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Granzyme B (EC 3.4.21.79) (C11) (CTLA-1) (Cathepsin G-like 1) (CTSGL1) (Cytotoxic T-lymphocyte proteinase 2) (Lymphocyte protease) (Fragmentin-2) (Granzyme-2) (Human lymphocyte protein) (HLP) (SECT) (T-cell serine protease 1-3E)

 GRAB_HUMAN              Reviewed;         247 AA.
P10144; Q8N1D2; Q9UCC1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
05-JUL-2017, entry version 191.
RecName: Full=Granzyme B;
EC=3.4.21.79;
AltName: Full=C11;
AltName: Full=CTLA-1;
AltName: Full=Cathepsin G-like 1;
Short=CTSGL1;
AltName: Full=Cytotoxic T-lymphocyte proteinase 2;
Short=Lymphocyte protease;
AltName: Full=Fragmentin-2;
AltName: Full=Granzyme-2;
AltName: Full=Human lymphocyte protein;
Short=HLP;
AltName: Full=SECT;
AltName: Full=T-cell serine protease 1-3E;
Flags: Precursor;
Name=GZMB; Synonyms=CGL1, CSPB, CTLA1, GRB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-55.
PubMed=2953813;
Schmid J., Weissmann C.;
"Induction of mRNA for a serine protease and a beta-thromboglobulin-
like protein in mitogen-stimulated human leukocytes.";
J. Immunol. 139:250-256(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-94.
PubMed=3258865;
Caputo A., Fahey D., Lloyd C., Vozab R., McCairns E., Rowe P.B.;
"Structure and differential mechanisms of regulation of expression of
a serine esterase gene in activated human T lymphocytes.";
J. Biol. Chem. 263:6363-6369(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-55.
PubMed=3261871; DOI=10.1073/pnas.85.18.6924;
Trapani J.A., Klein J.L., White P.C., Dupont B.;
"Molecular cloning of an inducible serine esterase gene from human
cytotoxic lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 85:6924-6928(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-55.
PubMed=2788607; DOI=10.1016/0888-7543(89)90093-1;
Klein J.L., Shows T.B., Dupont B., Trapani J.A.;
"Genomic organization and chromosomal assignment for a serine protease
gene (CSPB) expressed by human cytotoxic lymphocytes.";
Genomics 5:110-117(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-55.
PubMed=2365998;
Caputo A., Sauer D.E., Rowe P.B.;
"Nucleotide sequence and genomic organization of a human T lymphocyte
serine protease gene.";
J. Immunol. 145:737-744(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-55 AND ALA-94.
PubMed=2332171; DOI=10.1016/0378-1119(90)90311-E;
Haddad P., Clement M.-V., Bernard O., Larsen C.-J., Degos L.,
Sasportes M., Mathieu-Mahul D.;
"Structural organization of the hCTLA-1 gene encoding human granzyme
B.";
Gene 87:265-271(1990).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-55 AND
HIS-247.
TISSUE=Pancreas;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-23.
PubMed=2323780; DOI=10.1007/BF00195821;
Dahl C.A., Bach F.H., Chan W., Huebner K., Russo G., Croce C.M.,
Herfurth T., Cairns J.S.;
"Isolation of a cDNA clone encoding a novel form of granzyme B from
human NK cells and mapping to chromosome 14.";
Hum. Genet. 84:465-470(1990).
[10]
PROTEIN SEQUENCE OF 21-40, AND CHARACTERIZATION.
PubMed=3262682;
Hameed A., Lowrey D.M., Lichtenheld M., Podack E.R.;
"Characterization of three serine esterases isolated from human IL-2
activated killer cells.";
J. Immunol. 141:3142-3147(1988).
[11]
PROTEIN SEQUENCE OF 21-40, AND CHARACTERIZATION.
PubMed=3263427;
Kraehenbuhl O., Rey C., Jenne D.E., Lanzavecchia A., Groscurth P.,
Carrel S., Tschopp J.;
"Characterization of granzymes A and B isolated from granules of
cloned human cytotoxic T lymphocytes.";
J. Immunol. 141:3471-3477(1988).
[12]
PROTEIN SEQUENCE OF 21-39, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
SUBCELLULAR LOCATION.
TISSUE=Lymphocyte;
PubMed=8258716;
Froelich C.J., Zhang X., Turbov J., Hudig D., Winkler U., Hanna W.L.;
"Human granzyme B degrades aggrecan proteoglycan in matrix synthesized
by chondrocytes.";
J. Immunol. 151:7161-7171(1993).
[13]
PROTEIN SEQUENCE OF 21-38.
