GRAE_MOUSE
ID GRAE_MOUSE Reviewed; 248 AA.
AC P08884; P97389;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Granzyme E;
DE EC=3.4.21.-;
DE AltName: Full=CTL serine protease 2;
DE AltName: Full=Cytotoxic cell protease 3;
DE Short=CCP3;
DE AltName: Full=Cytotoxic serine protease 2;
DE AltName: Full=D12;
DE AltName: Full=MCSP2;
DE Flags: Precursor;
GN Name=Gzme; Synonyms=Ccp3, Ctla-6, Ctla6;
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].
RX PubMed=3292281; DOI=10.1016/0014-5793(88)81323-1;
RA Bleackley R.C., Duggan B., Ehrman N., Lobe C.G.;
RT "Isolation of two cDNA sequences which encode cytotoxic cell proteases.";
RL FEBS Lett. 234:153-159(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Prendergast J.A., Pinkoski M., Wolfenden A., Bleackley R.C.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-248.
RX PubMed=3260382; DOI=10.1073/pnas.85.13.4814;
RA Jenne D.E., Rey C., Haefliger J.-A., Qiao B.-Y., Groscurth P., Tschopp J.;
RT "Identification and sequencing of cDNA clones encoding the granule-
RT associated serine proteases granzymes D, E, and F of cytolytic T
RT lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4814-4818(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-248.
RC TISSUE=Cytotoxic 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).
RN [6]
RP PROTEIN SEQUENCE OF 21-40.
RX PubMed=3555842; DOI=10.1016/0092-8674(87)90544-7;
RA Masson D., Tschopp J.;
RT "A family of serine esterases in lytic granules of cytolytic T
RT lymphocytes.";
RL Cell 49:679-685(1987).
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; M36901; AAA37487.1; -; mRNA.
DR EMBL; X12821; CAA31308.1; -; mRNA.
DR EMBL; U66474; AAB19192.1; -; Genomic_DNA.
DR EMBL; X56988; CAA40306.1; -; Genomic_DNA.
DR EMBL; J03256; AAA37737.1; -; mRNA.
DR EMBL; X14093; CAA32255.1; -; mRNA.
DR CCDS; CCDS27143.1; -.
DR PIR; S01006; S01006.
DR RefSeq; NP_034503.2; NM_010373.3.
DR AlphaFoldDB; P08884; -.
DR SMR; P08884; -.
DR STRING; 10090.ENSMUSP00000086978; -.
DR MEROPS; S01.399; -.
DR GlyGen; P08884; 4 sites.
DR EPD; P08884; -.
DR PaxDb; P08884; -.
DR PeptideAtlas; P08884; -.
DR PRIDE; P08884; -.
DR DNASU; 14942; -.
DR Ensembl; ENSMUST00000089549; ENSMUSP00000086978; ENSMUSG00000022156.
DR GeneID; 14942; -.
DR KEGG; mmu:14942; -.
DR UCSC; uc007ubo.1; mouse.
DR CTD; 14942; -.
DR MGI; MGI:109265; Gzme.
DR VEuPathDB; HostDB:ENSMUSG00000022156; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P08884; -.
DR OMA; GWAKMES; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P08884; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 14942; 2 hits in 71 CRISPR screens.
DR PRO; PR:P08884; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P08884; protein.
DR Bgee; ENSMUSG00000022156; Expressed in gastrula and 25 other tissues.
DR Genevisible; P08884; 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 /evidence="ECO:0000269|PubMed:3555842"
FT /id="PRO_0000027407"
FT CHAIN 21..248
FT /note="Granzyme E"
FT /id="PRO_0000027408"
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 102
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 5
FT /note="L -> P (in Ref. 3; AAB19192)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="R -> K (in Ref. 5; AAA37487/CAA32255)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="S -> P (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27494 MW; 3A31912A45E93D3F CRC64;
MPPVLILLTL LLPLGAGAEE IIGGHVVKPH SRPYMAFVKS VDIEGNRRYC GGFLVQDDFV
LTAAHCRNRT MTVTLGAHNI KAKEETQQII PVAKAIPHPD YNATAFFSDI MLLKLESKAK
RTKAVRPLKL PRPNARVKPG DVCSVAGWGS RSINDTKASA RLREAQLVIQ EDEECKKRFR
HYTETTEICA GDLKKIKTPF KGDSGGPLVC DNKAYGLLAY AKNRTISSGV FTKIVHFLPW
ISRNMKLL
