MCPT2_RAT
ID MCPT2_RAT Reviewed; 247 AA.
AC P00770;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mast cell protease 2;
DE Short=rMCP-2;
DE EC=3.4.21.-;
DE AltName: Full=Group-specific protease;
DE AltName: Full=Mast cell protease II;
DE Short=rMCP-II;
DE Flags: Precursor;
GN Name=Mcpt2;
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 [GENOMIC DNA].
RX PubMed=3549719; DOI=10.1016/s0021-9258(18)61198-6;
RA Benfey P.N., Yin F.H., Leder P.;
RT "Cloning of the mast cell protease, RMCP II. Evidence for cell-specific
RT expression and a multi-gene family.";
RL J. Biol. Chem. 262:5377-5384(1987).
RN [2]
RP PROTEIN SEQUENCE OF 21-244.
RX PubMed=629933; DOI=10.1021/bi00598a010;
RA Woodbury R.G., Katunuma N., Kobayashi K., Titani K., Neurath H.;
RT "Covalent structure of a group-specific protease from rat small intestine.
RT Appendix: crystallographic data for a group specific protease from rat
RT intestine.";
RL Biochemistry 17:811-819(1978).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=3233198; DOI=10.1021/bi00421a019;
RA Remington S.J., Woodbury R.G., Reynolds R.A., Matthews B.W., Neurath H.;
RT "The structure of rat mast cell protease II at 1.9-A resolution.";
RL Biochemistry 27:8097-8105(1988).
CC -!- FUNCTION: This enzyme, isolated from small intestine, specifically
CC inactivates the apo forms of a certain group of intracellular pyridoxal
CC phosphate-requiring enzymes. It has chymotrypsin-like specificity
CC towards small substrates.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; J02712; AAA66284.1; -; Genomic_DNA.
DR PIR; A29548; PRRTG.
DR RefSeq; NP_742041.1; NM_172044.1.
DR PDB; 3RP2; X-ray; 1.90 A; A/B=21-244.
DR PDBsum; 3RP2; -.
DR AlphaFoldDB; P00770; -.
DR SMR; P00770; -.
DR STRING; 10116.ENSRNOP00000027988; -.
DR MEROPS; S01.141; -.
DR PaxDb; P00770; -.
DR PRIDE; P00770; -.
DR Ensembl; ENSRNOT00000091757; ENSRNOP00000069470; ENSRNOG00000020625.
DR GeneID; 29266; -.
DR KEGG; rno:29266; -.
DR UCSC; RGD:621058; rat.
DR CTD; 17225; -.
DR RGD; 621058; Mcpt2.
DR VEuPathDB; HostDB:ENSRNOG00000031304; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P00770; -.
DR OMA; WGKTGVR; -.
DR OrthoDB; 1522379at2759; -.
DR PhylomeDB; P00770; -.
DR TreeFam; TF333630; -.
DR EvolutionaryTrace; P00770; -.
DR PRO; PR:P00770; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000020625; Expressed in stomach and 14 other tissues.
DR ExpressionAtlas; P00770; baseline and differential.
DR Genevisible; P00770; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR033116; TRYPSIN_SER.
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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Reference proteome; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..20
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:629933"
FT /id="PRO_0000027441"
FT CHAIN 21..247
FT /note="Mast cell protease 2"
FT /id="PRO_0000027442"
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 ACT_SITE 109
FT /note="Charge relay system"
FT ACT_SITE 202
FT /note="Charge relay system"
FT DISULFID 50..66
FT DISULFID 143..208
FT DISULFID 174..187
FT CONFLICT 238
FT /note="W -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 47..62
FT /evidence="ECO:0007829|PDB:3RP2"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:3RP2"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3RP2"
FT TURN 174..178
FT /evidence="ECO:0007829|PDB:3RP2"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3RP2"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:3RP2"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:3RP2"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:3RP2"
SQ SEQUENCE 247 AA; 27102 MW; 051988042A97A47E CRC64;
MQALLFLMAL LLPSGAGAEE IIGGVESIPH SRPYMAHLDI VTEKGLRVIC GGFLISRQFV
LTAAHCKGRE ITVILGAHDV RKRESTQQKI KVEKQIIHES YNSVPNLHDI MLLKLEKKVE
LTPAVNVVPL PSPSDFIHPG AMCWAAGWGK TGVRDPTSYT LREVELRIMD EKACVDYRYY
EYKFQVCVGS PTTLRAAFMG DSGGPLLCAG VAHGIVSYGH PDAKPPAIFT RVSTYVPWIN
AVINTSS
