GRAC_MOUSE
ID GRAC_MOUSE Reviewed; 248 AA.
AC P08882; Q61389;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Granzyme C;
DE EC=3.4.21.-;
DE AltName: Full=B10;
DE AltName: Full=Cytotoxic cell protease 2;
DE Short=CCP2;
DE Flags: Precursor;
GN Name=Gzmc; Synonyms=Ctla-5, Ctla5;
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 [GENOMIC DNA].
RX PubMed=3264185; DOI=10.1021/bi00418a040;
RA Lobe C.G., Upton C., Duggan B., Ehrman N., Letellier M., Bell J.,
RA McFadden G., Bleackley R.C.;
RT "Organization of two genes encoding cytotoxic T lymphocyte-specific serine
RT proteases CCPI and CCPII.";
RL Biochemistry 27:6941-6946(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3257230;
RA Jenne D.E., Rey C., Masson D., Stanley K.K., Herz J., Plaetinck G.,
RA Tschopp J.;
RT "cDNA cloning of granzyme C, a granule-associated serine protease of
RT cytolytic T lymphocytes.";
RL J. Immunol. 140:318-323(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 159-248.
RX PubMed=3518058; DOI=10.1126/science.3518058;
RA Lobe C.G., Finlay B.B., Paranchych W., Paetkau V.H., Bleackley R.C.;
RT "Novel serine proteases encoded by two cytotoxic T lymphocyte-specific
RT genes.";
RL Science 232:858-861(1986).
RN [5]
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; M22527; AAA85454.1; -; Genomic_DNA.
DR EMBL; X12822; CAA31309.1; -; mRNA.
DR EMBL; M18459; AAA37734.1; -; mRNA.
DR EMBL; M12301; AAA37384.1; -; mRNA.
DR CCDS; CCDS27146.1; -.
DR PIR; B28952; PRMSC2.
DR RefSeq; NP_034501.2; NM_010371.3.
DR RefSeq; XP_011243265.1; XM_011244963.2.
DR PDB; 3FZZ; X-ray; 2.50 A; A/B=21-247.
DR PDB; 3G01; X-ray; 2.50 A; A/B=21-247.
DR PDBsum; 3FZZ; -.
DR PDBsum; 3G01; -.
DR AlphaFoldDB; P08882; -.
DR SMR; P08882; -.
DR STRING; 10090.ENSMUSP00000015585; -.
DR MEROPS; S01.137; -.
DR iPTMnet; P08882; -.
DR PhosphoSitePlus; P08882; -.
DR EPD; P08882; -.
DR PaxDb; P08882; -.
DR PeptideAtlas; P08882; -.
DR PRIDE; P08882; -.
DR ProteomicsDB; 271287; -.
DR DNASU; 14940; -.
DR Ensembl; ENSMUST00000015585; ENSMUSP00000015585; ENSMUSG00000079186.
DR GeneID; 14940; -.
DR KEGG; mmu:14940; -.
DR UCSC; uc007ubu.2; mouse.
DR CTD; 14940; -.
DR MGI; MGI:109256; Gzmc.
DR VEuPathDB; HostDB:ENSMUSG00000079186; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P08882; -.
DR OMA; CWGRLMN; -.
DR OrthoDB; 1076876at2759; -.
DR PhylomeDB; P08882; -.
DR TreeFam; TF333630; -.
DR BioGRID-ORCS; 14940; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gzmc; mouse.
DR EvolutionaryTrace; P08882; -.
DR PRO; PR:P08882; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P08882; protein.
DR Bgee; ENSMUSG00000079186; Expressed in gastrula and 45 other tissues.
DR ExpressionAtlas; P08882; baseline and differential.
DR Genevisible; P08882; 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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
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_0000027403"
FT CHAIN 21..248
FT /note="Granzyme C"
FT /id="PRO_0000027404"
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 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"
FT CONFLICT 69
FT /note="S -> R (in Ref. 3; AAA37734)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> F (in Ref. 4; AAA37384)"
FT /evidence="ECO:0000305"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3FZZ"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3FZZ"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:3FZZ"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3FZZ"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3FZZ"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3FZZ"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3G01"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:3FZZ"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3FZZ"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:3FZZ"
SQ SEQUENCE 248 AA; 27311 MW; AA6247655EC52289 CRC64;
MPPVLILLTL LLPLRAGAEE IIGGNEISPH SRPYMAYYEF LKVGGKKMFC GGFLVRDKFV
LTAAHCKGSS MTVTLGAHNI KAKEETQQII PVAKAIPHPD YNPDDRSNDI MLLKLVRNAK
RTRAVRPLNL PRRNAHVKPG DECYVAGWGK VTPDGEFPKT LHEVKLTVQK DQVCESQFQS
SYNRANEICV GDSKIKGASF EEDSGGPLVC KRAAAGIVSY GQTDGSAPQV FTRVLSFVSW
IKKTMKHS
