AMY1_MOUSE
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 03-AUG-2022, entry version 184.
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 IntAct; P00687; 16.
DR STRING; 10090.ENSMUSP00000070368; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; P00687; -.
DR PhosphoSitePlus; P00687; -.
DR CPTAC; non-CPTAC-3761; -.
DR jPOST; P00687; -.
DR MaxQB; P00687; -.
DR PaxDb; P00687; -.
DR PeptideAtlas; P00687; -.
DR PRIDE; P00687; -.
DR ProteomicsDB; 282085; -.
DR DNASU; 11722; -.
DR Ensembl; ENSMUST00000067980; ENSMUSP00000070368; ENSMUSG00000074264.
DR Ensembl; ENSMUST00000106540; ENSMUSP00000102150; ENSMUSG00000074264.
DR GeneID; 11722; -.
DR KEGG; mmu:11722; -.
DR UCSC; uc008rba.2; mouse.
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; 665362at2759; -.
DR PhylomeDB; P00687; -.
DR TreeFam; TF312850; -.
DR Reactome; R-MMU-189085; Digestion of dietary carbohydrate.
DR BioGRID-ORCS; 11722; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Amy1; mouse.
DR PRO; PR:P00687; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P00687; protein.
DR Bgee; ENSMUSG00000074264; Expressed in parotid gland and 209 other tissues.
DR ExpressionAtlas; P00687; baseline and differential.
DR Genevisible; P00687; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004556; F:alpha-amylase activity; ISO:MGI.
DR GO; GO:0016160; F:amylase activity; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; SSF51445; 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; CAA24099/
FT 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
