GRAF_MOUSE
ID GRAF_MOUSE Reviewed; 248 AA.
AC P08883;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Granzyme F;
DE EC=3.4.21.-;
DE AltName: Full=C134;
DE AltName: Full=CTL serine protease 3;
DE AltName: Full=Cytotoxic cell protease 4;
DE Short=CCP4;
DE AltName: Full=Cytotoxic serine protease 3;
DE AltName: Full=MCSP3;
DE Flags: Precursor;
GN Name=Gzmf; Synonyms=Ccp4, Ctla-7, Ctla7;
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 [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=1861068;
RA Jenne D.E., Zimmer M., Garcia-Sanz J.A., Tschopp J.F., Lichter P.;
RT "Genomic organization and subchromosomal in situ localization of the murine
RT granzyme F, a serine protease expressed in CD8+ T cells.";
RL J. Immunol. 147:1045-1052(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1880801; DOI=10.1016/0022-2836(91)90359-e;
RA Prendergast J.A., Pinkoski M., Wolfenden A., Bleackley R.C.;
RT "Structure and evolution of the cytotoxic cell proteinase genes CCP3, CCP4
RT and CCP5.";
RL J. Mol. Biol. 220:867-875(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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.
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).
RN [7]
RP PROTEIN SEQUENCE OF 21-45.
RX PubMed=2152187; DOI=10.1016/1046-5928(90)90049-5;
RA Jiang S., Hasselkus-Light C.S., Ojcius D.M., Young J.D.-E.;
RT "Purification of a membrane-associated serine esterase from murine
RT cytotoxic T lymphocytes by a single reverse-phase column.";
RL Protein Expr. Purif. 1:77-80(1990).
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; M36902; AAA37488.1; -; mRNA.
DR EMBL; X56989; CAA40307.1; -; Genomic_DNA.
DR EMBL; M96930; AAA37741.1; -; Genomic_DNA.
DR EMBL; J03257; AAA37738.1; -; mRNA.
DR EMBL; X12823; CAA31310.1; -; mRNA.
DR EMBL; X14094; CAA32256.1; -; mRNA.
DR CCDS; CCDS36936.1; -.
DR PIR; S24940; S01007.
DR RefSeq; NP_034504.1; NM_010374.3.
DR AlphaFoldDB; P08883; -.
DR SMR; P08883; -.
DR BioGRID; 200139; 1.
DR STRING; 10090.ENSMUSP00000022757; -.
DR MEROPS; S01.401; -.
DR GlyGen; P08883; 3 sites.
DR iPTMnet; P08883; -.
DR PhosphoSitePlus; P08883; -.
DR PaxDb; P08883; -.
DR PeptideAtlas; P08883; -.
DR PRIDE; P08883; -.
DR DNASU; 14943; -.
DR Ensembl; ENSMUST00000022757; ENSMUSP00000022757; ENSMUSG00000015441.
DR GeneID; 14943; -.
DR KEGG; mmu:14943; -.
DR UCSC; uc007ubs.1; mouse.
DR CTD; 14943; -.
DR MGI; MGI:109254; Gzmf.
DR VEuPathDB; HostDB:ENSMUSG00000015441; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P08883; -.
DR OMA; WGRTSIN; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P08883; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 14943; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gzmf; mouse.
DR PRO; PR:P08883; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P08883; protein.
DR Bgee; ENSMUSG00000015441; Expressed in gastrula and 11 other tissues.
DR ExpressionAtlas; P08883; baseline and differential.
DR Genevisible; P08883; 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:2152187,
FT ECO:0000269|PubMed:3555842"
FT /id="PRO_0000027409"
FT CHAIN 21..248
FT /note="Granzyme F"
FT /id="PRO_0000027410"
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 106
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"
SQ SEQUENCE 248 AA; 27642 MW; 02B4BB67F100DC38 CRC64;
MPPILILLTL LLPLRAGAEE IIGGHEVKPH SRPYMARVRF VKDNGKRHSC GGFLVQDYFV
LTAAHCTGSS MRVILGAHNI RAKEETQQII PVAKAIPHPA YDDKDNTSDI MLLKLESKAK
RTKAVRPLKL PRPNARVKPG HVCSVAGWGR TSINATQRSS CLREAQLIIQ KDKECKKYFY
KYFKTMQICA GDPKKIQSTY SGDSGGPLVC NNKAYGVLTY GLNRTIGPGV FTKVVHYLPW
ISRNMKLL
