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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   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.
DR   Genevisible; P97592; RN.
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
//