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   27-MAR-2024, entry version 169.
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; 10090-ENSMUSP00000015585; -.
DR   PeptideAtlas; P08882; -.
DR   ProteomicsDB; 271287; -.
DR   DNASU; 14940; -.
DR   Ensembl; ENSMUST00000015585.4; ENSMUSP00000015585.3; ENSMUSG00000079186.4.
DR   GeneID; 14940; -.
DR   KEGG; mmu:14940; -.
DR   UCSC; uc007ubu.2; mouse.
DR   AGR; MGI:109256; -.
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; QNDEECE; -.
DR   OrthoDB; 2540265at2759; -.
DR   PhylomeDB; P08882; -.
DR   TreeFam; TF333630; -.
DR   BioGRID-ORCS; 14940; 1 hit in 78 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 46 other cell types or tissues.
DR   ExpressionAtlas; P08882; baseline and differential.
DR   GO; GO:0044194; C:cytolytic granule; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24271:SF43; GRANZYME C; 1.
DR   PANTHER; PTHR24271; KALLIKREIN-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   Genevisible; P08882; MM.
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
//