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Granzyme G (EC 3.4.21.-) (CTL serine protease 1) (MCSP-1)

 GRAG_MOUSE              Reviewed;         248 AA.
P13366; P97388;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
05-JUL-2017, entry version 137.
RecName: Full=Granzyme G;
EC=3.4.21.-;
AltName: Full=CTL serine protease 1;
AltName: Full=MCSP-1;
Flags: Precursor;
Name=Gzmg;
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 [MRNA], AND PROTEIN SEQUENCE OF 21-48.
PubMed=2611223; DOI=10.1021/bi00445a060;
Jenne D.E., Masson D., Zimmer M., Haefliger J.-A., Li W.-H.,
Tschopp J.;
"Isolation and complete structure of the lymphocyte serine protease
granzyme G, a novel member of the granzyme multigene family in murine
cytolytic T lymphocytes. Evolutionary origin of lymphocyte
proteases.";
Biochemistry 28:7953-7961(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=8917549; DOI=10.1073/pnas.93.23.13090;
Pham C.T.N., MacIvor D.M., Hug B.A., Heusel J.W., Ley T.J.;
"Long-range disruption of gene expression by a selectable marker
cassette.";
Proc. Natl. Acad. Sci. U.S.A. 93:13090-13095(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 51-248.
TISSUE=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).
-!- 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; M36900; AAA37486.1; -; mRNA.
EMBL; U66473; AAB19191.1; -; Genomic_DNA.
EMBL; J02872; AAA37731.1; -; mRNA.
EMBL; X14092; CAA32254.1; -; mRNA.
CCDS; CCDS27144.1; -.
PIR; A33412; A33412.
PIR; S06176; S06176.
RefSeq; NP_034505.1; NM_010375.2.
UniGene; Mm.14868; -.
ProteinModelPortal; P13366; -.
SMR; P13366; -.
IntAct; P13366; 1.
MINT; MINT-4096735; -.
STRING; 10090.ENSMUSP00000015578; -.
MEROPS; S01.402; -.
EPD; P13366; -.
PaxDb; P13366; -.
PeptideAtlas; P13366; -.
PRIDE; P13366; -.
Ensembl; ENSMUST00000015578; ENSMUSP00000015578; ENSMUSG00000040284.
GeneID; 14944; -.
KEGG; mmu:14944; -.
UCSC; uc007ubq.1; mouse.
CTD; 14944; -.
MGI; MGI:109253; Gzmg.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P13366; -.
OMA; NDSKCEN; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P13366; -.
TreeFam; TF333630; -.
Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
PRO; PR:P13366; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000040284; -.
CleanEx; MM_GZMG; -.
ExpressionAtlas; P13366; baseline and differential.
Genevisible; P13366; 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 Activation peptide.
{ECO:0000269|PubMed:2611223}.
/FTId=PRO_0000027411.
CHAIN 21 248 Granzyme G.
/FTId=PRO_0000027412.
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 68 68 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}.
CONFLICT 60 60 V -> G (in Ref. 3; AAA37486/CAA32254).
{ECO:0000305}.
CONFLICT 207 207 P -> T (in Ref. 3; AAA37486/CAA32254).
{ECO:0000305}.
CONFLICT 224 224 R -> K (in Ref. 2; AAB19191).
{ECO:0000305}.
SEQUENCE 248 AA; 27381 MW; EAF4A438EABF04AF CRC64;
MPPILILLTL LLPLRAGAEE IIGGHEVKPH SRPYMAFIKS VDIEGKKKYC GGFLVQDDFV
LTAAHCRNRS MTVTLGAHNI KAKEETQQII PVAKAIPHPA FNRKHGTNDI MLLKLESKAK
RTKAVRPLKL PRPNARVKPG DVCSVAGWGK TSINATKASA RLREAQLIIQ EDEECKKLWY
TYSKTTQICA GDPKKVQAPY EGESGGPLVC DNLAYGVVSY GINRTITPGV FTKVVHFLPW
ISTNMKLL


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