Furin furin (paired basic amino acid cleaving enzyme) [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Furinprovided by RGD
Official Full Name: furin (paired basic amino acid cleaving enzyme)provided by RGD
Primary source: RGD:3274
See related: Ensembl:ENSRNOG00000011352 AllianceGenome:RGD:3274
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: Pace; Pcsk3
Summary: Enables serine-type endopeptidase activity. Involved in several processes, including positive regulation of cell migration; positive regulation of transforming growth factor beta receptor signaling pathway; and protein processing. Located in Golgi cisterna; endoplasmic reticulum membrane; and plasma membrane. Orthologous to human FURIN (furin, paired basic amino acid cleaving enzyme). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Kidney (RPKM 322.8), Liver (RPKM 310.4) and 9 other tissues See more
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 1q31

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	1	NC_086019.1 (143757389..143770430, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	1	NC_051336.1 (134348142..134361182, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	1	NC_005100.4 (142185092..142198167, complement)

Chromosome 1 - NC_086019.1 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

Expression

Go to the top of the page Help

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

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

MiR-22-3p in exosomes increases the risk of heart failure after down-regulation of FURIN.
Title: MiR-22-3p in exosomes increases the risk of heart failure after down-regulation of FURIN.
TGFbeta treatment aggravated hypoxia-induced BBB permeability but ALK5 or Furin blockade reversed injury-induced permeability changes. Thus during insult Furin compromises endothelial integrity by mediating the effects of TGFbeta. Targeting the Furin or ALK5 pathway may offer novel therapeutic strategies for improving BBB stability and CNS function during disease.
Title: Furin inhibition prevents hypoxic and TGFβ-mediated blood-brain barrier disruption.
overexpression of PCs, furin and PC5, but not PC7, which are all expressed in SMC, increase PKGI cleavage in a dose-dependent manner
Title: Proprotein convertases play an important role in regulating PKGI endoproteolytic cleavage and nuclear transport.
these data suggest that furin may play an important role in regulating apoptosis and proliferation of granulosa cells.
Title: Proprotein convertase furin regulates apoptosis and proliferation of granulosa cells in the rat ovary.
upregulated during the preovulatory period, which results in activation of proteinases associated with the breakdown of the follicular wall during ovulation
Title: Ovarian furin (proprotein convertase subtilisin/kexin type3): expression, localization, and potential role in ovulation in the rat.
integrin bidirectional signalling is critically controlled by furin
Title: Integrin cleavage regulates bidirectional signalling in vascular smooth muscle cells.
Disturbances of the MT1-MMP/furin interaction must account for a lack in extracellular matrix remodeling, increased deposition of glomerular basement membrane material, and loss of glomerular filtration integrity in diabetic glomerulopathy.
Title: Expression and localization of MT1-MMP and furin in the glomerular wall of short- and long-term diabetic rats.
proGHRH is initially cleave by furin at preproGHRH29-30, followed by a second cleavage at preproGHRH74 primarily by PC1 to generate GHRH and GHRH-RP peptides, respectively.
Title: Stepwise posttranslational processing of progrowth hormone-releasing hormone (proGHRH) polypeptide by furin and PC1.
CDX2 regulates furin expression in intestinal epithelial cells
Title: The CDX2 transcription factor regulates furin expression during intestinal epithelial cell differentiation.
Data suggest that inhibition of furin and PC5 and resulting inhibition of insulin-like growth factor 1 receptor (IGF-1R) activation can inhibit IGF-1-induced membrane-type 1 matrix metalloproteinase activity in vascular smooth muscle cells.
Title: Proprotein convertases regulate insulin-like growth factor 1-induced membrane-type 1 matrix metalloproteinase in VSMCs via endoproteolytic activation of the insulin-like growth factor-1 receptor.

