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Granzyme F (EC 3.4.21.-) (C134) (CTL serine protease 3) (Cytotoxic cell protease 4) (CCP4) (Cytotoxic serine protease 3) (MCSP3)

 GRAF_MOUSE              Reviewed;         248 AA.
P08883;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
05-JUL-2017, entry version 154.
RecName: Full=Granzyme F;
EC=3.4.21.-;
AltName: Full=C134;
AltName: Full=CTL serine protease 3;
AltName: Full=Cytotoxic cell protease 4;
Short=CCP4;
AltName: Full=Cytotoxic serine protease 3;
AltName: Full=MCSP3;
Flags: Precursor;
Name=Gzmf; Synonyms=Ccp4, Ctla-7, Ctla7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Spleen;
PubMed=1861068;
Jenne D.E., Zimmer M., Garcia-Sanz J.A., Tschopp J.F., Lichter P.;
"Genomic organization and subchromosomal in situ localization of the
murine granzyme F, a serine protease expressed in CD8+ T cells.";
J. Immunol. 147:1045-1052(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1880801; DOI=10.1016/0022-2836(91)90359-E;
Prendergast J.A., Pinkoski M., Wolfenden A., Bleackley R.C.;
"Structure and evolution of the cytotoxic cell proteinase genes CCP3,
CCP4 and CCP5.";
J. Mol. Biol. 220:867-875(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3292281; DOI=10.1016/0014-5793(88)81323-1;
Bleackley R.C., Duggan B., Ehrman N., Lobe C.G.;
"Isolation of two cDNA sequences which encode cytotoxic cell
proteases.";
FEBS Lett. 234:153-159(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3260382; DOI=10.1073/pnas.85.13.4814;
Jenne D.E., Rey C., Haefliger J.-A., Qiao B.-Y., Groscurth P.,
Tschopp J.;
"Identification and sequencing of cDNA clones encoding the granule-
associated serine proteases granzymes D, E, and F of cytolytic T
lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 85:4814-4818(1988).
[5]
NUCLEOTIDE SEQUENCE.
TISSUE=Cytotoxic T-cell;
PubMed=3053963; DOI=10.1084/jem.168.5.1839;
Kwon B.S., Kestler D., Lee E., Wakulchik M., Young J.D.-E.;
"Isolation and sequence analysis of serine protease cDNAs from mouse
cytolytic T lymphocytes.";
J. Exp. Med. 168:1839-1854(1988).
[6]
PROTEIN SEQUENCE OF 21-40.
PubMed=3555842; DOI=10.1016/0092-8674(87)90544-7;
Masson D., Tschopp J.;
"A family of serine esterases in lytic granules of cytolytic T
lymphocytes.";
Cell 49:679-685(1987).
[7]
PROTEIN SEQUENCE OF 21-45.
PubMed=2152187; DOI=10.1016/1046-5928(90)90049-5;
Jiang S., Hasselkus-Light C.S., Ojcius D.M., Young J.D.-E.;
"Purification of a membrane-associated serine esterase from murine
cytotoxic T lymphocytes by a single reverse-phase column.";
Protein Expr. Purif. 1:77-80(1990).
-!- FUNCTION: This enzyme is probably necessary for target cell lysis
in cell-mediated immune responses.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic
granules of cytolytic T-lymphocytes.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M36902; AAA37488.1; -; mRNA.
EMBL; X56989; CAA40307.1; -; Genomic_DNA.
EMBL; M96930; AAA37741.1; -; Genomic_DNA.
EMBL; J03257; AAA37738.1; -; mRNA.
EMBL; X12823; CAA31310.1; -; mRNA.
EMBL; X14094; CAA32256.1; -; mRNA.
CCDS; CCDS36936.1; -.
PIR; S24940; S01007.
RefSeq; NP_034504.1; NM_010374.3.
UniGene; Mm.457976; -.
ProteinModelPortal; P08883; -.
SMR; P08883; -.
BioGrid; 200139; 1.
IntAct; P08883; 1.
MINT; MINT-4096717; -.
STRING; 10090.ENSMUSP00000022757; -.
MEROPS; S01.401; -.
iPTMnet; P08883; -.
PhosphoSitePlus; P08883; -.
PaxDb; P08883; -.
PeptideAtlas; P08883; -.
PRIDE; P08883; -.
Ensembl; ENSMUST00000022757; ENSMUSP00000022757; ENSMUSG00000015441.
GeneID; 14943; -.
KEGG; mmu:14943; -.
UCSC; uc007ubs.1; mouse.
CTD; 14943; -.
MGI; MGI:109254; Gzmf.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P08883; -.
OMA; SANMECA; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P08883; -.
TreeFam; TF333630; -.
Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
ChiTaRS; Gzmf; mouse.
PRO; PR:P08883; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000015441; -.
CleanEx; MM_GZMF; -.
ExpressionAtlas; P08883; baseline and differential.
Genevisible; P08883; MM.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Cytolysis; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
Serine protease; Signal; Zymogen.
SIGNAL 1 18
PROPEP 19 20 {ECO:0000269|PubMed:2152187,
ECO:0000269|PubMed:3555842}.
/FTId=PRO_0000027409.
CHAIN 21 248 Granzyme F.
/FTId=PRO_0000027410.
DOMAIN 21 246 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system. {ECO:0000250}.
ACT_SITE 109 109 Charge relay system. {ECO:0000250}.
ACT_SITE 204 204 Charge relay system. {ECO:0000250}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 143 210 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 175 189 {ECO:0000255|PROSITE-ProRule:PRU00274}.
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


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