LOCUS       NP_001010970             521 aa            linear   ROD 17-JUL-2023
DEFINITION  alpha-amylase 1 precursor [Rattus norvegicus].
ACCESSION   NP_001010970 XP_579333
VERSION     NP_001010970.1
DBSOURCE    REFSEQ: accession NM_001010970.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Mutlu A, Ozturk M, Akpinar G, Kasap M and Kanli A.
  TITLE     Proteomics analysis of pleomorphic adenoma of the human parotid
            gland
  JOURNAL   Eur Arch Otorhinolaryngol 274 (8), 3183-3195 (2017)
   PUBMED   28497265
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Chen,L.H., Yang,Z.M. and Chen,W.W.
  TITLE     Parallel increase in secretory activity between N-glycosylated and
            nonglycosylated alpha-amylase without protein synthesis after
            short-term beta-adrenergic receptor activation in isolated rat
            parotid acinar cells
  JOURNAL   Anal Quant Cytopathol Histpathol 36 (5), 279-284 (2014)
   PUBMED   25804000
  REMARK    GeneRIF: Our findings suggest a parallel increase in secretory
            activity between N-glycosylated and nonglycosylated a-amylase after
            b-adrenergic receptor activation.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Archambaud C, Nahori MA, Soubigou G, Becavin C, Laval L, Lechat P,
            Smokvina T, Langella P, Lecuit M and Cossart P.
  TITLE     Impact of lactobacilli on orally acquired listeriosis
  JOURNAL   Proc Natl Acad Sci U S A 109 (41), 16684-16689 (2012)
   PUBMED   23012479
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Chang M, Alsaigh T, Kistler EB and Schmid-Schonbein GW.
  TITLE     Breakdown of mucin as barrier to digestive enzymes in the ischemic
            rat small intestine
  JOURNAL   PLoS One 7 (6), e40087 (2012)
   PUBMED   22768227
  REMARK    GeneRIF: 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.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Imai A, Yoshie S, Ishibashi K, Haga-Tsujimura M, Nashida T,
            Shimomura H and Fukuda M.
  TITLE     EPI64 protein functions as a physiological GTPase-activating
            protein for Rab27 protein and regulates amylase release in rat
            parotid acinar cells
  JOURNAL   J Biol Chem 286 (39), 33854-33862 (2011)
   PUBMED   21832089
  REMARK    GeneRIF: 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.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Venkatesh SG, Tan J, Gorr SU and Darling DS.
  TITLE     Isoproterenol increases sorting of parotid gland cargo proteins to
            the basolateral pathway
  JOURNAL   Am J Physiol Cell Physiol 293 (2), C558-C565 (2007)
   PUBMED   17537806
  REMARK    GeneRIF: Increased salivary amylase was detected in sera of
            isoproterenol-treated animals, suggesting increased routing of the
            regulated secretory proteins to the basolateral pathway.
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Youssef R, Malaisse WJ, Courtois P and Sener A.
  TITLE     Alteration of alpha-amylase secretion from rat parotid cells in the
            absence of extracellular bicarbonate
  JOURNAL   Int J Mol Med 12 (2), 199-200 (2003)
   PUBMED   12851717
  REMARK    GeneRIF: 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
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Sierra,F., Pittet,A.C. and Schibler,U.
  TITLE     Different tissue-specific expression of the amylase gene Amy-1 in
            mice and rats
  JOURNAL   Mol Cell Biol 6 (11), 4067-4076 (1986)
   PUBMED   3025629
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Bloor,J.H. and Meisler,M.H.
  TITLE     Additional evidence for the close linkage of amy-1 and amy-2 in the
            mouse
  JOURNAL   J Hered 71 (6), 449-451 (1980)
   PUBMED   6163812
REFERENCE   10 (residues 1 to 521)
  AUTHORS   MacDonald,R.J., Crerar,M.M., Swain,W.F., Pictet,R.L., Thomas,G. and
            Rutter,W.J.
  TITLE     Structure of a family of rat amylase genes
  JOURNAL   Nature 287 (5778), 117-122 (1980)
   PUBMED   6159531
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB057450.1.
            
            On Apr 19, 2005 this sequence version replaced XP_579333.1.
            
            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 :: AB057450.1, FQ219213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760400, SAMEA5760476
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="2"
                     /map="2q42"
     Protein         1..521
                     /product="alpha-amylase 1 precursor"
                     /EC_number="3.2.1.1"
                     /note="amylase 1, salivary; alpha-amylase 1; amylase,
                     alpha 1A (salivary)"
                     /calculated_mol_wt=55765
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=3084
     Region          35..426
                     /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"
     Site            order(83..84,87..88,123,126,187..190,220,222..223,
                     225..226,258,260,265,324..325,330)
                     /site_type="active"
                     /db_xref="CDD:200456"
     Site            order(125,192)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:200456"
     Site            order(222,258,325)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200456"
     Region          432..520
                     /region_name="Aamy_C"
                     /note="Aamy_C domain; smart00632"
                     /db_xref="CDD:214749"
     CDS             1..521
                     /gene="Amy1"
                     /gene_synonym="Amy1a"
                     /coded_by="NM_001010970.1:47..1612"
                     /db_xref="GeneID:24203"
                     /db_xref="RGD:2113"
ORIGIN      
        1 mreycqhhsr mkfflllsli glcwaqydph tfygrssivh lfewrwvdia kecerylapn
       61 gfggvqvspp nenivvnspf rpwweryqpi sykicsrsgn edefrdmvnr cnnvgvriyv
      121 davinhmcgv gaeagqsstc gsyfnpnnrd fpgvpysgfd fndgkcktgs ggienyndaa
      181 qvrdcrlsgl ldlalekdyv rtkvadymnh lidigvagfr ldaskhmwpg dikavldklh
      241 nlntkwfseg skpfiyqevi dlggeavssn eyfgngrvte fkygaklgkv lrkwdgekma
      301 ylknwgegwg fmpsdralvf vdnhdnqrgh gaggssiltf wdarlykmav gfmlahpygf
      361 trvmssfhwp ryfengkdvn dwvgppnnng atkevtinsd stcgndwvce hrwrqirnmv
      421 afrnvvngqp fanwwdngsn qvafgrgnkg fivfnnddwd lsttlqtglp agtycdvisg
      481 dkvdgnctgi kvyvgsdgna yfsisnsaed pfiaihvesk i
//