PubMed=1985927;
Poe M., Blake J.T., Boulton D.A., Gammon M., Sigal N.H., Wu J.K.,
Zweerink H.J.;
"Human cytotoxic lymphocyte granzyme B. Its purification from granules
and the characterization of substrate and inhibitor specificity.";
J. Biol. Chem. 266:98-103(1991).
[14]
PROTEIN SEQUENCE OF 19-33.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[15]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 21-247.
PubMed=11209755; DOI=10.1515/BC.2000.148;
Estebanez-Perpina E., Fuentes-Prior P., Belorgey D., Braun M.,
Kiefersauer R., Maskos K., Huber R., Rubin H., Bode W.;
"Crystal structure of the caspase activator human granzyme B, a
proteinase highly specific for an Asp-P1 residue.";
Biol. Chem. 381:1203-1214(2000).
[16]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-247.
PubMed=11325591; DOI=10.1016/S1074-5521(01)00018-7;
Rotonda J., Garcia-Calvo M., Bull H.G., Geissler W.M., McKeever B.M.,
Willoughby C.A., Thornberry N.A., Becker J.W.;
"The three-dimensional structure of human granzyme B compared to
caspase-3, key mediators of cell death with cleavage specificity for
aspartic acid in P1.";
Chem. Biol. 8:357-368(2001).
[17]
VARIANTS GLN-55 AND HIS-247.
PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
Nakamura Y.;
"Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
nine esterase genes, and two other genes in the Japanese population.";
J. Hum. Genet. 48:249-270(2003).
-!- 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.
-!- CATALYTIC ACTIVITY: Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-
Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-. {ECO:0000269|PubMed:8258716}.
-!- ENZYME REGULATION: Inactivated by the serine protease inhibitor
diisopropylfluorophosphate. {ECO:0000269|PubMed:8258716}.
-!- INTERACTION:
P14222:PRF1; NbExp=3; IntAct=EBI-2505785, EBI-724466;
P10124:SRGN; NbExp=2; IntAct=EBI-2505785, EBI-744915;
-!- SUBCELLULAR LOCATION: Cytoplasmic granule
{ECO:0000269|PubMed:8258716}. Note=Cytoplasmic granules of
cytolytic T-lymphocytes and natural killer cells.
-!- INDUCTION: By staphylococcal enterotoxin A (SEA) in peripheral
blood leukocytes.
-!- SIMILARITY: Belongs to the peptidase S1 family. Granzyme
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M17016; AAA36627.1; -; mRNA.
EMBL; J03189; AAA36603.1; -; mRNA.
EMBL; J04071; AAA52118.1; -; mRNA.
EMBL; J03072; AAB59528.1; -; Genomic_DNA.
EMBL; M38193; AAA67124.1; -; Genomic_DNA.
EMBL; M28879; AAA75490.1; -; Genomic_DNA.
EMBL; AL136018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030195; AAH30195.1; -; mRNA.
CCDS; CCDS9633.1; -.
PIR; A61021; A61021.
RefSeq; NP_004122.2; NM_004131.5.
UniGene; Hs.1051; -.
PDB; 1FQ3; X-ray; 3.10 A; A/B=21-247.
PDB; 1IAU; X-ray; 2.00 A; A=21-247.
PDBsum; 1FQ3; -.
PDBsum; 1IAU; -.
ProteinModelPortal; P10144; -.
SMR; P10144; -.
BioGrid; 109257; 30.
IntAct; P10144; 6.
MINT; MINT-4528791; -.
STRING; 9606.ENSP00000216341; -.
BindingDB; P10144; -.
ChEMBL; CHEMBL2316; -.
GuidetoPHARMACOLOGY; 2369; -.
MEROPS; S01.010; -.
iPTMnet; P10144; -.
PhosphoSitePlus; P10144; -.
BioMuta; GZMB; -.
DMDM; 317373361; -.
PaxDb; P10144; -.
PeptideAtlas; P10144; -.
PRIDE; P10144; -.
DNASU; 3002; -.
Ensembl; ENST00000216341; ENSP00000216341; ENSG00000100453.
GeneID; 3002; -.
KEGG; hsa:3002; -.
UCSC; uc001wps.4; human.
CTD; 3002; -.
DisGeNET; 3002; -.
GeneCards; GZMB; -.
H-InvDB; HIX0011578; -.
HGNC; HGNC:4709; GZMB.
HPA; CAB000376; -.
HPA; HPA003418; -.
MIM; 123910; gene.
neXtProt; NX_P10144; -.
OpenTargets; ENSG00000100453; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P10144; -.
KO; K01353; -.
