(data stored in SCRATCH zone)

SWISSPROT: 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   05-JUL-2017, entry version 138.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3549719;
RA   Benfey P.N., Yin F.H., Leder P.;
RT   "Cloning of the mast cell protease, RMCP II. Evidence for cell-
RT   specific 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
RT   intestine. Appendix: crystallographic data for a group specific
RT   protease from rat 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.,
RA   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
CC       pyridoxal phosphate-requiring enzymes. It has chymotrypsin-like
CC       specificity towards small substrates.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; J02712; AAA66284.1; -; Genomic_DNA.
DR   PIR; A29548; PRRTG.
DR   RefSeq; NP_742041.1; NM_172044.1.
DR   UniGene; Rn.9443; -.
DR   PDB; 3RP2; X-ray; 1.90 A; A/B=21-244.
DR   PDBsum; 3RP2; -.
DR   ProteinModelPortal; P00770; -.
DR   SMR; P00770; -.
DR   STRING; 10116.ENSRNOP00000027988; -.
DR   MEROPS; S01.141; -.
DR   PaxDb; P00770; -.
DR   Ensembl; ENSRNOT00000027988; ENSRNOP00000027988; ENSRNOG00000020625.
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   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00760000118895; -.
DR   HOGENOM; HOG000251820; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P00770; -.
DR   KO; K08662; -.
DR   OMA; CKGREIT; -.
DR   PhylomeDB; P00770; -.
DR   TreeFam; TF333630; -.
DR   EvolutionaryTrace; P00770; -.
DR   PRO; PR:P00770; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000020625; -.
DR   ExpressionAtlas; P00770; baseline and differential.
DR   Genevisible; P00770; RN.
DR   GO; GO:0030141; C:secretory granule; 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   InterPro; IPR009003; Peptidase_S1_PA.
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;
DR   PRODOM; P00770.
DR   SWISS-2DPAGE; P00770.
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     18
FT   PROPEP       19     20       Activation peptide.
FT                                {ECO:0000269|PubMed:629933}.
FT                                /FTId=PRO_0000027441.
FT   CHAIN        21    247       Mast cell protease 2.
FT                                /FTId=PRO_0000027442.
FT   DOMAIN       21    244       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE     65     65       Charge relay system.
FT   ACT_SITE    109    109       Charge relay system.
FT   ACT_SITE    202    202       Charge relay system.
FT   DISULFID     50     66
FT   DISULFID    143    208
FT   DISULFID    174    187
FT   CONFLICT    238    238       W -> T (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       35     41       {ECO:0000244|PDB:3RP2}.
FT   STRAND       47     62       {ECO:0000244|PDB:3RP2}.
FT   HELIX        64     66       {ECO:0000244|PDB:3RP2}.
FT   STRAND       69     76       {ECO:0000244|PDB:3RP2}.
FT   STRAND       88     97       {ECO:0000244|PDB:3RP2}.
FT   STRAND      103    105       {ECO:0000244|PDB:3RP2}.
FT   STRAND      111    117       {ECO:0000244|PDB:3RP2}.
FT   STRAND      142    152       {ECO:0000244|PDB:3RP2}.
FT   STRAND      155    157       {ECO:0000244|PDB:3RP2}.
FT   STRAND      162    169       {ECO:0000244|PDB:3RP2}.
FT   HELIX       171    173       {ECO:0000244|PDB:3RP2}.
FT   TURN        174    178       {ECO:0000244|PDB:3RP2}.
FT   TURN        182    184       {ECO:0000244|PDB:3RP2}.
FT   STRAND      185    188       {ECO:0000244|PDB:3RP2}.
FT   TURN        199    203       {ECO:0000244|PDB:3RP2}.
FT   STRAND      205    208       {ECO:0000244|PDB:3RP2}.
FT   STRAND      211    218       {ECO:0000244|PDB:3RP2}.
FT   STRAND      227    231       {ECO:0000244|PDB:3RP2}.
FT   HELIX       232    243       {ECO:0000244|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
//

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