ID   GRZ2_RAT                Reviewed;         248 AA.
AC   Q06606;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Granzyme-like protein 2;
DE            EC=3.4.21.-;
DE   AltName: Full=GLP-2;
DE   AltName: Full=Granzyme-like protein II;
DE            Short=GLP II;
DE   AltName: Full=Mast cell protease 10;
DE            Short=rMCP-10;
DE   AltName: Full=Mast cell protease X;
DE            Short=rMCP-X;
DE   Flags: Precursor;
GN   Name=Mcpt10;
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   TISSUE=Duodenum;
RX   PubMed=8508925; DOI=10.1016/0014-5793(93)81398-j;
RA   Amerik A.Y., Yarovoi S.V., Grigorenko V.G., Antonov V.K.;
RT   "Identification, sequence analysis, and characterization of cDNA clones
RT   encoding two granzyme-like serine proteinases from rat duodenum.";
RL   FEBS Lett. 324:226-230(1993).
CC   -!- FUNCTION: This enzyme is necessary for target cell lysis in cell-
CC       mediated immune responses.
CC   -!- TISSUE SPECIFICITY: Duodenum, lung and spleen.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; X68657; CAA48624.1; -; mRNA.
DR   PIR; S33756; S33756.
DR   RefSeq; NP_058842.1; NM_017146.1.
DR   RefSeq; NP_067609.1; NM_021598.2.
DR   AlphaFoldDB; Q06606; -.
DR   SMR; Q06606; -.
DR   STRING; 10116.ENSRNOP00000066083; -.
DR   MEROPS; S01.008; -.
DR   GlyGen; Q06606; 2 sites.
DR   PaxDb; Q06606; -.
DR   PRIDE; Q06606; -.
DR   Ensembl; ENSRNOT00000099690; ENSRNOP00000097551; ENSRNOG00000063482.
DR   GeneID; 29269; -.
DR   GeneID; 54269; -.
DR   UCSC; RGD:3063; rat.
DR   CTD; 17231; -.
DR   CTD; 54269; -.
DR   RGD; 3063; Mcpt10.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT01030000234551; -.
DR   InParanoid; Q06606; -.
DR   PhylomeDB; Q06606; -.
DR   TreeFam; TF333630; -.
DR   BRENDA; 3.4.21.B3; 5301.
DR   PRO; PR:Q06606; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; 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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..20
FT                   /note="Activation peptide"
FT                   /id="PRO_0000027429"
FT   CHAIN           21..248
FT                   /note="Granzyme-like protein 2"
FT                   /id="PRO_0000027430"
FT   DOMAIN          21..243
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        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        201
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        142..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   248 AA;  27463 MW;  6F362AFAE0E3D76F CRC64;
     MFLFLFFLVA ILPVNTEGGE IIWGTESKPH SRPYMAFIKF YDSNSEPHHC GGFLVAKDIV
     MTAAHCNGRN IKVTLGAHNI KKQENTQVIS VVKAKPHENY DRDSHFNDIM LLKLERKAQL
     NGVVKTIALP RSQDWVKPGQ VCTVAGWGRL ANCTSSNTLQ EVNLEVQKGQ KCQDMSEDYN
     DSIQLCVGNP SEGKATGKGD SGGPFVCDGV AQGIVSYRLC TGTLPRVFTR ISSFIPWIQK
     TMKVLQQS