Reviewed, UniProtKB/Swiss-Prot P04187 (GRAB_MOUSE)

Names and origin

Protein names

Recommended name:
    Granzyme B(G,H)
    EC=3.4.21.79
Alternative name(s):
    Cytotoxic cell protease 1
      Short name=CCP1
      Short name=CTLA-1
    Fragmentin-2

Gene names

Name:	Gzmb
Synonyms:	Ctla-1, Ctla1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the peptidase S1 family. Granzyme subfamily. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Apoptosis Cytolysis
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW induction of apoptosis by granzyme Inferred from direct assay. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: MGI serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Propeptide

19 – 20

2

Activation peptide

PRO_0000027401

Chain

21 – 247

227

Granzyme B(G,H)

PRO_0000027402

Regions

Domain

21 – 245

225

Peptidase S1

Sites

Active site

64

1

Charge relay system By similarity

Active site

108

1

Charge relay system By similarity

Active site

203

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

71

1

N-linked (GlcNAc...) Potential

Glycosylation

182

1

N-linked (GlcNAc...) Potential

Disulfide bond

49 ↔ 65

By similarity

Disulfide bond

142 ↔ 209

By similarity

Disulfide bond

173 ↔ 188

By similarity

Secondary structure

1

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247

Helix Strand Turn

Details...

Beta strand

35 – 41

7

Beta strand

43 – 55

13

Beta strand

58 – 61

4

Helix

63 – 65

3

Beta strand

68 – 75

8

Beta strand

87 – 96

10

Turn

102 – 104

3

Beta strand

110 – 116

7

Beta strand

141 – 147

7

Beta strand

149 – 151

3

Beta strand

154 – 156

3

Beta strand

161 – 168

8

Helix

170 – 174

5

Turn

175 – 177

3

Helix

178 – 180

3

Helix

183 – 185

3

Beta strand

186 – 189

4

Turn

200 – 204

5

Beta strand

206 – 209

4

Beta strand

212 – 219

8

Beta strand

228 – 232

5

Helix

233 – 245

13

Sequences

	Sequence		Length	Mass (Da)
	P04187-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: 996BCD199965C6D6	FASTA	247	27,470
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel serine proteases encoded by two cytotoxic T lymphocyte-specific genes." Lobe C.G., Finlay B.B., Paranchych W., Paetkau V.H., Bleackley R.C. Science 232:858-861(1986) [PubMed: 3518058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Organization of two genes encoding cytotoxic T lymphocyte-specific serine proteases CCPI and CCPII." Lobe C.G., Upton C., Duggan B., Ehrman N., Letellier M., Bell J., McFadden G., Bleackley R.C. Biochemistry 27:6941-6946(1988) [PubMed: 3264185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The inducible cytotoxic T-lymphocyte-associated gene transcript CTLA-1 sequence and gene localization to mouse chromosome 14." 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. Nature 322:268-271(1986) [PubMed: 3090449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[5]	"Genetic mapping of 40 cDNA clones on the mouse genome by PCR." Ko M.S., Wang X., Horton J.H., Hagen M.D., Takahashi N., Maezaki Y., Nadeau J.H. Mamm. Genome 5:349-355(1994) [PubMed: 8043949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 227-247. Strain: C57BL/6J.
[6]	"A family of serine esterases in lytic granules of cytolytic T lymphocytes." Masson D., Tschopp J. Cell 49:679-685(1987) [PubMed: 3555842] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-40.
[7]	"Comparative molecular model building of two serine proteinases from cytotoxic T lymphocytes." Murphy M.E.P., Moult J., Bleackley R.C., Gershenfeld H., Weissman I.L., James M.N.G. Proteins 4:190-204(1988) [PubMed: 3237717] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04072 mRNA. Translation: CAA27715.1.
M12302 mRNA. Translation: AAA37383.1.
M22526 Genomic DNA. Translation: AAB61756.1.
BC002085 mRNA. Translation: AAH02085.1.
U05707 Genomic DNA. Translation: AAB60470.1.

IPI

IPI00114066.

PIR

PRMSCL. A94288.

RefSeq

NP_038570.1.

UniGene

Mm.14874

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CP1	model	-	A	21-247	[»]

SMR

P04187. Positions 21-245.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-562N.

STRING

P04187.

Protein family/group databases

MEROPS

S01.136.

Proteomic databases

PRIDE

P04187.

Genome annotation databases

Ensembl

ENSMUST00000015581; ENSMUSP00000015581; ENSMUSG00000015437; Mus musculus. [Genome view]

GeneID

14939.

KEGG

mmu:14939.

UCSC

uc007ubv.1. mouse.

Organism-specific databases

CTD

14939.

MGI

MGI:109267. Gzmb.

Phylogenomic databases

eggNOG

roNOG09047.

HOGENOM

HBG755338.

HOVERGEN

P04187.

InParanoid

P04187.

OMA

STIEICA.

OrthoDB

EOG9CZF11.

PhylomeDB

P04187.

Enzyme and pathway databases

BRENDA

3.4.21.79. 244.

Gene expression databases

ArrayExpress

P04187.

Bgee

P04187.

CleanEx

MM_GZMB.

Genevestigator

P04187.

GermOnline

ENSMUSG00000015437. Mus musculus.

Family and domain databases

InterPro

IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

287263.

SOURCE

Search...

Entry information

Entry name

GRAB_MOUSE

Accession

Primary (citable) accession number: P04187

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	January 19, 2010
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)