GRAG_MOUSE
ID GRAG_MOUSE Reviewed; 248 AA.
AC P13366; P97388;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Granzyme G;
DE EC=3.4.21.-;
DE AltName: Full=CTL serine protease 1;
DE AltName: Full=MCSP-1;
DE Flags: Precursor;
GN Name=Gzmg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-48.
RX PubMed=2611223; DOI=10.1021/bi00445a060;
RA Jenne D.E., Masson D., Zimmer M., Haefliger J.-A., Li W.-H., Tschopp J.;
RT "Isolation and complete structure of the lymphocyte serine protease
RT granzyme G, a novel member of the granzyme multigene family in murine
RT cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases.";
RL Biochemistry 28:7953-7961(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=8917549; DOI=10.1073/pnas.93.23.13090;
RA Pham C.T.N., MacIvor D.M., Hug B.A., Heusel J.W., Ley T.J.;
RT "Long-range disruption of gene expression by a selectable marker
RT cassette.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13090-13095(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-248.
RC TISSUE=T-cell;
RX PubMed=3053963; DOI=10.1084/jem.168.5.1839;
RA Kwon B.S., Kestler D., Lee E., Wakulchik M., Young J.D.-E.;
RT "Isolation and sequence analysis of serine protease cDNAs from mouse
RT cytolytic T lymphocytes.";
RL J. Exp. Med. 168:1839-1854(1988).
CC -!- FUNCTION: This enzyme is probably necessary for target cell lysis in
CC cell-mediated immune responses.
CC -!- SUBCELLULAR LOCATION: Cytolytic granule.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; M36900; AAA37486.1; -; mRNA.
DR EMBL; U66473; AAB19191.1; -; Genomic_DNA.
DR EMBL; J02872; AAA37731.1; -; mRNA.
DR EMBL; X14092; CAA32254.1; -; mRNA.
DR CCDS; CCDS27144.1; -.
DR PIR; A33412; A33412.
DR PIR; S06176; S06176.
DR RefSeq; NP_034505.1; NM_010375.2.
DR AlphaFoldDB; P13366; -.
DR SMR; P13366; -.
DR BioGRID; 200140; 4.
DR STRING; 10090.ENSMUSP00000015578; -.
DR MEROPS; S01.402; -.
DR GlyGen; P13366; 3 sites.
DR EPD; P13366; -.
DR PaxDb; P13366; -.
DR PeptideAtlas; P13366; -.
DR PRIDE; P13366; -.
DR ProteomicsDB; 271323; -.
DR DNASU; 14944; -.
DR Ensembl; ENSMUST00000015578; ENSMUSP00000015578; ENSMUSG00000040284.
DR GeneID; 14944; -.
DR KEGG; mmu:14944; -.
DR UCSC; uc007ubq.1; mouse.
DR CTD; 14944; -.
DR MGI; MGI:109253; Gzmg.
DR VEuPathDB; HostDB:ENSMUSG00000040284; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P13366; -.
DR OMA; EDQECEK; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P13366; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 14944; 3 hits in 73 CRISPR screens.
DR PRO; PR:P13366; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P13366; protein.
DR Bgee; ENSMUSG00000040284; Expressed in gastrula and 28 other tissues.
DR ExpressionAtlas; P13366; baseline and differential.
DR Genevisible; P13366; MM.
DR GO; GO:0044194; C:cytolytic granule; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0140507; P:granzyme-mediated programmed cell death signaling pathway; ISO:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; ISO:MGI.
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 Cytolysis; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Protease; Reference proteome; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT PROPEP 19..20
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2611223"
FT /id="PRO_0000027411"
FT CHAIN 21..248
FT /note="Granzyme G"
FT /id="PRO_0000027412"
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 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
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 175..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CONFLICT 60
FT /note="V -> G (in Ref. 3; AAA37486/CAA32254)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="P -> T (in Ref. 3; AAA37486/CAA32254)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> K (in Ref. 2; AAB19191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27381 MW; EAF4A438EABF04AF CRC64;
MPPILILLTL LLPLRAGAEE IIGGHEVKPH SRPYMAFIKS VDIEGKKKYC GGFLVQDDFV
LTAAHCRNRS MTVTLGAHNI KAKEETQQII PVAKAIPHPA FNRKHGTNDI MLLKLESKAK
RTKAVRPLKL PRPNARVKPG DVCSVAGWGK TSINATKASA RLREAQLIIQ EDEECKKLWY
TYSKTTQICA GDPKKVQAPY EGESGGPLVC DNLAYGVVSY GINRTITPGV FTKVVHFLPW
ISTNMKLL
