1.
UniGeneiRn.145977.
Rn.202971.

Genome annotation databases

EnsembliENSRNOT00000028012; ENSRNOP00000028012; ENSRNOG00000020633.
GeneIDi100360872.
KEGGirno:100360872.
UCSCiRGD:3062. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67915 mRNA. Translation: AAB48268.1.
S69206 mRNA. Translation: AAB30269.1.
PIRiJC2125.
RefSeqiNP_001264597.1. NM_001277668.1.
UniGeneiRn.145977.
Rn.202971.

3D structure databases

ProteinModelPortaliP09650.
SMRiP09650. Positions 21-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028012.

Protein family/group databases

MEROPSiS01.149.

Proteomic databases

PaxDbiP09650.
PRIDEiP09650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028012; ENSRNOP00000028012; ENSRNOG00000020633.
GeneIDi100360872.
KEGGirno:100360872.
UCSCiRGD:3062. rat.

Organism-specific databases

CTDi100360872.
RGDi3062. Mcpt1.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP09650.
OMAiYMAQLEI.
PhylomeDBiP09650.
TreeFamiTF333630.

Miscellaneous databases

PROiP09650.

Gene expression databases

ExpressionAtlasiP09650. baseline.
GenevestigatoriP09650.

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. "Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."
    Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.
    J. Exp. Med. 185:13-29(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Mast cell.
  2. "Molecular cloning of rat mast cell protease 1 and development of specific probes for its gene transcript."
    Rouleau A., Garbarg M., Schwartz J.C., Ruat M.
    Biochem. Biophys. Res. Commun. 199:593-602(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-260.
  3. "Amino acid sequence of rat mast cell protease I (chymase)."
    le Trong H., Parmelee D.C., Walsh K.A., Neurath H., Woodbury R.G.
    Biochemistry 26:6988-6994(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-247.
  4. "A major serine protease in rat skeletal muscle: evidence for its mast cell origin."
    Woodbury R.G., Everitt M., Sanada Y., Katunuma N., Lagunoff D., Neurath H.
    Proc. Natl. Acad. Sci. U.S.A. 75:5311-5313(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-73.
  5. "Identification of a chymotrypsin-like mast cell protease in rat brain capable of generating the N-terminus of the Alzheimer amyloid beta-protein."
    Nelson R.B., Siman R., Iqbal M.A., Potter H.
    J. Neurochem. 61:567-577(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-34; 91-101 AND 232-238, FUNCTION.

Entry informationi

Entry nameiMCPT1_RAT
AccessioniPrimary (citable) accession number: P09650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: March 4, 2015
This is version 127 of the entry and version 3 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.