Senp3 SUMO specific peptidase 3 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Senp3provided by RGD
Official Full Name: SUMO specific peptidase 3provided by RGD
Primary source: RGD:1312040
See related: Ensembl:ENSRNOG00000013746 AllianceGenome:RGD:1312040
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Predicted to enable SUMO-specific isopeptidase activity and thiol-dependent deubiquitinase. Predicted to be involved in protein desumoylation. Predicted to act upstream of or within protein metabolic process. Predicted to be located in nucleolus and nucleoplasm. Predicted to be part of MLL1 complex. Predicted to be active in nucleus. Orthologous to human SENP3 (SUMO specific peptidase 3). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Thymus (RPKM 107.8), Spleen (RPKM 89.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 10q24

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (54889445..54898359, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (54390698..54399590, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (56277609..56286867, complement)

Chromosome 10 - NC_086028.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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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?

we performed ischemia and ischemia-reperfusion experiments in the cardiomyocyte H9C2 cell line. Similar to whole hearts, ischemia induced a decrease in cytosolic SENP3. Furthermore, shRNA-mediated knockdown of SENP3 led to an increase in the rate of cell death upon reperfusion.
Title: Protective role of the deSUMOylating enzyme SENP3 in myocardial ischemia-reperfusion injury.
Study found that high oxidative stress level following subarachnoid hemorrhage induced rising of SENP3
Title: Inhibition of SENP3 by lentivirus induces suppression of apoptosis in experimental subarachnoid hemorrhage in rats.
SENP3 protein expression was significantly up-regulated after subarachnoid hemorrhage in cerebral cortex.
Title: Expression and cell distribution of SENP3 in the cerebral cortex after experimental subarachnoid hemorrhage in rats: a pilot study.
Western blot analysis showed a significant upregulation of SENP3 and active caspase-3 following H(2)O(2) stimulation
Title: An upregulation of SENP3 after spinal cord injury: implications for neuronal apoptosis.

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables cysteine-type deubiquitinase activity	ISO Inferred from Sequence Orthology more info
enables cysteine-type peptidase activity	ISO Inferred from Sequence Orthology more info
enables deSUMOylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables deSUMOylase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in negative regulation of double-strand break repair via homologous recombination	ISO Inferred from Sequence Orthology more info
involved_in protein desumoylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein desumoylation	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of MLL1 complex	ISO Inferred from Sequence Orthology more info
located_in nucleolus	ISO Inferred from Sequence Orthology more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: sentrin-specific protease 3

Names: SUMO/sentrin specific peptidase 3; SUMO/sentrin specific protease 3; Sumo1/sentrin/SMT3 specific peptidase 3

NP_001013134.2

EC 3.4.22.68

XP_038941907.1

EC 3.4.22.68

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_001013116.2 → NP_001013134.2 sentrin-specific protease 3

See identical proteins and their annotated locations for NP_001013134.2

Status: VALIDATED

Source sequence(s)

BC101901, BF407260

UniProtKB/TrEMBL

A6HFT2, Q3MID8

Related

ENSRNOP00000087578.1, ENSRNOT00000113186.1

Conserved Domains (1) summary

pfam02902
Location:394 → 566

Peptidase_C48; Ulp1 protease family, C-terminal catalytic domain

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086028.1 Reference GRCr8

Range

54889445..54898359 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_039085979.2 → XP_038941907.1 sentrin-specific protease 3 isoform X1

UniProtKB/TrEMBL

G3V7S5, Q3MID8

Related

ENSRNOP00000018670.6

Conserved Domains (1) summary

pfam02902
Location:394 → 532

Peptidase_C48; Ulp1 protease family, C-terminal catalytic domain