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P09650

- MCPT1_RAT

UniProt

P09650 - MCPT1_RAT

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Protein

Mast cell protease 1

Gene

Mcpt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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: RGD

GO - Biological processi

  1. 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: 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 region Source: UniProtKB-KW
  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 .
PIRi JC2125.
RefSeqi NP_001264597.1. NM_001277668.1.
UniGenei Rn.145977.
Rn.202971.

3D structure databases

ProteinModelPortali P09650.
SMRi P09650. Positions 21-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000028012.

Protein family/group databases

MEROPSi S01.149.

Proteomic databases

PaxDbi P09650.
PRIDEi P09650.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000028012 ; ENSRNOP00000028012 ; ENSRNOG00000020633 .
GeneIDi 100360872.
KEGGi rno:100360872.
UCSCi RGD:3062. rat.

Organism-specific databases

CTDi 100360872.
RGDi 3062. Mcpt1.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118895.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P09650.
OMAi YMAQLEI.
PhylomeDBi P09650.
TreeFami TF333630.

Miscellaneous databases

PROi P09650.

Gene expression databases

ExpressionAtlasi P09650. baseline.
Genevestigatori P09650.

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. "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(1997) [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(1994) [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(1987) [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(1978) [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(1993) [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: October 29, 2014
This is version 124 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