MASCOT Search Results
Protein View: NP_004029.2
alpha-amylase 1 precursor [Homo sapiens]
LOCUS NP_004029 511 aa linear PRI 06-OCT-2016
DEFINITION alpha-amylase 1 precursor [Homo sapiens].
ACCESSION NP_004029 XP_001127960
VERSION NP_004029.2
DBSOURCE REFSEQ: accession NM_004038.3
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 511)
AUTHORS Nater UM, La Marca R, Erni K and Ehlert U.
TITLE Alpha-Amylase Activity in Blood Increases after Pharmacological,
But Not Psychological, Activation of the Adrenergic System
JOURNAL PLoS ONE 10 (6), E0130449 (2015)
PUBMED 26110636
REMARK GeneRIF: Alpha-amylase in blood increases after pharmacological
activation of the adrenergic pathways suggesting that sympathetic
receptors are responsible for these changes. Psychological stress,
however, does not seem to have an impact on alpha-amylase in blood
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 511)
AUTHORS Edmonds R, Burkett B, Leicht A and McKean M.
TITLE Effect of chronic training on heart rate variability, salivary IgA
and salivary alpha-amylase in elite swimmers with a disability
JOURNAL PLoS ONE 10 (6), E0127749 (2015)
PUBMED 26043224
REMARK GeneRIF: The purpose of this study was to a) determine the heart
rate variability (HRV) and saliva markers of immunity (salivary
immunoglobulin A; sIgA) and stress (salivary alpha-amylase; sAA)
responses to chronic training in elite swimmers with a disability.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 511)
AUTHORS Yang,Z., Lin,J., Chen,L., Zhang,M., Yang,X. and Chen,W.
TITLE Influences of AMY1 gene copy number and protein expression on
salivary alpha-amylase activity before and after citric acid
stimulation in splenic asthenia children
JOURNAL J Tradit Chin Med 35 (3), 266-272 (2015)
PUBMED 26237829
REMARK GeneRIF: Splenic asthenia children had positive correlations
between AMY1 copy number and sAA activity before or after citric
acid stimulation.
REFERENCE 4 (residues 1 to 511)
AUTHORS Chen LH, Yang ZM, Chen WW, Lin J, Zhang M, Yang XR and Zhao LB.
TITLE Attenuated acute salivary alpha-amylase responses to gustatory
stimulation with citric acid in thin children
JOURNAL Br. J. Nutr. 113 (7), 1078-1085 (2015)
PUBMED 25784372
REMARK GeneRIF: genetic association study in population in China: Data
suggest that copy number variation of AMY1A gene is not associated
with down-regulation of salivary response in thin children as
compared to salivary response in normal weight children.
REFERENCE 5 (residues 1 to 511)
AUTHORS Zheng,R., Zhang,J., Ying,Z. and Zheng,N.
TITLE Low Serum Amylase is Associated with Gestational Diabetes Mellitus
in Chinese Pregnant Women
JOURNAL Clin. Lab. 61 (10), 1423-1428 (2015)
PUBMED 26642703
REMARK GeneRIF: low serum amylase level is significantly associated with
increased risk of gestational diabetes mellitus
REFERENCE 6 (residues 1 to 511)
AUTHORS Bank RA, Hettema EH, Arwert F, Amerongen AV and Pronk JC.
TITLE Electrophoretic characterization of posttranslational modifications
of human parotid salivary alpha-amylase
JOURNAL Electrophoresis 12 (1), 74-79 (1991)
PUBMED 1710976
REFERENCE 7 (residues 1 to 511)
AUTHORS Groot PC, Mager WH, Henriquez NV, Pronk JC, Arwert F, Planta RJ,
Eriksson AW and Frants RR.
TITLE Evolution of the human alpha-amylase multigene family through
unequal, homologous, and inter- and intrachromosomal crossovers
JOURNAL Genomics 8 (1), 97-105 (1990)
PUBMED 2081604
REFERENCE 8 (residues 1 to 511)
AUTHORS Handy,D.E., Larsen,S.H., Karn,R.C. and Hodes,M.E.
TITLE Identification of a human salivary amylase gene. Partial sequence
of genomic DNA suggests a mode of regulation different from that of
mouse, Amy1
JOURNAL Mol. Biol. Med. 4 (3), 145-155 (1987)
PUBMED 2442579
REFERENCE 9 (residues 1 to 511)
AUTHORS Davis,M.M., Hodes,M.E., Munsick,R.A., Ulbright,T.M. and
Goldstein,D.J.
