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Protein

Granzyme G

Gene

Gzmg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme is probably necessary for target cell lysis in cell-mediated immune responses.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Charge relay systemBy similarity
Active sitei109 – 1091Charge relay systemBy similarity
Active sitei204 – 2041Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cytolysis

Enzyme and pathway databases

ReactomeiR-MMU-75108. Activation, myristolyation of BID and translocation to mitochondria.

Protein family/group databases

MEROPSiS01.402.

Names & Taxonomyi

Protein namesi
Recommended name:
Granzyme G (EC:3.4.21.-)
Alternative name(s):
CTL serine protease 1
MCSP-1
Gene namesi
Name:Gzmg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:109253. Gzmg.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 202Activation peptide1 PublicationPRO_0000027411
Chaini21 – 248228Granzyme GPRO_0000027412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 66PROSITE-ProRule annotation
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi143 ↔ 210PROSITE-ProRule annotation
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi175 ↔ 189PROSITE-ProRule annotation
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP13366.
PaxDbiP13366.
PRIDEiP13366.

Expressioni

Gene expression databases

BgeeiP13366.
CleanExiMM_GZMG.
ExpressionAtlasiP13366. baseline and differential.
GenevisibleiP13366. MM.

Interactioni

Protein-protein interaction databases

IntActiP13366. 1 interaction.
MINTiMINT-4096735.
STRINGi10090.ENSMUSP00000015578.

Structurei

3D structure databases

ProteinModelPortaliP13366.
SMRiP13366. Positions 21-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 246226Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP13366.
OMAiQEDHECK.
OrthoDBiEOG7RRF7Z.
PhylomeDBiP13366.
TreeFamiTF333630.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPILILLTL LLPLRAGAEE IIGGHEVKPH SRPYMAFIKS VDIEGKKKYC
60 70 80 90 100
GGFLVQDDFV LTAAHCRNRS MTVTLGAHNI KAKEETQQII PVAKAIPHPA
110 120 130 140 150
FNRKHGTNDI MLLKLESKAK RTKAVRPLKL PRPNARVKPG DVCSVAGWGK
160 170 180 190 200
TSINATKASA RLREAQLIIQ EDEECKKLWY TYSKTTQICA GDPKKVQAPY
210 220 230 240
EGESGGPLVC DNLAYGVVSY GINRTITPGV FTKVVHFLPW ISTNMKLL
Length:248
Mass (Da):27,381
Last modified:January 1, 1990 - v1
Checksum:iEAF4A438EABF04AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601V → G in AAA37486 (PubMed:3053963).Curated
Sequence conflicti60 – 601V → G in CAA32254 (PubMed:3053963).Curated
Sequence conflicti207 – 2071P → T in AAA37486 (PubMed:3053963).Curated
Sequence conflicti207 – 2071P → T in CAA32254 (PubMed:3053963).Curated
Sequence conflicti224 – 2241R → K in AAB19191 (PubMed:8917549).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36900 mRNA. Translation: AAA37486.1.
U66473 Genomic DNA. Translation: AAB19191.1.
J02872 mRNA. Translation: AAA37731.1.
X14092 mRNA. Translation: CAA32254.1.
CCDSiCCDS27144.1.
PIRiA33412.
S06176.
RefSeqiNP_034505.1. NM_010375.2.
UniGeneiMm.14868.

Genome annotation databases

EnsembliENSMUST00000015578; ENSMUSP00000015578; ENSMUSG00000040284.
GeneIDi14944.
KEGGimmu:14944.
UCSCiuc007ubq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36900 mRNA. Translation: AAA37486.1.
U66473 Genomic DNA. Translation: AAB19191.1.
J02872 mRNA. Translation: AAA37731.1.
X14092 mRNA. Translation: CAA32254.1.
CCDSiCCDS27144.1.
PIRiA33412.
S06176.
RefSeqiNP_034505.1. NM_010375.2.
UniGeneiMm.14868.

3D structure databases

ProteinModelPortaliP13366.
SMRiP13366. Positions 21-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP13366. 1 interaction.
MINTiMINT-4096735.
STRINGi10090.ENSMUSP00000015578.

Protein family/group databases

MEROPSiS01.402.

Proteomic databases

EPDiP13366.
PaxDbiP13366.
PRIDEiP13366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015578; ENSMUSP00000015578; ENSMUSG00000040284.
GeneIDi14944.
KEGGimmu:14944.
UCSCiuc007ubq.1. mouse.

Organism-specific databases

CTDi14944.
MGIiMGI:109253. Gzmg.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP13366.
OMAiQEDHECK.
OrthoDBiEOG7RRF7Z.
PhylomeDBiP13366.
TreeFamiTF333630.

Enzyme and pathway databases

ReactomeiR-MMU-75108. Activation, myristolyation of BID and translocation to mitochondria.

Miscellaneous databases

NextBioi287283.
PROiP13366.
SOURCEiSearch...

Gene expression databases

BgeeiP13366.
CleanExiMM_GZMG.
ExpressionAtlasiP13366. baseline and differential.
GenevisibleiP13366. MM.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases."
    Jenne D.E., Masson D., Zimmer M., Haefliger J.-A., Li W.-H., Tschopp J.
    Biochemistry 28:7953-7961(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-48.
  2. "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.
  3. "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 51-248.
    Tissue: T-cell.

Entry informationi

Entry nameiGRAG_MOUSE
AccessioniPrimary (citable) accession number: P13366
Secondary accession number(s): P97388
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.