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P23946

- CMA1_HUMAN

UniProt

P23946 - CMA1_HUMAN

Protein

Chymase

Gene

CMA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei66 – 661Charge relay system
    Active sitei110 – 1101Charge relay system
    Active sitei203 – 2031Charge relay system

    GO - Molecular functioni

    1. peptide binding Source: Ensembl
    2. serine-type endopeptidase activity Source: UniProtKB
    3. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. angiotensin maturation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. cellular response to glucose stimulus Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. interleukin-1 beta biosynthetic process Source: BHF-UCL
    7. midbrain development Source: Ensembl
    8. peptide metabolic process Source: Ensembl
    9. positive regulation of angiogenesis Source: Ensembl
    10. regulation of inflammatory response Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKP23946.

    Protein family/group databases

    MEROPSiS01.140.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymase (EC:3.4.21.39)
    Alternative name(s):
    Alpha-chymase
    Mast cell protease I
    Gene namesi
    Name:CMA1
    Synonyms:CYH, CYM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2097. CMA1.

    Subcellular locationi

    Secreted. Cytoplasmic granule
    Note: Mast cell granules.

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. intracellular Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26623.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Propeptidei20 – 212Activation peptide1 PublicationPRO_0000027433
    Chaini22 – 247226ChymasePRO_0000027434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 67
    Glycosylationi80 – 801N-linked (GlcNAc...)2 Publications
    Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
    Disulfide bondi144 ↔ 209
    Disulfide bondi175 ↔ 188

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP23946.
    PRIDEiP23946.

    PTM databases

    PhosphoSiteiP23946.

    Miscellaneous databases

    PMAP-CutDBP23946.

    Expressioni

    Tissue specificityi

    Mast cells in lung, heart, skin and placenta. Expressed in both normal skin and in urticaria pigmentosa lesions.1 Publication

    Gene expression databases

    ArrayExpressiP23946.
    BgeeiP23946.
    CleanExiHS_CMA1.
    GenevestigatoriP23946.

    Organism-specific databases

    HPAiCAB000363.
    HPA052634.

    Interactioni

    Protein-protein interaction databases

    BioGridi107624. 2 interactions.
    STRINGi9606.ENSP00000250378.

    Structurei

    Secondary structure

    1
    247
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 427
    Beta strandi44 – 474
    Beta strandi49 – 579
    Beta strandi60 – 634
    Helixi65 – 673
    Beta strandi70 – 778
    Beta strandi79 – 835
    Beta strandi89 – 9810
    Turni104 – 1063
    Beta strandi112 – 1187
    Beta strandi124 – 1263
    Beta strandi143 – 15311
    Beta strandi163 – 1708
    Helixi172 – 1754
    Turni183 – 1853
    Beta strandi186 – 1905
    Turni192 – 1943
    Beta strandi206 – 2094
    Beta strandi212 – 2198
    Beta strandi228 – 2325
    Helixi233 – 24614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KLTX-ray1.90A22-247[»]
    1NN6X-ray1.75A20-247[»]
    1PJPX-ray2.20A22-247[»]
    1T31X-ray1.90A22-247[»]
    2HVXX-ray2.60A22-247[»]
    3N7OX-ray1.80A22-247[»]
    3S0NX-ray1.95A22-247[»]
    4AFQX-ray1.51A/B22-247[»]
    4AFSX-ray1.90A22-247[»]
    4AFUX-ray1.82A/B22-247[»]
    4AFZX-ray2.25A/B22-247[»]
    4AG1X-ray1.40A22-247[»]
    4AG2X-ray1.80A/B22-247[»]
    4K2YX-ray2.30A22-247[»]
    4K5ZX-ray1.80A22-247[»]
    4K60X-ray1.50A22-247[»]
    4K69X-ray1.50A22-247[»]
    4KP0X-ray2.80A22-247[»]
    ProteinModelPortaliP23946.
    SMRiP23946. Positions 22-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23946.

    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

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP23946.
    KOiK01329.
    OMAiTLHHDIM.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiP23946.
    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.

    P23946-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF    50
    CGGFLIRRNF VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP 100
    KYNTSTLHHD IMLLKLKEKA SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG 150
    RTGVLKPGSD TLQEVKLRLM DPQACSHFRD FDHNLQLCVG NPRKTKSAFK 200
    GDSGGPLLCA GVAQGIVSYG RSDAKPPAVF TRISHYRPWI NQILQAN 247
    Length:247
    Mass (Da):27,325
    Last modified:March 1, 1992 - v1
    Checksum:iDC1464A049ED6B00
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281C → S in AAB26828. (PubMed:8495723)Curated
    Sequence conflicti131 – 1322FP → AV AA sequence (PubMed:8144971)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461G → R.
    Corresponds to variant rs5246 [ dbSNP | Ensembl ].
    VAR_011770
    Natural varianti66 – 661H → R.1 Publication
    Corresponds to variant rs5247 [ dbSNP | Ensembl ].
    VAR_011771
    Natural varianti98 – 981R → H.
    Corresponds to variant rs13306252 [ dbSNP | Ensembl ].
    VAR_029190

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64269 Genomic DNA. Translation: AAA52020.1.
    M69137 Genomic DNA. Translation: AAA52021.1.
    M69136 mRNA. Translation: AAA52019.1.
    AB451464 mRNA. Translation: BAG70278.1.
    CH471078 Genomic DNA. Translation: EAW66007.1.
    BC069110 mRNA. Translation: AAH69110.1.
    BC069370 mRNA. Translation: AAH69370.1.
    BC069490 mRNA. Translation: AAH69490.1.
    BC103975 mRNA. Translation: AAI03976.1.
    S61334 mRNA. Translation: AAB26828.1.
    X59072 Genomic DNA. Translation: CAA41796.1.
    CCDSiCCDS9630.1.
    PIRiA40967. KYHUCM.
    RefSeqiNP_001827.1. NM_001836.3.
    UniGeneiHs.135626.

