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P08884 (GRAE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Granzyme E
EC=3.4.21.-
Alternative name(s):
CTL serine protease 2
Cytotoxic cell protease 3
Short name=CCP3
Cytotoxic serine protease 2
D12
MCSP2
Gene names
Name:Gzme
Synonyms:Ccp3, Ctla-6, Ctla6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length248 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 probably necessary for target cell lysis in cell-mediated immune responses.

Subcellular location

Cytoplasmic granule. Note: Cytoplasmic granules of cytolytic T-lymphocytes.

Sequence similarities

Belongs to the peptidase S1 family. Granzyme subfamily.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processCytolysis
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 202
PRO_0000027407
Chain21 – 248228Granzyme E
PRO_0000027408

Regions

Domain21 – 246226Peptidase S1

Sites

Active site651Charge relay system By similarity
Active site1091Charge relay system By similarity
Active site2041Charge relay system By similarity

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 66 By similarity
Disulfide bond143 ↔ 210 By similarity
Disulfide bond175 ↔ 189 By similarity

Experimental info

Sequence conflict51L → P in AAB19192. Ref.3
Sequence conflict1321R → K in AAA37487. Ref.5
Sequence conflict1321R → K in CAA32255. Ref.5
Sequence conflict1501S → P Ref.3
Sequence conflict1501S → P Ref.4

Sequences

Sequence LengthMass (Da)Tools
P08884 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 3A31912A45E93D3F

FASTA24827,494
        10         20         30         40         50         60 
MPPVLILLTL LLPLGAGAEE IIGGHVVKPH SRPYMAFVKS VDIEGNRRYC GGFLVQDDFV 

        70         80         90        100        110        120 
LTAAHCRNRT MTVTLGAHNI KAKEETQQII PVAKAIPHPD YNATAFFSDI MLLKLESKAK 

       130        140        150        160        170        180 
RTKAVRPLKL PRPNARVKPG DVCSVAGWGS RSINDTKASA RLREAQLVIQ EDEECKKRFR 

       190        200        210        220        230        240 
HYTETTEICA GDLKKIKTPF KGDSGGPLVC DNKAYGLLAY AKNRTISSGV FTKIVHFLPW 


ISRNMKLL

« Hide

References

[1]"Isolation of two cDNA sequences which encode cytotoxic cell proteases."
Bleackley R.C., Duggan B., Ehrman N., Lobe C.G.
FEBS Lett. 234:153-159(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Prendergast J.A., Pinkoski M., Wolfenden A., Bleackley R.C.
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Long-range disruption of gene expression by a selectable marker cassette."
Pham C.T.N., MacIvor D.M., Hug B.A., Heusel J.W., Ley T.J.
Proc. Natl. Acad. Sci. U.S.A. 93:13090-13095(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[4]"Identification and sequencing of cDNA clones encoding the granule-associated serine proteases granzymes D, E, and F of cytolytic T lymphocytes."
Jenne D.E., Rey C., Haefliger J.-A., Qiao B.-Y., Groscurth P., Tschopp J.
Proc. Natl. Acad. Sci. U.S.A. 85:4814-4818(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-248.
[5]"Isolation and sequence analysis of serine protease cDNAs from mouse cytolytic T lymphocytes."
Kwon B.S., Kestler D., Lee E., Wakulchik M., Young J.D.-E.
J. Exp. Med. 168:1839-1854(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-248.
Tissue: Cytotoxic T-cell.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M36901 mRNA. Translation: AAA37487.1.
X12821 mRNA. Translation: CAA31308.1.
U66474 Genomic DNA. Translation: AAB19192.1.
X56988 Genomic DNA. Translation: CAA40306.1.
J03256 mRNA. Translation: AAA37737.1.
X14093 mRNA. Translation: CAA32255.1.
IPIIPI00323939.
PIRS01006.
RefSeqNP_034503.2. NM_010373.3.
UniGeneMm.14424.

3D structure databases

ProteinModelPortalP08884.
SMRP08884. Positions 21-248.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000015588.

Protein family/group databases

MEROPSS01.399.

Proteomic databases

PaxDbP08884.
PRIDEP08884.

Protocols and materials databases

DNASU14942.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089549; ENSMUSP00000086978; ENSMUSG00000022156.
GeneID14942.
KEGGmmu:14942.
UCSCuc007ubp.1. mouse.

Organism-specific databases

CTD14942.
MGIMGI:109265. Gzme.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00700000104027.
HOGENOMHOG000251820.
HOVERGENHBG013304.
KOK01362.
OMAHYTETTE.

Gene expression databases

ArrayExpressP08884.
BgeeP08884.
CleanExMM_GZME.
GenevestigatorP08884.
GermOnlineENSMUSG00000022156. Mus musculus.

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. Pept_Ser_Cys. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287275.
SOURCESearch...

Entry information

Entry nameGRAE_MOUSE
AccessionPrimary (citable) accession number: P08884
Secondary accession number(s): P97389
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 3, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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