Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P23946 (CMA1_HUMAN)

Last modified June 16, 2009. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chymase
    EC=3.4.21.39
Alternative name(s):
    Alpha-chymase
    Mast cell protease I
Gene names
Name: CMA1
Synonyms: CYH, CYM
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Secreted. Cytoplasmic granule. Note: Mast cell granules.

Tissue specificity

Mast cells in lung, heart, skin and placenta.

Sequence similarities

Belongs to the peptidase S1 family. Granzyme subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological processinterleukin-1 beta biosynthetic process

Inferred from direct assay. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: InterPro

regulation of inflammatory response

Inferred by curator. Source: UniProtKB

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity Ref.2

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Propeptide20 – 212Activation peptide
PRO_0000027433
Chain22 – 247226Chymase
PRO_0000027434

Regions

Domain22 – 245224Peptidase S1

Sites

Active site661Charge relay system
Active site1101Charge relay system
Active site2031Charge relay system

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Ref.1
Glycosylation1031N-linked (GlcNAc...)
Disulfide bond51 ↔ 67
Disulfide bond144 ↔ 209
Disulfide bond175 ↔ 188

Natural variations

Natural variant461G → R: dbSNP rs5246.
VAR_011770
Natural variant661H → R: dbSNP rs5247. Ref.3
VAR_011771
Natural variant981R → H: dbSNP rs13306252.
VAR_029190

Experimental info

Sequence conflict281C → S in AAB26828. Ref.4

Secondary structure

.................................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23946-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: DC1464A049ED6B00

FASTA24727,325
        10         20         30         40         50         60 
MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF CGGFLIRRNF 

        70         80         90        100        110        120 
VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA 

       130        140        150        160        170        180 
SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRD 

       190        200        210        220        230        240 
FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG RSDAKPPAVF TRISHYRPWI 


NQILQAN 

« Hide

References

« Hide 'large scale' references
[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: 2071582] [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: 1894611] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Heart.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-66.
[4]"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: 8495723] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-247.
[5]"Angiotensin II-forming heart chymase is a mast-cell-specific enzyme."
Jenne D.E., Tschopp J.
Biochem. J. 276:567-568(1991) [PubMed: 2049082] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 26-60.
Tissue: Placenta.
[6]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-103, MASS SPECTROMETRY.
Tissue: Liver.
[7]"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: 9400368] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[8]"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: 9931257] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[9]Erratum
Pereira P.J.P., Wang Z.-M., Rubin H., Huber R., Bode W., Schechter N.M., Strobl S.
J. Mol. Biol. 286:817-817(1999) [PubMed: 10208809] [Abstract]
+Additional computationally mapped references.

Cross-references

Sequence databases

M64269 Genomic DNA. Translation: AAA52020.1.
M69137 Genomic DNA. Translation: AAA52021.1.
M69136 mRNA. Translation: AAA52019.1.
BC069110 mRNA. Translation: AAH69110.1.
BC069370 mRNA. Translation: AAH69370.1.
BC069490 mRNA. Translation: AAH69490.1.
BC103975 mRNA. Translation: AAI03976.1.
X59072 Genomic DNA. Translation: CAA41796.1.
S61334 mRNA. Translation: AAB26828.1.
IPIIPI00013937.
PIRKYHUCM. A40967.
RefSeqNP_001827.1.
UniGeneHs.135626

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KLTX-ray1.90A22-247[»]
1NN6X-ray1.75A20-247[»]
1PJPX-ray2.20A22-247[»]
1T31X-ray1.90A22-247[»]
2HVXX-ray2.60A22-247[»]
ModBaseSearch...

Protein family/group databases

MEROPSS01.140.

PTM databases

PhosphoSiteP23946.

Proteomic databases

PRIDEP23946.

Genome annotation databases

EnsemblENSG00000092009. Homo sapiens. [Contig view]
GeneID1215.
KEGGhsa:1215.

Organism-specific databases

GeneCardsGC14M024044.
H-InvDBHIX0037752.
HGNCHGNC:2097. CMA1.
HPACAB000363.
MIM118938. gene.
PharmGKBPA26623.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP23946.
OMAP23946. RKTKSAF.

Enzyme and pathway databases

BRENDA3.4.21.39. 247.

Gene expression databases

ArrayExpressP23946.
BgeeP23946.
CleanExHS_CMA1.
GermOnlineENSG00000092009. Homo sapiens.

Family and domain databases

InterProIPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP23946.
NextBio5003.
PMAP-CutDBP23946.
SOURCESearch...

Entry information

Entry nameCMA1_HUMAN
AccessionPrimary (citable) accession number: P23946
Secondary accession number(s): Q16018, Q3SY36
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents