TRYM_CANLF
ID TRYM_CANLF Reviewed; 280 AA.
AC P19236; Q66NX5; Q66NX6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Mastin;
DE EC=3.4.21.-;
DE AltName: Full=Mast cell protease 3;
DE Short=DMP;
DE Short=MCP-3;
DE Short=dMCP-3;
DE AltName: Full=Mastocytoma protease;
DE Flags: Precursor;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND SUBUNIT.
RC TISSUE=Lung;
RX PubMed=15708374; DOI=10.1016/j.abb.2004.12.025;
RA Raymond W.W., Sommerhoff C.P., Caughey G.H.;
RT "Mastin is a gelatinolytic mast cell peptidase resembling a mini-
RT proteasome.";
RL Arch. Biochem. Biophys. 435:311-322(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-280.
RC TISSUE=Mastocytoma;
RX PubMed=2504277; DOI=10.1021/bi00436a004;
RA Vanderslice P., Craik C.S., Nadel J.A., Caughey G.H.;
RT "Molecular cloning of dog mast cell tryptase and a related protease:
RT structural evidence of a unique mode of serine protease activation.";
RL Biochemistry 28:4148-4155(1989).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Caughey G.H.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 31-42, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, AND GLYCOSYLATION.
RC TISSUE=Mastocytoma;
RX PubMed=7768912; DOI=10.1074/jbc.270.22.13164;
RA Raymond W.W., Tam E.K., Blount J.L., Caughey G.H.;
RT "Purification and characterization of dog mast cell protease-3, an
RT oligomeric relative of tryptases.";
RL J. Biol. Chem. 270:13164-13170(1995).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8144904;
RA Yezzi M.J., Hsieh I.E., Caughey G.H.;
RT "Mast cell and neutrophil expression of dog mast cell protease-3. A novel
RT tryptase-related serine protease.";
RL J. Immunol. 152:3064-3072(1994).
CC -!- FUNCTION: Trypsin-like serine protease. Has a preference for extended
CC substrates with basic residues at the P1 position; Arg is preferred
CC over Lys. Active towards calcitonin gene-related peptide and gelatin.
CC Not active towards substance P, vasoactive intestinal peptide, type I
CC collagen or azocasein. {ECO:0000269|PubMed:15708374}.
CC -!- ACTIVITY REGULATION: Inhibited by leupeptin and bis(5-amidino-2-
CC benzimidazolyl)methane (BABIM). {ECO:0000269|PubMed:7768912}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0-8.5.;
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000269|PubMed:15708374,
CC ECO:0000269|PubMed:7768912}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8144904}.
CC -!- TISSUE SPECIFICITY: Mononuclear cells within skin, intestine, trachea
CC and lung parenchyma, and polymorphonuclear leukocytes within
CC capillaries and blood. {ECO:0000269|PubMed:8144904}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7768912}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY665677; AAU06206.1; -; mRNA.
DR EMBL; AY665678; AAU06207.1; -; Genomic_DNA.
DR EMBL; M24665; AAA30855.2; -; mRNA.
DR PIR; B32410; B32410.
DR RefSeq; NP_001005260.1; NM_001005260.1.
DR AlphaFoldDB; P19236; -.
DR SMR; P19236; -.
DR STRING; 9612.ENSCAFP00000028974; -.
DR MEROPS; S01.145; -.
DR PaxDb; P19236; -.
DR GeneID; 448801; -.
DR KEGG; cfa:448801; -.
DR eggNOG; KOG3627; Eukaryota.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..30
FT /evidence="ECO:0000269|PubMed:7768912"
FT /id="PRO_0000027475"
FT CHAIN 31..280
FT /note="Mastin"
FT /id="PRO_0000027476"
FT DOMAIN 31..275
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 77
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 161..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 194..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 224..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 123
FT /note="W -> R (in Ref. 1; AAU06207)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="S -> T (in Ref. 2; AAA30855)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="K -> R (in Ref. 1; AAU06207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 31025 MW; 20D2A44A02B8D986 CRC64;
MLWLLVLTAP WLGGSVPISP DPGLRHEQVG IVGGCKVPAR RYPWQVSLRF HGMGSGQWQH
ICGGSLIHPQ WVLTAAHCVE LEGLEAATLR VQVGQLRLYD HDQLCNVTEI IRHPNFNMSW
YGWDSADIAL LKLEAPLTLS EDVNLVSLPS PSLIVPPGML CWVTGWGDIA DHTPLPPPYH
LQEVEVPIVG NRECNCHYQT ILEQDDEVIK QDMLCAGSEG HDSCQMDSGG PLVCRWKCTW
IQVGVVSWGY GCGYNLPGVY ARVTSYVSWI HQHIPLSPGP
