ID   AMY1_MOUSE              Reviewed;         511 AA.
AC   P00687; Q921Y7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 199.
DE   RecName: Full=Alpha-amylase 1;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase 1;
DE   AltName: Full=Salivary and hepatic alpha-amylase;
DE   Flags: Precursor;
GN   Name=Amy1; Synonyms=Amy-1-a, Amy1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=6157477; DOI=10.1016/0092-8674(80)90125-7;
RA   Hagenbuechle O., Bovey R., Young R.A.;
RT   "Tissue-specific expression of mouse-alpha-amylase genes: nucleotide
RT   sequence of isoenzyme mRNAs from pancreas and salivary gland.";
RL   Cell 21:179-187(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver, and Salivary gland;
RX   PubMed=6162108; DOI=10.1038/289643a0;
RA   Hagenbuechle O., Tosi M., Schibler U., Bovey R., Wellauer P.K., Young R.A.;
RT   "Mouse liver and salivary gland alpha-amylase mRNAs differ only in 5' non-
RT   translated sequences.";
RL   Nature 289:643-646(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RC   STRAIN=A/J; TISSUE=Liver, and Salivary gland;
RX   PubMed=6162570; DOI=10.1016/0092-8674(81)90140-9;
RA   Young R.A., Hagenbuechle O., Schibler U.;
RT   "A single mouse alpha-amylase gene specifies two different tissue-specific
RT   mRNAs.";
RL   Cell 23:451-458(1981).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-292.
RC   STRAIN=A/J; TISSUE=Liver, and Salivary gland;
RX   PubMed=6176715; DOI=10.1016/0022-2836(82)90004-3;
RA   Schibler U., Pittet A.-C., Young R.A., Hagenbuechle O., Tosi M.,
RA   Gellman S., Wellauer P.K.;
RT   "The mouse alpha-amylase multigene family. Sequence organization of members
RT   expressed in the pancreas, salivary gland and liver.";
RL   J. Mol. Biol. 155:247-266(1982).
RN   [8]
RP   SIGNAL SEQUENCE CLEAVAGE SITE, AND PYROGLUTAMATE FORMATION AT GLN-16.
RA   Karn R.C., Petersen T.E., Hjorth J.P., Nieles J.T., Roepstorff P.;
RT   "Characterization of the amino termini of mouse salivary and pancreatic
RT   amylases.";
RL   FEBS Lett. 126:292-296(1981).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P04746};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P04746};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in liver and saliva.
CC   -!- MISCELLANEOUS: Hepatic and salivary alpha-amylases are encoded by the
CC       same gene; however, their mRNAs have different 5'-UTR sequences.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; J00356; AAA37221.1; -; mRNA.
DR   EMBL; V00717; CAA24097.1; -; mRNA.
DR   EMBL; V00719; CAA24099.1; -; mRNA.
DR   EMBL; V00720; CAA24100.1; -; mRNA.
DR   EMBL; AK029642; BAC26543.1; -; mRNA.
DR   EMBL; CH466532; EDL12410.1; -; Genomic_DNA.
DR   EMBL; CH466532; EDL12411.1; -; Genomic_DNA.
DR   EMBL; CH466532; EDL12412.1; -; Genomic_DNA.
DR   EMBL; BC009121; AAH09121.1; -; mRNA.
DR   EMBL; J00353; AAA37219.1; -; Genomic_DNA.
DR   EMBL; J00354; AAA37220.1; -; Genomic_DNA.
DR   CCDS; CCDS17776.1; -.
DR   PIR; A90798; ALMSS.
DR   RefSeq; NP_001103975.1; NM_001110505.1.
DR   RefSeq; NP_031472.2; NM_007446.2.
DR   AlphaFoldDB; P00687; -.
DR   SMR; P00687; -.
DR   BioGRID; 198093; 2.
DR   FunCoup; P00687; 184.
DR   IntAct; P00687; 16.
DR   STRING; 10090.ENSMUSP00000070368; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GlyGen; P00687; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P00687; -.
DR   PhosphoSitePlus; P00687; -.
DR   SwissPalm; P00687; -.
