Mcpt4 mast cell protease 4 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Mcpt4provided by RGD
Official Full Name: mast cell protease 4provided by RGD
Primary source: RGD:3064
See related: EnsemblRapid:ENSRNOG00000024785 AllianceGenome:RGD:3064
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 heparin binding activity; peptide binding activity; and serine-type endopeptidase activity. Involved in protein catabolic process. Predicted to be active in extracellular space. [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in Thymus (RPKM 9.5), Kidney (RPKM 2.2) and 2 other tissues See more
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Genomic context

Location:: 15p12

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	15	NC_086033.1 (33471491..33474112)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	15	NC_051350.1 (29501595..29504216)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	15	NC_005114.4 (34751550..34754409)

Chromosome 15 - NC_086033.1 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?

investigation of substrate recognition profile
Title: Rat mast cell protease 4 is a beta-chymase with unusually stringent substrate recognition profile.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables heparin binding	IDA Inferred from Direct Assay more info	PubMed
enables peptide binding	IDA Inferred from Direct Assay more info	PubMed
enables serine-type endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables serine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in protein catabolic process	IDA Inferred from Direct Assay more info	PubMed
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

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Preferred Names: mast cell protease 4

Names: mast cell protease IV; rMCP-4; rMCP-IV

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_019321.2 → NP_062194.1 mast cell protease 4 precursor

See identical proteins and their annotated locations for NP_062194.1

Status: PROVISIONAL

Source sequence(s)

U67907

UniProtKB/Swiss-Prot

P97592

UniProtKB/TrEMBL

A6KH70

Related

ENSRNOP00000069727.1, ENSRNOT00000089559.3

Conserved Domains (2) summary

smart00020
Location:20 → 239

Tryp_SPc; Trypsin-like serine protease

cd00190
Location:21 → 242

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 ...