    Genome annotation databases

    EnsembliENST00000250378; ENSP00000250378; ENSG00000092009.
    GeneIDi1215.
    KEGGihsa:1215.
    UCSCiuc001wpp.1. human.

    Polymorphism databases

    DMDMi126825.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64269 Genomic DNA. Translation: AAA52020.1 .
    M69137 Genomic DNA. Translation: AAA52021.1 .
    M69136 mRNA. Translation: AAA52019.1 .
    AB451464 mRNA. Translation: BAG70278.1 .
    CH471078 Genomic DNA. Translation: EAW66007.1 .
    BC069110 mRNA. Translation: AAH69110.1 .
    BC069370 mRNA. Translation: AAH69370.1 .
    BC069490 mRNA. Translation: AAH69490.1 .
    BC103975 mRNA. Translation: AAI03976.1 .
    S61334 mRNA. Translation: AAB26828.1 .
    X59072 Genomic DNA. Translation: CAA41796.1 .
    CCDSi CCDS9630.1.
    PIRi A40967. KYHUCM.
    RefSeqi NP_001827.1. NM_001836.3.
    UniGenei Hs.135626.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KLT X-ray 1.90 A 22-247 [» ]
    1NN6 X-ray 1.75 A 20-247 [» ]
    1PJP X-ray 2.20 A 22-247 [» ]
    1T31 X-ray 1.90 A 22-247 [» ]
    2HVX X-ray 2.60 A 22-247 [» ]
    3N7O X-ray 1.80 A 22-247 [» ]
    3S0N X-ray 1.95 A 22-247 [» ]
    4AFQ X-ray 1.51 A/B 22-247 [» ]
    4AFS X-ray 1.90 A 22-247 [» ]
    4AFU X-ray 1.82 A/B 22-247 [» ]
    4AFZ X-ray 2.25 A/B 22-247 [» ]
    4AG1 X-ray 1.40 A 22-247 [» ]
    4AG2 X-ray 1.80 A/B 22-247 [» ]
    4K2Y X-ray 2.30 A 22-247 [» ]
    4K5Z X-ray 1.80 A 22-247 [» ]
    4K60 X-ray 1.50 A 22-247 [» ]
    4K69 X-ray 1.50 A 22-247 [» ]
    4KP0 X-ray 2.80 A 22-247 [» ]
    ProteinModelPortali P23946.
    SMRi P23946. Positions 22-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107624. 2 interactions.
    STRINGi 9606.ENSP00000250378.

    Chemistry

    BindingDBi P23946.
    ChEMBLi CHEMBL4068.
    GuidetoPHARMACOLOGYi 2340.

    Protein family/group databases

    MEROPSi S01.140.

    PTM databases

    PhosphoSitei P23946.

    Polymorphism databases

    DMDMi 126825.

    Proteomic databases

    PaxDbi P23946.
    PRIDEi P23946.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250378 ; ENSP00000250378 ; ENSG00000092009 .
    GeneIDi 1215.
    KEGGi hsa:1215.
    UCSCi uc001wpp.1. human.

    Organism-specific databases

    CTDi 1215.
    GeneCardsi GC14M024974.
    HGNCi HGNC:2097. CMA1.
    HPAi CAB000363.
    HPA052634.
    MIMi 118938. gene.
    neXtProti NX_P23946.
    PharmGKBi PA26623.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi P23946.
    KOi K01329.
    OMAi TLHHDIM.
    OrthoDBi EOG7RRF7Z.
    PhylomeDBi P23946.
    TreeFami TF333630.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RK P23946.

    Miscellaneous databases

    EvolutionaryTracei P23946.
    GeneWikii CMA1.
    GenomeRNAii 1215.
    NextBioi 5003.
    PMAP-CutDB P23946.
    PROi P23946.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23946.
    Bgeei P23946.
    CleanExi HS_CMA1.
    Genevestigatori P23946.

    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. "Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase."
      Caughey G.H., Zerweck E.H., Vanderslice P.
      J. Biol. Chem. 266:12956-12963(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning of the gene and cDNA for human heart chymase."
      Urata H., Kinoshita A., Perez D.M., Misono K.S., Bumpus F.M., Graham R.M., Husain A.
      J. Biol. Chem. 266:17173-17179(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Heart.
    3. "Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions."
      Schechter N.M., Wang Z.M., Blacher R.W., Lessin S.R., Lazarus G.S., Rubin H.
      J. Immunol. 152:4062-4069(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-56; 123-132; 136-148; 167-194 AND 197-247, TISSUE SPECIFICITY.
      Tissue: Skin.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-66.
    7. "Purification and molecular cloning of chymase from human tonsils."
      Sukenaga Y., Kido H., Neki A., Enomoto M., Ishida K., Takagi K., Katunuma N.
      FEBS Lett. 323:119-122(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-247.
    8. "Angiotensin II-forming heart chymase is a mast-cell-specific enzyme."
      Jenne D.E., Tschopp J.
      Biochem. J. 276:567-568(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-60.
      Tissue: Placenta.
    9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-103.
      Tissue: Liver.
    10. "Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A."
      McGrath M.E., Mirzadegan T., Schmidt B.F.
      Biochemistry 36:14318-14324(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    11. "The 2.2-A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity."
      Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M., Strobl S.
      J. Mol. Biol. 286:163-173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiCMA1_HUMAN
    AccessioniPrimary (citable) accession number: P23946
    Secondary accession number(s): B5BUM8
    , Q16018, Q3SY36, Q9UDH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3