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Granzyme B(G,H) (EC 3.4.21.79) (CTLA-1) (Cytotoxic cell protease 1) (CCP1) (Fragmentin-2)

 GRAB_MOUSE              Reviewed;         247 AA.
P04187;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
28-FEB-2018, entry version 179.
RecName: Full=Granzyme B(G,H);
EC=3.4.21.79;
AltName: Full=CTLA-1;
AltName: Full=Cytotoxic cell protease 1;
Short=CCP1;
AltName: Full=Fragmentin-2;
Flags: Precursor;
Name=Gzmb; Synonyms=Ctla-1, Ctla1;
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].
PubMed=3518058; DOI=10.1126/science.3518058;
Lobe C.G., Finlay B.B., Paranchych W., Paetkau V.H., Bleackley R.C.;
"Novel serine proteases encoded by two cytotoxic T lymphocyte-specific
genes.";
Science 232:858-861(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3264185; DOI=10.1021/bi00418a040;
Lobe C.G., Upton C., Duggan B., Ehrman N., Letellier M., Bell J.,
McFadden G., Bleackley R.C.;
"Organization of two genes encoding cytotoxic T lymphocyte-specific
serine proteases CCPI and CCPII.";
Biochemistry 27:6941-6946(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3090449; DOI=10.1038/322268a0;
Brunet J.-F., Dosseto M., Denizot F., Mattei M.-G., Clark W.R.,
Haqqi T.M., Ferrier P., Nabholz M., Schmitt-Verhulst A.-M.,
Luciani M.-F., Golstein P.;
"The inducible cytotoxic T-lymphocyte-associated gene transcript CTLA-
1 sequence and gene localization to mouse chromosome 14.";
Nature 322:268-271(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE OF 227-247.
STRAIN=C57BL/6J;
PubMed=8043949; DOI=10.1007/BF00356553;
Ko M.S., Wang X., Horton J.H., Hagen M.D., Takahashi N., Maezaki Y.,
Nadeau J.H.;
"Genetic mapping of 40 cDNA clones on the mouse genome by PCR.";
Mamm. Genome 5:349-355(1994).
[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]
3D-STRUCTURE MODELING.
PubMed=3237717; DOI=10.1002/prot.340040306;
Murphy M.E.P., Moult J., Bleackley R.C., Gershenfeld H.,
Weissman I.L., James M.N.G.;
"Comparative molecular model building of two serine proteinases from
cytotoxic T lymphocytes.";
Proteins 4:190-204(1988).
-!- FUNCTION: This enzyme is necessary for target cell lysis in cell-
mediated immune responses. It cleaves after Asp. Seems to be
linked to an activation cascade of caspases (aspartate-specific
cysteine proteases) responsible for apoptosis execution. Cleaves
caspase-3, -7, -9 and 10 to give rise to active enzymes mediating
apoptosis (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-
Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic
granules of cytolytic T-lymphocytes and natural killer cells.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; X04072; CAA27715.1; -; mRNA.
EMBL; M12302; AAA37383.1; -; mRNA.
EMBL; M22526; AAB61756.1; -; Genomic_DNA.
EMBL; BC002085; AAH02085.1; -; mRNA.
EMBL; U05707; AAB60470.1; -; Genomic_DNA.
CCDS; CCDS27147.1; -.
PIR; A94288; PRMSCL.
RefSeq; NP_038570.1; NM_013542.3.
UniGene; Mm.14874; -.
PDB; 2CP1; Model; -; A=21-247.
PDBsum; 2CP1; -.
ProteinModelPortal; P04187; -.
SMR; P04187; -.
BioGrid; 200135; 6.
IntAct; P04187; 1.
MINT; P04187; -.
STRING; 10090.ENSMUSP00000015581; -.
MEROPS; S01.136; -.
iPTMnet; P04187; -.
PhosphoSitePlus; P04187; -.
EPD; P04187; -.
PaxDb; P04187; -.
PeptideAtlas; P04187; -.
PRIDE; P04187; -.
Ensembl; ENSMUST00000015581; ENSMUSP00000015581; ENSMUSG00000015437.
GeneID; 14939; -.
KEGG; mmu:14939; -.
UCSC; uc007ubv.1; mouse.
CTD; 3002; -.
MGI; MGI:109267; Gzmb.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P04187; -.
KO; K01353; -.
OMA; CVGDPEI; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P04187; -.
TreeFam; TF333630; -.
Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
PRO; PR:P04187; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000015437; -.
CleanEx; MM_GZMB; -.
ExpressionAtlas; P04187; baseline and differential.
Genevisible; P04187; MM.
GO; GO:0044194; C:cytolytic granule; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008236; F:serine-type peptidase activity; IDA:MGI.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; IDA:MGI.
GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:InterPro.
GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR037553; Granzyme_B.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR24271:SF41; PTHR24271:SF41; 1.
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;
3D-structure; Apoptosis; 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:3555842}.
/FTId=PRO_0000027401.
CHAIN 21 247 Granzyme B(G,H).
/FTId=PRO_0000027402.
DOMAIN 21 245 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 64 64 Charge relay system. {ECO:0000250}.
ACT_SITE 108 108 Charge relay system. {ECO:0000250}.
ACT_SITE 203 203 Charge relay system. {ECO:0000250}.
SITE 228 228 Mediates preference for Asp-containing
substrates. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 65 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 142 209 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 173 188 {ECO:0000255|PROSITE-ProRule:PRU00274}.
SEQUENCE 247 AA; 27470 MW; 996BCD199965C6D6 CRC64;
MKILLLLLTL SLASRTKAGE IIGGHEVKPH SRPYMALLSI KDQQPEAICG GFLIREDFVL
TAAHCEGSII NVTLGAHNIK EQEKTQQVIP MVKCIPHPDY NPKTFSNDIM LLKLKSKAKR
TRAVRPLNLP RRNVNVKPGD VCYVAGWGRM APMGKYSNTL QEVELTVQKD RECESYFKNR
YNKTNQICAG DPKTKRASFR GDSGGPLVCK KVAAGIVSYG YKDGSPPRAF TKVSSFLSWI
KKTMKSS


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