OMA; CVGDPEI; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P10144; -.
TreeFam; TF333630; -.
Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
SIGNOR; P10144; -.
ChiTaRS; GZMB; human.
EvolutionaryTrace; P10144; -.
GeneWiki; GZMB; -.
GenomeRNAi; 3002; -.
PMAP-CutDB; P10144; -.
PRO; PR:P10144; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100453; -.
CleanEx; HS_GZMB; -.
ExpressionAtlas; P10144; baseline and differential.
Genevisible; P10144; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0001772; C:immunological synapse; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0030141; C:secretory granule; IBA:GO_Central.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
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;
3D-structure; Apoptosis; Complete proteome; Cytolysis;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 18 {ECO:0000269|PubMed:15340161}.
PROPEP 19 20 Activation peptide.
{ECO:0000269|PubMed:1985927,
ECO:0000269|PubMed:3262682,
ECO:0000269|PubMed:3263427,
ECO:0000269|PubMed:8258716}.
/FTId=PRO_0000027399.
CHAIN 21 247 Granzyme B.
/FTId=PRO_0000027400.
DOMAIN 21 245 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 64 64 Charge relay system.
ACT_SITE 108 108 Charge relay system.
ACT_SITE 203 203 Charge relay system.
SITE 228 228 Mediates preference for Asp-containing
substrates. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 65
DISULFID 142 209
DISULFID 173 188
VARIANT 55 55 R -> Q (in dbSNP:rs8192917).
{ECO:0000269|PubMed:12721789,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2332171,
ECO:0000269|PubMed:2365998,
ECO:0000269|PubMed:2788607,
ECO:0000269|PubMed:2953813,
ECO:0000269|PubMed:3261871}.
/FTId=VAR_018371.
VARIANT 94 94 P -> A (in dbSNP:rs11539752).
{ECO:0000269|PubMed:2332171,
ECO:0000269|PubMed:3258865}.
/FTId=VAR_047409.
VARIANT 247 247 Y -> H (in dbSNP:rs2236338).
{ECO:0000269|PubMed:12721789,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_018381.
CONFLICT 32 33 RP -> PR (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 72 72 V -> G (in Ref. 3; AAA52118).
{ECO:0000305}.
CONFLICT 212 212 V -> C (in Ref. 4; AAB59528).
{ECO:0000305}.
STRAND 35 41 {ECO:0000244|PDB:1IAU}.
STRAND 46 55 {ECO:0000244|PDB:1IAU}.
STRAND 58 61 {ECO:0000244|PDB:1IAU}.
HELIX 63 65 {ECO:0000244|PDB:1IAU}.
STRAND 68 75 {ECO:0000244|PDB:1IAU}.
TURN 79 82 {ECO:0000244|PDB:1FQ3}.
STRAND 87 96 {ECO:0000244|PDB:1IAU}.
TURN 102 104 {ECO:0000244|PDB:1IAU}.
STRAND 110 116 {ECO:0000244|PDB:1IAU}.
STRAND 141 148 {ECO:0000244|PDB:1IAU}.
STRAND 150 154 {ECO:0000244|PDB:1IAU}.
STRAND 161 167 {ECO:0000244|PDB:1IAU}.
HELIX 170 176 {ECO:0000244|PDB:1IAU}.
TURN 177 180 {ECO:0000244|PDB:1IAU}.
TURN 183 185 {ECO:0000244|PDB:1IAU}.
STRAND 186 190 {ECO:0000244|PDB:1IAU}.
STRAND 205 209 {ECO:0000244|PDB:1IAU}.
STRAND 212 220 {ECO:0000244|PDB:1IAU}.
STRAND 228 232 {ECO:0000244|PDB:1IAU}.
HELIX 233 236 {ECO:0000244|PDB:1IAU}.
HELIX 237 245 {ECO:0000244|PDB:1IAU}.
SEQUENCE 247 AA; 27716 MW; C652271918EF24F9 CRC64;
MQPILLLLAF LLLPRADAGE IIGGHEAKPH SRPYMAYLMI WDQKSLKRCG GFLIRDDFVL
TAAHCWGSSI NVTLGAHNIK EQEPTQQFIP VKRPIPHPAY NPKNFSNDIM LLQLERKAKR
TRAVQPLRLP SNKAQVKPGQ TCSVAGWGQT APLGKHSHTL QEVKMTVQED RKCESDLRHY
YDSTIELCVG DPEIKKTSFK GDSGGPLVCN KVAQGIVSYG RNNGMPPRAC TKVSSFVHWI
KKTMKRY


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Genprice Inc, Invoices and accounting
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