TITLE Pancreatic amylase expression in human pancreatic development
JOURNAL Hybridoma 5 (2), 137-145 (1986)
PUBMED 2424823
REFERENCE 10 (residues 1 to 511)
AUTHORS Nishide,T., Nakamura,Y., Emi,M., Yamamoto,T., Ogawa,M., Mori,T. and
Matsubara,K.
TITLE Primary structure of human salivary alpha-amylase gene
JOURNAL Gene 41 (2-3), 299-304 (1986)
PUBMED 2423416
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from CB956272.1, BC063129.1 and
BC070302.1.
On or before Sep 20, 2006 this sequence version replaced
gi:113412273, gi:4757750.
Summary: Amylases are secreted proteins that hydrolyze
1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides,
and thus catalyze the first step in digestion of dietary starch and
glycogen. The human genome has a cluster of several amylase genes
that are expressed at high levels in either salivary gland or
pancreas. This gene encodes an amylase isoenzyme produced by the
salivary gland. Alternative splicing results in multiple transcript
variants encoding the same protein. [provided by RefSeq, Jul 2008].
Transcript Variant: This variant (1) represents the longer
transcript. Variants 1 and 2 encode the same protein.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: BC070302.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA1968832, SAMEA2142853
[ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..511
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="1"
/map="1p21.1"
Protein 1..511
/product="alpha-amylase 1 precursor"
/EC_number="3.2.1.1"
/note="glycogenase; amylase, salivary, alpha-1A; salivary
amylase alpha 1A; alpha-amylase 1; salivary alpha-amylase;
1,4-alpha-D-glucan glucanohydrolase 1"
sig_peptide 1..15
/inference="COORDINATES: ab initio prediction:SignalP:4.0"
/calculated_mol_wt=1876
mat_peptide 16..511
/product="alpha-amylase 1"
/calculated_mol_wt=55910
Site 16
/site_type="other"
/experiment="experimental evidence, no additional details
recorded"
/note=". {ECO:0000250|UniProtKB:P00687}; propagated from
UniProtKB/Swiss-Prot (P04745.2)"
Region 25..416
/region_name="AmyAc_bac_euk_AmyA"
/note="Alpha amylase catalytic domain found in bacterial
and eukaryotic Alpha amylases (also called
1,4-alpha-D-glucan-4-glucanohydrolase); cd11317"
/db_xref="CDD:200456"
Region 46..>315
/region_name="AmyA"
/note="Glycosidase [Carbohydrate transport and
metabolism]; COG0366"
/db_xref="CDD:223443"
Site order(73..74,77..78,113,116,177..180,210,212..213,
215..216,248,250,255,314..315,320)
/site_type="active"
/db_xref="CDD:200456"
Site order(115,182)
/site_type="other"
/note="Ca binding site [ion binding]"
/db_xref="CDD:200456"
Site order(212,248,315)
/site_type="active"
/note="catalytic site [active]"
/db_xref="CDD:200456"
Site 315
/site_type="other"
/experiment="experimental evidence, no additional details
recorded"
/note="Transition state stabilizer.
{ECO:0000250|UniProtKB:P04746}; propagated from
UniProtKB/Swiss-Prot (P04745.2)"
Site 365
/site_type="amidation"
/experiment="experimental evidence, no additional details
recorded"
/note="Deamidated asparagine, partial.
{ECO:0000269|PubMed:1710976}; propagated from
UniProtKB/Swiss-Prot (P04745.2)"
Region 422..510
/region_name="Aamy_C"
/note="Aamy_C domain; smart00632"
/db_xref="CDD:214749"
Site 427
/site_type="amidation"
/experiment="experimental evidence, no additional details
recorded"
/note="Deamidated asparagine, partial, alternate.
{ECO:0000269|PubMed:1710976}; propagated from
UniProtKB/Swiss-Prot (P04745.2)"
Site 474
/site_type="amidation"
/experiment="experimental evidence, no additional details
recorded"
/note="Deamidated asparagine, partial.
{ECO:0000269|PubMed:1710976}; propagated from
UniProtKB/Swiss-Prot (P04745.2)"
CDS 1..511
/gene="AMY1A"
/gene_synonym="AMY1"
/coded_by="NM_004038.3:296..1831"
/db_xref="CCDS:CCDS30782.1"
/db_xref="GeneID:276"
/db_xref="HGNC:HGNC:474"
/db_xref="MIM:104700"