Submit: New GeneRIF Correction See all GeneRIFs (12)

General gene information

Go to the top of the page Help

Markers

Furin (e-PCR), detects polymorphism
- UniSTS:532487

Pcsk3 (e-PCR), detects polymorphism
- UniSTS:144143

PMC156147P3 (e-PCR)
- UniSTS:271380

RH94589 (e-PCR)
- UniSTS:119837

FURIN (e-PCR)
- UniSTS:503074

D1Smu12 (e-PCR)
- UniSTS:532057

FURIN (e-PCR)
- UniSTS:265098

D1Bda27 (e-PCR)
- UniSTS:239774

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables heparan sulfate binding	IEA Inferred from Electronic Annotation more info
enables heparan sulfate binding	ISO Inferred from Sequence Orthology more info
enables heparan sulfate binding	ISS Inferred from Sequence or Structural Similarity more info
enables heparin binding	IEA Inferred from Electronic Annotation more info
enables heparin binding	ISO Inferred from Sequence Orthology more info
enables heparin binding	ISS Inferred from Sequence or Structural Similarity more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nerve growth factor binding	IEA Inferred from Electronic Annotation more info
enables nerve growth factor binding	ISO Inferred from Sequence Orthology more info
enables peptidase activity	ISO Inferred from Sequence Orthology more info
enables peptide binding	IEA Inferred from Electronic Annotation more info
enables peptide binding	ISO Inferred from Sequence Orthology more info
enables protease binding	IEA Inferred from Electronic Annotation more info
enables protease binding	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
enables serine-type endopeptidase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables serine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
enables serine-type endopeptidase activity	ISS Inferred from Sequence or Structural Similarity more info
enables serine-type endopeptidase inhibitor activity	IEA Inferred from Electronic Annotation more info
enables serine-type endopeptidase inhibitor activity	ISO Inferred from Sequence Orthology more info
enables serine-type peptidase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in blastocyst formation	IEA Inferred from Electronic Annotation more info
involved_in blastocyst formation	ISO Inferred from Sequence Orthology more info
involved_in cytokine precursor processing	IEA Inferred from Electronic Annotation more info
involved_in cytokine precursor processing	ISO Inferred from Sequence Orthology more info
involved_in cytokine precursor processing	ISS Inferred from Sequence or Structural Similarity more info
involved_in dibasic protein processing	IEA Inferred from Electronic Annotation more info
involved_in dibasic protein processing	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of low-density lipoprotein particle receptor catabolic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of low-density lipoprotein particle receptor catabolic process	ISO Inferred from Sequence Orthology more info
NOT involved_in negative regulation of nerve growth factor production	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of transforming growth factor beta1 production	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of transforming growth factor beta1 production	ISO Inferred from Sequence Orthology more info
involved_in nerve growth factor production	IEA Inferred from Electronic Annotation more info
involved_in nerve growth factor production	ISO Inferred from Sequence Orthology more info
involved_in peptide biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in peptide biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in peptide hormone processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in peptide hormone processing	IEA Inferred from Electronic Annotation more info
involved_in peptide hormone processing	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of transforming growth factor beta receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of viral entry into host cell	IEA Inferred from Electronic Annotation more info
involved_in protein maturation	ISO Inferred from Sequence Orthology more info
involved_in protein processing	IDA Inferred from Direct Assay more info	PubMed
involved_in protein processing	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within protein processing	ISO Inferred from Sequence Orthology more info
involved_in protein processing	ISO Inferred from Sequence Orthology more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info
involved_in regulation of cholesterol transport	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within regulation of cholesterol transport	ISO Inferred from Sequence Orthology more info
involved_in regulation of protein catabolic process	ISO Inferred from Sequence Orthology more info
involved_in regulation of signal transduction	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within regulation of signal transduction	ISO Inferred from Sequence Orthology more info
involved_in secretion by cell	IEA Inferred from Electronic Annotation more info
involved_in secretion by cell	ISO Inferred from Sequence Orthology more info
involved_in signal peptide processing	IEA Inferred from Electronic Annotation more info
involved_in signal peptide processing	ISO Inferred from Sequence Orthology more info
involved_in viral life cycle	IEA Inferred from Electronic Annotation more info
involved_in viral life cycle	ISO Inferred from Sequence Orthology more info
involved_in zymogen activation	IEA Inferred from Electronic Annotation more info
involved_in zymogen activation	ISO Inferred from Sequence Orthology more info
involved_in zymogen inhibition	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in Golgi cisterna	IDA Inferred from Direct Assay more info	PubMed
is_active_in Golgi membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in Golgi membrane	IEA Inferred from Electronic Annotation more info
located_in Golgi membrane	ISO Inferred from Sequence Orthology more info
located_in cell surface	IEA Inferred from Electronic Annotation more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum membrane	IDA Inferred from Direct Assay more info	PubMed
located_in endosome membrane	IEA Inferred from Electronic Annotation more info
NOT located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in membrane raft	IEA Inferred from Electronic Annotation more info
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
is_active_in trans-Golgi network	IBA Inferred from Biological aspect of Ancestor more info
located_in trans-Golgi network	IEA Inferred from Electronic Annotation more info
located_in trans-Golgi network	ISO Inferred from Sequence Orthology more info
located_in trans-Golgi network transport vesicle	IEA Inferred from Electronic Annotation more info
located_in trans-Golgi network transport vesicle	ISO Inferred from Sequence Orthology more info

General protein information

Go to the top of the page Help

Preferred Names: furin

Names: Paired basic amino acid cleaving enzyme (furin); Proprotein convertase subtilisin/kexin type 3 (paired basic amino acid cleaving enzyme, furin, membrane associated receptor protein); dibasic-processing enzyme; paired basic amino acid residue-cleaving enzyme; prohormone convertase 3; proprotein convertase subtilisin/kexin type3

NP_062204.2

EC 3.4.21.75

XP_008757777.1

EC 3.4.21.75

XP_063128016.1

EC 3.4.21.75

XP_063128021.1

EC 3.4.21.75

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_019331.2 → NP_062204.2 furin precursor

Status: PROVISIONAL

Source sequence(s)

JAXUCZ010000001

UniProtKB/Swiss-Prot

P23377

UniProtKB/TrEMBL

A6JCC0, G3V7I9

Related

ENSRNOP00000015521.1, ENSRNOT00000015521.3

Conserved Domains (4) summary

cd04059
Location:113 → 402

Peptidases_S8_Protein_convertases_Kexins_Furin-lik; Peptidase S8 family domain in Protein convertases

smart00261
Location:638 → 675

FU; Furin-like repeats

pfam01483
Location:484 → 570

P_proprotein; Proprotein convertase P-domain

pfam16470
Location:33 → 107

S8_pro-domain; Peptidase S8 pro-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_086019.1 Reference GRCr8

Range

143757389..143770430 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_008759555.4 → XP_008757777.1 furin isoform X1

See identical proteins and their annotated locations for XP_008757777.1

UniProtKB/Swiss-Prot

P23377

UniProtKB/TrEMBL

A6JCC0, G3V7I9

Related

ENSRNOP00000088681.1

Conserved Domains (4) summary

cd04059
Location:113 → 402

Peptidases_S8_Protein_convertases_Kexins_Furin-lik; Peptidase S8 family domain in Protein convertases

smart00261
Location:638 → 675

FU; Furin-like repeats

pfam01483
Location:484 → 570

P_proprotein; Proprotein convertase P-domain

pfam16470
Location:33 → 107

S8_pro-domain; Peptidase S8 pro-domain
XM_063271951.1 → XP_063128021.1 furin isoform X1

UniProtKB/TrEMBL

A6JCC0, G3V7I9
XM_063271946.1 → XP_063128016.1 furin isoform X1

UniProtKB/TrEMBL

A6JCC0, G3V7I9