Tpsb2 tryptase beta 2 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Tpsb2provided by RGD
Official Full Name: tryptase beta 2provided by RGD
Primary source: RGD:3065
See related: EnsemblRapid:ENSRNOG00000018611 AllianceGenome:RGD:3065
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
Also known as: Mcpt6
Summary: Predicted to enable heparin binding activity and serine-type endopeptidase activity. Predicted to be involved in proteolysis. Predicted to be active in extracellular space. Orthologous to human TPSAB1 (tryptase alpha/beta 1) and TPSB2 (tryptase beta 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Muscle (RPKM 18.9), Heart (RPKM 14.7) and 5 other tissues See more
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Genomic context

Location:: 10q12

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (14886310..14888102)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (14381779..14383571)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (14722672..14724464)

Chromosome 10 - NC_086028.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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General gene information

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Markers

PMC316772P2 (e-PCR)
- UniSTS:273046

D17Mit46 (e-PCR), detects polymorphism
- UniSTS:116638

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables heparin binding	ISO Inferred from Sequence Orthology more info
enables peptidase activity	ISO Inferred from Sequence Orthology more info
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

Process	Evidence Code	Pubs
involved_in proteolysis	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

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Preferred Names: tryptase beta-2

Names: mast cell protease 6; rMCP-6; tryptase-2

NP_062053.2

EC 3.4.21.59

NCBI Reference Sequences (RefSeq)

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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_019180.2 → NP_062053.2 tryptase beta-2 precursor

See identical proteins and their annotated locations for NP_062053.2

Status: PROVISIONAL

Source sequence(s)

U67909

UniProtKB/TrEMBL

A6HD23, G3V8F2

Related

ENSRNOP00000025220.6, ENSRNOT00000025220.8

Conserved Domains (2) summary

smart00020
Location:30 → 266

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:30 → 268

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 ...