DR   CPTAC; non-CPTAC-3761; -.
DR   jPOST; P00687; -.
DR   PaxDb; 10090-ENSMUSP00000070368; -.
DR   PeptideAtlas; P00687; -.
DR   ProteomicsDB; 282085; -.
DR   Pumba; P00687; -.
DR   DNASU; 11722; -.
DR   Ensembl; ENSMUST00000067980.12; ENSMUSP00000070368.6; ENSMUSG00000074264.13.
DR   Ensembl; ENSMUST00000106540.8; ENSMUSP00000102150.2; ENSMUSG00000074264.13.
DR   GeneID; 11722; -.
DR   KEGG; mmu:11722; -.
DR   UCSC; uc008rba.2; mouse.
DR   AGR; MGI:88019; -.
DR   CTD; 11722; -.
DR   MGI; MGI:88019; Amy1.
DR   VEuPathDB; HostDB:ENSMUSG00000074264; -.
DR   eggNOG; KOG2212; Eukaryota.
DR   GeneTree; ENSGT00940000163518; -.
DR   HOGENOM; CLU_013336_2_1_1; -.
DR   InParanoid; P00687; -.
DR   OMA; FRYAYDL; -.
DR   OrthoDB; 550577at2759; -.
DR   PhylomeDB; P00687; -.
DR   Reactome; R-MMU-189085; Digestion of dietary carbohydrate.
DR   BioGRID-ORCS; 11722; 0 hits in 78 CRISPR screens.
DR   PRO; PR:P00687; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P00687; protein.
DR   Bgee; ENSMUSG00000074264; Expressed in parotid gland and 210 other cell types or tissues.
DR   ExpressionAtlas; P00687; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB.
DR   GO; GO:0016160; F:amylase activity; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISO:GO_Central.
DR   GO; GO:0031404; F:chloride ion binding; ISO:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   FunFam; 2.60.40.1180:FF:000020; Pancreatic alpha-amylase; 1.
DR   FunFam; 3.20.20.80:FF:000056; Pancreatic alpha-amylase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; Glycosidase;
KW   Hydrolase; Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|Ref.8"
FT   CHAIN           16..511
FT                   /note="Alpha-amylase 1"
FT                   /id="PRO_0000001403"
FT   ACT_SITE        212
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         115
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         182
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         210
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         313
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   BINDING         352
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   SITE            315
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   MOD_RES         16
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|Ref.8"
FT   DISULFID        43..101
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        85..130
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        156..175
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        393..399
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   DISULFID        465..477
FT                   /evidence="ECO:0000250|UniProtKB:P04746"
FT   CONFLICT        29
FT                   /note="V -> I (in Ref. 1; AAA37221/CAA24097, 2;
FT                   CAA24099/CAA24100 and 6; AAA37219)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="L -> Q (in Ref. 2; CAA24099/CAA24100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="F -> L (in Ref. 1; AAA37221/CAA24097 and 2;
FT                   CAA24099/CAA24100)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  57644 MW;  CC5399F4C23E1105 CRC64;
     MKFFLLLSLI GFCWAQYDPH TQYGRTAIVH LFEWRWVDIA KECERYLAPN GFAGVQVSPP
     NENIVVHSPS RPWWERYQPI SYKICSRSGN EDEFRDMVNR CNNVGVRIYV DAVINHMCGV
     GAQAGQSSTC GSYFNPNNRD FPGVPYSGFD FNDGKCRTAS GGIENYQDAA QVRDCRLSGL
     LDLALEKDYV RTKVADYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNTKWFSQG
     SRPFIFQEVI DLGGEAVSSN EYFGNGRVTE FKYGAKLGKV MRKWDGEKMS YLKNWGEGWG
     LMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYYWP
     RNFQNGKDVN DWVGPPNNNG KTKEVSINPD STCGNDWICE HRWRQIRNMV AFRNVVNGQP
     FANWWDNDSN QVAFGRGNKG FIVFNNDDWA LSETLQTGLP AGTYCDVISG DKVDGNCTGI
     KVYVGNDGKA HFSISNSAED PFIAIHAESK I
//