PAMR1 peptidase domain containing associated with muscle regeneration 1 [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: PAMR1provided by VGNC
Official Full Name: peptidase domain containing associated with muscle regeneration 1provided by VGNC
Primary source: VGNC:VGNC:32562
See related: BGD:BT21562; Ensembl:ENSBTAG00000012630
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: DKFZP586H2123
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 15

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_12	current	ARS-UCD2.0 (GCF_002263795.3)	15	NC_037342.1 (65950554..66028064, complement)

Chromosome 15 - NC_037342.1 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:: NC_037342.1 Chromosome 15 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: Dominette sequence data
BioProject: PRJNA294306
Analysis date: Tue Dec 17 08:57:05 2024

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables calcium ion binding	IEA Inferred from Electronic Annotation more info	PubMed
enables serine-type endopeptidase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in proteolysis	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: inactive serine protease PAMR1

Names: peptidase domain-containing protein associated with muscle regeneration 1; regeneration associated muscle protease; regeneration-associated muscle protease homolog

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_001015591.1 → NP_001015591.1 inactive serine protease PAMR1 precursor

See identical proteins and their annotated locations for NP_001015591.1

Status: PROVISIONAL

Source sequence(s)

BT020875

UniProtKB/Swiss-Prot

Q5E9P5

UniProtKB/TrEMBL

A0A3Q1LJQ3

Related

ENSBTAP00000016767.5, ENSBTAT00000016767.7

Conserved Domains (5) summary

cd00033
Location:280 → 343

CCP; Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system

smart00020
Location:461 → 715

Tryp_SPc; Trypsin-like serine protease

cd00041
Location:128 → 234

CUB; CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

cd00054
Location:240 → 272

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...

cd00190
Location:461 → 718

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 ...