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P04187 (GRAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Granzyme B(G,H)

EC=3.4.21.79
Alternative name(s):
CTLA-1
Cytotoxic cell protease 1
Short name=CCP1
Fragmentin-2
Gene names
Name:Gzmb
Synonyms:Ctla-1, Ctla1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 202Activation peptide
PRO_0000027401
Chain21 – 247227Granzyme B(G,H)
PRO_0000027402

Regions

Domain21 – 245225Peptidase S1

Sites

Active site641Charge relay system By similarity
Active site1081Charge relay system By similarity
Active site2031Charge relay system By similarity
Site2281Mediates preference for Asp-containing substrates By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 65 By similarity
Disulfide bond142 ↔ 209 By similarity
Disulfide bond173 ↔ 188 By similarity

Secondary structure

......................................... 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04187 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 996BCD199965C6D6

FASTA24727,470
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS27147.1.
PIRPRMSCL. A94288.
RefSeqNP_038570.1. NM_013542.2.
UniGeneMm.14874.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CP1model-A21-247[»]
ProteinModelPortalP04187.
SMRP04187. Positions 21-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200135. 5 interactions.
DIPDIP-562N.
IntActP04187. 1 interaction.
MINTMINT-4096650.

Protein family/group databases

MEROPSS01.136.

PTM databases

PhosphoSiteP04187.

Proteomic databases

MaxQBP04187.
PaxDbP04187.
PRIDEP04187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015581; ENSMUSP00000015581; ENSMUSG00000015437.
GeneID14939.
KEGGmmu:14939.
UCSCuc007ubv.1. mouse.

Organism-specific databases

CTD3002.
MGIMGI:109267. Gzmb.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP04187.
KOK01353.
OMAEECESKL.
OrthoDBEOG7RRF7Z.
PhylomeDBP04187.
TreeFamTF333630.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

ArrayExpressP04187.
BgeeP04187.
CleanExMM_GZMB.
GenevestigatorP04187.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287263.
PROP04187.
SOURCESearch...

Entry information

Entry nameGRAB_MOUSE
AccessionPrimary (citable) accession number: P04187
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: July 9, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot