ID   GRZ1_RAT                Reviewed;         248 AA.
AC   Q06605;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Granzyme-like protein 1;
DE            EC=3.4.21.-;
DE   AltName: Full=GLP I;
DE   AltName: Full=Granzyme-like protein I;
DE            Short=GLP-1;
DE   Flags: Precursor;
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.
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; X66693; CAA47235.1; -; mRNA.
DR   PIR; S33755; S33755.
DR   RefSeq; NP_001316820.1; NM_001329891.1.
DR   AlphaFoldDB; Q06605; -.
DR   SMR; Q06605; -.
DR   STRING; 10116.ENSRNOP00000029828; -.
DR   MEROPS; S01.097; -.
DR   GlyGen; Q06605; 1 site.
DR   PRIDE; Q06605; -.
DR   GeneID; 102553861; -.
DR   UCSC; RGD:2320097; rat.
DR   eggNOG; KOG3627; Eukaryota.
DR   OrthoDB; 1076876at2759; -.
DR   PhylomeDB; Q06605; -.
DR   BRENDA; 3.4.21.B3; 5301.
DR   PRO; PR:Q06605; -.
DR   Proteomes; UP000002494; Unplaced.
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_0000027427"
FT   CHAIN           21..248
FT                   /note="Granzyme-like protein 1"
FT                   /id="PRO_0000027428"
FT   DOMAIN          21..246
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        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        174..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   248 AA;  27236 MW;  036C81B43A88F972 CRC64;
     MNLLLLLLTV SLAPTTEAAE IIGGHEADPH SRPYMAYLQY KNEDSRDTIC GGFLIREDFV
     LTAAHCSGSK INVTLGAHNI KEQEKTQQVI PVVKIIPHPA YNAKTISNDI MLLKLKSKAK
     RTRAVKTLSL PRSNFKVKPG DVCYVAGWGK LGPMGKFPDK LQEVELTVQE DQECETYLKN
     AYDKANQICA GDPKIKCASF QGDSGGPLVC KKVAAGIVSY GRKDGSTPRA FTKVSTFLSW
     IEETMKKS