Gzmk granzyme K [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Gzmkprovided by RGD
Official Full Name: granzyme Kprovided by RGD
Primary source: RGD:68401
See related: EnsemblRapid:ENSRNOG00000010661 AllianceGenome:RGD:68401
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables serine-type peptidase activity. Predicted to be involved in protein maturation. Predicted to be active in extracellular space and secretory granule. Orthologous to human GZMK (granzyme K). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Spleen (RPKM 351.8), Lung (RPKM 262.7) and 4 other tissues See more
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 2q14

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (46573997..46582015, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (44840811..44848829, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (45069136..45077154, complement)

Chromosome 2 - NC_086020.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type peptidase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in granzyme-mediated programmed cell death signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein maturation	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info

General protein information

Go to the top of the page Help

Preferred Names: granzyme K

Names: NK-Tryp-2; NK-tryptase-2; RNK-Tryp-2

NP_058815.1

EC 3.4.21.-

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_017119.2 → NP_058815.1 granzyme K precursor

See identical proteins and their annotated locations for NP_058815.1

Status: PROVISIONAL

Source sequence(s)

L19694

UniProtKB/Swiss-Prot

P49864

UniProtKB/TrEMBL

A6I5R1, F1M8K5

Related

ENSRNOP00000014319.3, ENSRNOT00000014319.7

Conserved Domains (2) summary

smart00020
Location:25 → 248

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:26 → 251

Tryp_SPc; Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad ...