Serpina12 serine (or cysteine) peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Serpina12provided by MGI
Official Full Name: serine (or cysteine) peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12provided by MGI
Primary source: MGI:MGI:1915304
See related: Ensembl:ENSMUSG00000041567 AllianceGenome:MGI:1915304
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 4632419J12Rik
Summary: Predicted to enable serine-type endopeptidase inhibitor activity. Acts upstream of or within negative regulation of gluconeogenesis; positive regulation of signal transduction; and regulation of lipid metabolic process. Located in extracellular space and plasma membrane. Is expressed in back skin. Orthologous to human SERPINA12 (serpin family A member 12). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Low expression observed in reference dataset See more
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Genomic context

Location:: 12 E; 12 53.05 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	12	NC_000078.7 (103995028..104010702, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	12	NC_000078.6 (104028769..104044443, complement)

Chromosome 12 - NC_000078.7 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SERPINA12 promotes the tumorigenic capacity of HCC stem cells through hyperactivation of AKT/beta-catenin signaling.
Title: SERPINA12 promotes the tumorigenic capacity of HCC stem cells through hyperactivation of AKT/β-catenin signaling.
A Vaspin-HSPA1L complex protects proximal tubular cells from organelle stress in diabetic kidney disease.
Title: A Vaspin-HSPA1L complex protects proximal tubular cells from organelle stress in diabetic kidney disease.
VASPIN reduces inflammation and endoplasmic reticulum stress of renal tubular epithelial cells by inhibiting HMGB1 and relieves renal ischemia-reperfusion injury.
Title: VASPIN reduces inflammation and endoplasmic reticulum stress of renal tubular epithelial cells by inhibiting HMGB1 and relieves renal ischemia-reperfusion injury.
Insulin induces expression of the hepatic vaspin gene.
Title: Insulin induces expression of the hepatic vaspin gene.
These findings indicate that vaspin is prone to osteoporosis protection.
Title: Vaspin protects mouse mesenchymal stem cells from oxidative stress-induced apoptosis through the MAPK/p38 pathway.
These results suggest that C/EBPalpha positively regulates hepatic vaspin expression through two functional CEBPREs. Thus, vaspin is a novel C/EBPalpha target gene in the liver.
Title: Vaspin is a novel target gene of hepatic CCAAT-enhancer-binding protein.
Vaspin mRNA and protein expression is increased in brown adipose tissue of cold-exposed and high-fat fed mice.
Title: Brown adipose tissue (BAT) specific vaspin expression is increased after obesogenic diets and cold exposure and linked to acute changes in DNA-methylation.
Vaspin overexpression reduces ischaemia/reperfusion - induced myocardial apoptosis in mice.
Title: Vaspin alleviates myocardial ischaemia/reperfusion injury via activating autophagic flux and restoring lysosomal function.
The results of the current study indicated that vaspin inhibited the progression of atherosclerotic plaques in apoE(/) mice by inhibiting endoplasmic reticulum stress-induced macrophage apoptosis.
Title: Vaspin attenuates the progression of atherosclerosis by inhibiting ER stress-induced macrophage apoptosis in apoE‑/‑ mice.
Vaspin inhibited RANKL-induced osteoclastogenesis in RAW264.7 cells and bone marrow cells.
Title: Vaspin attenuates RANKL-induced osteoclast formation in RAW264.7 cells.

Submit: New GeneRIF Correction See all GeneRIFs (13)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (2) 1 citation
Endonuclease-mediated (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Serpina12 (e-PCR), detects polymorphism
- UniSTS:502671

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables molecular function inhibitor activity	ISO Inferred from Sequence Orthology more info
enables peptidase inhibitor activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables serine-type endopeptidase inhibitor activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
acts_upstream_of gluconeogenesis	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of lipid biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of endopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within negative regulation of gluconeogenesis	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within negative regulation of lipid biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within negative regulation of peptidase activity	IEA Inferred from Electronic Annotation more info
acts_upstream_of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within positive regulation of insulin receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within regulation of cholesterol metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within regulation of triglyceride metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: serpin A12

Names: serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 12; vaspin; visceral adipose tissue-derived serine protease inhibitor; visceral adipose-specific SERPIN

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_026535.2 → NP_080811.1 serpin A12 precursor

See identical proteins and their annotated locations for NP_080811.1

Status: PROVISIONAL

Source sequence(s)

AC134902

Consensus CDS

CCDS26145.1

UniProtKB/Swiss-Prot

Q7TMF5, Q9CQ32

UniProtKB/TrEMBL

Q6P6M3

Related

ENSMUSP00000045572.4, ENSMUST00000043915.4

Conserved Domains (1) summary

cd02056
Location:51 → 408

alpha-1-antitrypsin_like; alpha-1-antitrypsin_like. This family contains a variety of different members of clade A of the serpin superfamily. They include the classical serine proteinase inhibitors, alpha-1-antitrypsin and alpha-1-antichymotrypsin, protein C inhibitor, ...