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P50339

- CMA1_RAT

UniProt

P50339 - CMA1_RAT

Protein

Chymase

Gene

Cma1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

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

    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. peptidase activity Source: RGD
    2. peptide binding Source: RGD
    3. serine-type endopeptidase activity Source: RGD

    GO - Biological processi

    1. cellular response to glucose stimulus Source: RGD
    2. interleukin-1 beta biosynthetic process Source: Ensembl
    3. midbrain development Source: RGD
    4. peptide metabolic process Source: RGD
    5. positive regulation of angiogenesis Source: RGD
    6. proteolysis Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    ReactomeiREACT_195025. Signaling by SCF-KIT.
    REACT_198590. Activation of Matrix Metalloproteinases.
    REACT_198807. Metabolism of Angiotensinogen to Angiotensins.

    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 protease 3
    Short name:
    rMCP-3
    Mast cell protease 5
    Short name:
    rMCP-5
    Mast cell protease III
    Short name:
    rMCP-III
    Gene namesi
    Name:Cma1
    Synonyms:Mcpt3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi2365. Cma1.

    Subcellular locationi

    Secreted. Cytoplasmic granule
    Note: Secretory granules.

    GO - Cellular componenti

    1. extracellular matrix Source: Ensembl
    2. extracellular region Source: RGD
    3. intracellular Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Propeptidei20 – 212Activation peptidePRO_0000027443
    Chaini22 – 247226ChymasePRO_0000027444Add
    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

    PRIDEiP50339.

    Expressioni

    Tissue specificityi

    Mast cells.

    Gene expression databases

    GenevestigatoriP50339.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliP50339.
    SMRiP50339. 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

    GeneTreeiENSGT00740000115279.
    HOVERGENiHBG013304.
    KOiK01329.
    OMAiTLHHDIM.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiP50339.

    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.

    P50339-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLHALCLLL LLLGSSTKAG EIIGGTECIP HSRPYMAYLE IVTSDNYLSA    50
    CSGFLIRRNF VLTAAHCAGR SITVLLGAHN KTYKEDTWQK LEVEKQFIHP 100
    NYDKRLVLHD IMLLKLKEKA KLTLGVGTLP LSANFNFIPP GRMCRAVGWG 150
    RTNVNEPASD TLQEVKMRLQ EPQSCKHFTS FQHKSQLCVG NPKKMQNVYK 200
    GDSGGPLLCA GIAQGIASYV HPNAKPPAVF TRISHYRPWI NKILREN 247
    Length:247
    Mass (Da):27,569
    Last modified:October 1, 1996 - v1
    Checksum:i6525D7BF1BFDF053
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38495 mRNA. Translation: BAA07507.1.
    U67908 mRNA. Translation: AAB48261.1.
    PIRiS59135.
    RefSeqiNP_037224.1. NM_013092.1.
    UniGeneiRn.10182.

    Genome annotation databases

    EnsembliENSRNOT00000067539; ENSRNOP00000061330; ENSRNOG00000020563.
    GeneIDi25627.
    KEGGirno:25627.
    UCSCiRGD:2365. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38495 mRNA. Translation: BAA07507.1 .
    U67908 mRNA. Translation: AAB48261.1 .
    PIRi S59135.
    RefSeqi NP_037224.1. NM_013092.1.
    UniGenei Rn.10182.

    3D structure databases

    ProteinModelPortali P50339.
    SMRi P50339. Positions 22-247.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P50339.
    ChEMBLi CHEMBL3168.

    Protein family/group databases

    MEROPSi S01.150.

    Proteomic databases

    PRIDEi P50339.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000067539 ; ENSRNOP00000061330 ; ENSRNOG00000020563 .
    GeneIDi 25627.
    KEGGi rno:25627.
    UCSCi RGD:2365. rat.

    Organism-specific databases

    CTDi 1215.
    RGDi 2365. Cma1.

    Phylogenomic databases

    GeneTreei ENSGT00740000115279.
    HOVERGENi HBG013304.
    KOi K01329.
    OMAi TLHHDIM.
    OrthoDBi EOG7RRF7Z.
    PhylomeDBi P50339.

    Enzyme and pathway databases

    Reactomei REACT_195025. Signaling by SCF-KIT.
    REACT_198590. Activation of Matrix Metalloproteinases.
    REACT_198807. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    NextBioi 607417.

    Gene expression databases

    Genevestigatori P50339.

    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 encoding a novel rat mast-cell proteinase, rMCP-3, and its expression in comparison with other rat mast-cell proteinases."
      Ide H., Itoh H., Tomita M., Murakumo Y., Kobayashi T., Maruyama H., Osada Y., Nawa Y.
      Biochem. J. 311:675-680(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peritoneal mast cell.
    2. "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] OF 2-247.
      Strain: Sprague-Dawley.

    Entry informationi

    Entry nameiCMA1_RAT
    AccessioniPrimary (citable) accession number: P50339
    Secondary accession number(s): Q9R2C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 94 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, 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