[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3518058 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1021/bi00418a040; PubMed=3264185 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1038/322268a0; PubMed=3090449 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1007/BF00356553; PubMed=8043949 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0092-8674(87)90544-7; PubMed=3555842 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1002/prot.340040306; PubMed=3237717 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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).
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 [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X04072; CAA27715.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12302; AAA37383.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22526; AAB61756.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002085; AAH02085.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U05707; AAB60470.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A94288; PRMSCL.

NP_038570.1; -.

3D structure databases

PDB

2CP1; Model; -; A=21-247.

[ExPASy / RCSB / EBI]

2CP1; -.

P04187; 21-245.

Protein-protein interaction databases

DIP

DIP:562N; -.

Protein family/group databases

MEROPS

S01.136; -.

Organism-specific databases

MGI

MGI:109267; Gzmb.

Gene expression databases

ArrayExpress

P04187; -.

CleanEx

MM_GZMB; -.

GermOnline

ENSMUSG00000015437; Mus musculus.

Ontologies

GO:0008233;	Molecular function: peptidase activity (inferred from mutant phenotype from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0008626;	Biological process: induction of apoptosis by granzyme (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000015437; Mus musculus. [Contig view]

GeneID

14939; -.

KEGG

mmu:14939; -.

Phylogenomic databases

HOGENOM

P04187; -.

HOVERGEN

P04187; -.

Other

NextBio

287263; -.

SOURCE

Gzmb; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Apoptosis; Cytolysis; Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`PROPEP`	`19 20`	`2`	`Activation peptide.`	`PRO_0000027401`
`CHAIN`	`21 247`	`227`	`Granzyme B(G,H).`	`PRO_0000027402`
`DOMAIN`	`21 245`	`225`	`Peptidase S1.`
`ACT_SITE`	`64 64`		`Charge relay system (By similarity).`
`ACT_SITE`	`108 108`		`Charge relay system (By similarity).`
`ACT_SITE`	`203 203`		`Charge relay system (By similarity).`
`CARBOHYD`	`71 71`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`182 182`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`49 65`		`By similarity.`
`DISULFID`	`142 209`		`By similarity.`
`DISULFID`	`173 188`		`By similarity.`
`STRAND`	`35 41`	`7`
`STRAND`	`43 55`	`13`
`STRAND`	`58 61`	`4`
`HELIX`	`63 65`	`3`
`STRAND`	`68 75`	`8`
`STRAND`	`87 96`	`10`
`TURN`	`102 104`	`3`
`STRAND`	`110 116`	`7`
`STRAND`	`141 147`	`7`
`STRAND`	`149 151`	`3`
`STRAND`	`154 156`	`3`
`STRAND`	`161 168`	`8`
`HELIX`	`170 174`	`5`
`TURN`	`175 177`	`3`
`HELIX`	`178 180`	`3`
`HELIX`	`183 185`	`3`
`STRAND`	`186 189`	`4`
`TURN`	`200 204`	`5`
`STRAND`	`206 209`	`4`
`STRAND`	`212 219`	`8`
`STRAND`	`228 232`	`5`
`HELIX`	`233 245`	`13`

Sequence information

Length: 247 AA [This is the length of the unprocessed precursor]

Molecular weight: 27470 Da [This is the MW of the unprocessed precursor]

CRC64: 996BCD199965C6D6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKILLLLLTL SLASRTKAGE IIGGHEVKPH SRPYMALLSI KDQQPEAICG GFLIREDFVL 

        70         80         90        100        110        120 
TAAHCEGSII NVTLGAHNIK EQEKTQQVIP MVKCIPHPDY NPKTFSNDIM LLKLKSKAKR 

       130        140        150        160        170        180 
TRAVRPLNLP RRNVNVKPGD VCYVAGWGRM APMGKYSNTL QEVELTVQKD RECESYFKNR 

       190        200        210        220        230        240 
YNKTNQICAG DPKTKRASFR GDSGGPLVCK KVAAGIVSYG YKDGSPPRAF TKVSSFLSWI 


KKTMKSS

P04187 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools