ID MCPT4_RAT Reviewed; 246 AA.
AC P97592;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Mast cell protease 4;
DE Short=rMCP-4;
DE EC=3.4.21.-;
DE AltName: Full=Mast cell protease IV;
DE Short=rMCP-IV;
DE Flags: Precursor;
GN Name=Mcpt4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=8996238; DOI=10.1084/jem.185.1.13;
RA Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.;
RT "Secretory granule proteases in rat mast cells. Cloning of 10 different
RT serine proteases and a carboxypeptidase A from various rat mast cell
RT populations.";
RL J. Exp. Med. 185:13-29(1997).
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. Note=Secretory
CC granules.
CC -!- TISSUE SPECIFICITY: Mast cells.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; U67907; AAB48260.1; -; mRNA.
DR RefSeq; NP_062194.1; NM_019321.2.
DR AlphaFoldDB; P97592; -.
DR SMR; P97592; -.
DR STRING; 10116.ENSRNOP00000069727; -.
DR MEROPS; S01.005; -.
DR PhosphoSitePlus; P97592; -.
DR PaxDb; 10116-ENSRNOP00000027918; -.
DR Ensembl; ENSRNOT00000089559.2; ENSRNOP00000069727.1; ENSRNOG00000024785.5.
DR Ensembl; ENSRNOT00055020505; ENSRNOP00055016507; ENSRNOG00055012065.
DR Ensembl; ENSRNOT00060041624; ENSRNOP00060034494; ENSRNOG00060024019.
DR Ensembl; ENSRNOT00065053164; ENSRNOP00065043665; ENSRNOG00065030849.
DR GeneID; 54270; -.
DR KEGG; rno:54270; -.
DR UCSC; RGD:3064; rat.
DR AGR; RGD:3064; -.
DR CTD; 17227; -.
DR RGD; 3064; Mcpt4.
DR VEuPathDB; HostDB:ENSRNOG00000070675; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR InParanoid; P97592; -.
DR OMA; LRIMEMK; -.
DR OrthoDB; 2540265at2759; -.
DR PhylomeDB; P97592; -.
DR TreeFam; TF333630; -.
DR PRO; PR:P97592; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000024785; Expressed in thymus and 5 other cell types or tissues.
DR ExpressionAtlas; P97592; baseline and differential.
DR Genevisible; P97592; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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 PANTHER; PTHR24271:SF23; CHYMASE 2, MAST CELL-RELATED; 1.
DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..20
FT /note="Activation peptide"
FT /id="PRO_0000027445"
FT CHAIN 21..246
FT /note="Mast cell protease 4"
FT /id="PRO_0000027446"
FT DOMAIN 21..244
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 109
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 143..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 174..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ SEQUENCE 246 AA; 27042 MW; 412FF51D05098778 CRC64;
MKALLFLMAL LLPSGAGAEE IIGGVESIPH SRPYMALLKI VTEEGHVTFC GGFLISLQFV
LTAAHCHGRE ITVTLGAHDM SKRESTQQKI KVVKQIFPLK YNLFSNFRDI MLLKLEQKAV
LTPSVNVIPL PQSSDIIKPG TMCLAAGWGQ TGVKEPNSNT LREVMLRIME MKACKDYRHY
DNRFQICVGI PQMLKLAYKG DSGGPLVCAG VAHGIVSHGP GRGIPPIIFT RISSYVSWIN
RVIRGN
//
