Amy1 amylase alpha 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Amy1provided by RGD
Official Full Name: amylase alpha 1provided by RGD
Primary source: RGD:2113
See related: EnsemblRapid:ENSRNOG00000064517 AllianceGenome:RGD:2113
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: Amy1a
Summary: Predicted to enable alpha-amylase activity. Predicted to be involved in carbohydrate metabolic process. Located in extracellular space. Orthologous to several human genes including AMY2B (amylase alpha 2B). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Liver (RPKM 2325.4) and Spleen (RPKM 717.1) See more
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Genomic context

Location:: 2q42

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (204071101..204085910, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (201382678..201397487, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (216428709..216443518, complement)

Chromosome 2 - NC_086020.1 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?

Our findings suggest a parallel increase in secretory activity between N-glycosylated and nonglycosylated a-amylase after b-adrenergic receptor activation.
Title: Parallel increase in secretory activity between N-glycosylated and nonglycosylated α-amylase without protein synthesis after short-term β-adrenergic receptor activation in isolated rat parotid acinar cells.
These results indicate that mucin plays an important role in the preservation of the mucosal barrier and that ischemia but not digestive enzymes disturbs mucin integrity, while digestive enzymes actively mediate epithelial cell disruption.
Title: Breakdown of mucin as barrier to digestive enzymes in the ischemic rat small intestine.
EPI64 acted as a physiological Rab27-GAP that enhanced GTPase activity of Rab27 in response to IPR stimulation, and that this activity is required for IPR-induced amylase release.
Title: EPI64 protein functions as a physiological GTPase-activating protein for Rab27 protein and regulates amylase release in rat parotid acinar cells.
Amylase-positive cells constitute an additional subset of taste receptor cells also associated with chemoreceptorial and/or secretory molecules, confirming the occurrence of various pathways in taste buds.
Title: Amylase expression in taste receptor cells of rat circumvallate papillae.
Increased salivary amylase was detected in sera of isoproterenol-treated animals, suggesting increased routing of the regulated secretory proteins to the basolateral pathway.
Title: Isoproterenol increases sorting of parotid gland cargo proteins to the basolateral pathway.
the HCO3-anion participates in the secretory sequence at sites distal to the identification of secretagogues in both endocrine and exocrine cells, the absence of extracellular bicarbonate is shown to decrease by about 50% basal alpha-amylase secretion
Title: Alteration of alpha-amylase secretion from rat parotid cells in the absence of extracellular bicarbonate.

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General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables alpha-amylase activity	IBA Inferred from Biological aspect of Ancestor more info
enables alpha-amylase activity	TAS Traceable Author Statement more info	PubMed
enables amylase activity	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in carbohydrate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to bacterium	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
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: alpha-amylase 1

Names: amylase 1, salivary; amylase, alpha 1A (salivary)

NP_001010970.1

EC 3.2.1.1

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_001010970.1 → NP_001010970.1 alpha-amylase 1 precursor

See identical proteins and their annotated locations for NP_001010970.1

Status: PROVISIONAL

Source sequence(s)

AB057450

UniProtKB/TrEMBL

A0A8I6A5R3, A6HV62, A6HV63, Q99N59

Related

ENSRNOP00000088062.1, ENSRNOT00000098690.2

Conserved Domains (3) summary

cd11317
Location:35 → 426

AmyAc_bac_euk_AmyA; Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase)

smart00632
Location:432 → 520

Aamy_C; Aamy_C domain

COG0366
Location:56 → 325

AmyA; Glycosidase [Carbohydrate transport and metabolism]