AMYP_MOUSE
ID AMYP_MOUSE Reviewed; 508 AA.
AC P00688; Q4VBW6; Q61295; Q61296; Q64301;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Pancreatic alpha-amylase;
DE Short=PA;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=Amy2; Synonyms=Amy2a;
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 [GENOMIC DNA].
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] (ISOZYMES A1; B(A) AND B(C)).
RC STRAIN=CE/J;
RX PubMed=6098446; DOI=10.1002/j.1460-2075.1984.tb02213.x;
RA Tosi M., Bovey R., Astolfi S., Bodary S., Meisler M.H., Wellauer P.K.;
RT "Multiple non-allelic genes encoding pancreatic alpha-amylase of mouse are
RT expressed in a strain-specific fashion.";
RL EMBO J. 3:2809-2816(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
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 MRNA].
RC TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 AND 267-290.
RC STRAIN=A/J;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
RX PubMed=2987507; DOI=10.1016/0022-2836(85)90022-1;
RA Bodary S., Grossi G., Hagenbuechle O., Wellauer P.K.;
RT "Members of the Amy-2 alpha-amylase gene family of mouse strain CE/J
RT contain duplicated 5' termini.";
RL J. Mol. Biol. 182:1-10(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 (ISOZYMES AMY-2.1Y AND AMY-2.2Y).
RX PubMed=2436036; DOI=10.1128/mcb.7.1.326-334.1987;
RA Osborn L., Rosenberg M.P., Keller S.A., Meisler M.H.;
RT "Tissue-specific and insulin-dependent expression of a pancreatic amylase
RT gene in transgenic mice.";
RL Mol. Cell. Biol. 7:326-334(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 267-289 AND 388-470 (ISOZYMES
RP A1 AND B1).
RC STRAIN=YRB/KI;
RX PubMed=2414282; DOI=10.1016/s0021-9258(17)38747-1;
RA Gumucio D.L., Wiebauer K., Dranginis A., Samuelson L.C., Treisman L.O.,
RA Caldwell R.M., Antonucci T.K., Meisler M.H.;
RT "Evolution of the amylase multigene family. YBR/Ki mice express a
RT pancreatic amylase gene which is silent in other strains.";
RL J. Biol. Chem. 260:13483-13489(1985).
RN [9]
RP SIGNAL SEQUENCE CLEAVAGE SITE, AND PYROGLUTAMATE FORMATION AT GLN-16.
RX PubMed=6165618; DOI=10.1016/0014-5793(81)80264-5;
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. 126:293-296(1981).
RN [10]
RP PROTEIN SEQUENCE OF 407-458.
RC STRAIN=YBR;
RX PubMed=6180955; DOI=10.1093/genetics/101.1.91;
RA Strahler J.R., Meisler M.;
RT "Two distinct pancreatic amylase genes are active in YBR mice.";
RL Genetics 101:91-102(1982).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] MET-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
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, extracellular space.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; V00718; CAA24098.1; -; mRNA.
DR EMBL; X02576; CAA26413.1; -; mRNA.
DR EMBL; X02577; CAA26414.1; -; mRNA.
DR EMBL; X02578; CAA26415.1; -; mRNA.
DR EMBL; AK133526; BAE21706.1; -; mRNA.
DR EMBL; BC094924; AAH94924.1; -; mRNA.
DR EMBL; BC100579; AAI00580.1; -; mRNA.
DR EMBL; J00357; AAA37228.1; -; Genomic_DNA.
DR EMBL; J00358; AAA37229.1; -; Genomic_DNA.
DR EMBL; J00361; AAA37233.1; -; Genomic_DNA.
DR EMBL; X02343; CAA26202.1; -; Genomic_DNA.
DR EMBL; M16540; AAA37223.1; -; Genomic_DNA.
DR EMBL; M15965; AAA37226.1; -; Genomic_DNA.
DR EMBL; M11895; AAA37224.1; -; mRNA.
DR EMBL; M11896; AAA37227.1; -; mRNA.
DR EMBL; M11891; AAA37222.1; -; Genomic_DNA.
DR CCDS; CCDS17775.1; -.
DR PIR; A90995; ALMSP1.
DR PIR; B90798; ALMSP.
DR PIR; B90995; ALMSPC.
DR PIR; C90995; ALMSPA.
DR PIR; I49493; I49493.
DR PIR; I49494; I49494.
DR RefSeq; NP_001036176.1; NM_001042711.2.
DR RefSeq; NP_001153622.1; NM_001160150.1.
DR RefSeq; NP_001153623.1; NM_001160151.1.
DR RefSeq; NP_001153624.1; NM_001160152.1.
DR AlphaFoldDB; P00688; -.
DR SMR; P00688; -.
DR STRING; 10090.ENSMUSP00000096264; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; P00688; -.
DR PhosphoSitePlus; P00688; -.
DR SWISS-2DPAGE; P00688; -.
DR CPTAC; non-CPTAC-3891; -.
DR jPOST; P00688; -.
DR MaxQB; P00688; -.
DR PaxDb; P00688; -.
DR PeptideAtlas; P00688; -.
DR PRIDE; P00688; -.
DR ProteomicsDB; 282086; -.
DR DNASU; 109959; -.
DR Ensembl; ENSMUST00000098667; ENSMUSP00000096264; ENSMUSG00000096569.
DR Ensembl; ENSMUST00000098673; ENSMUSP00000096270; ENSMUSG00000074268.
DR Ensembl; ENSMUST00000179314; ENSMUSP00000136894; ENSMUSG00000093931.
DR Ensembl; ENSMUST00000179568; ENSMUSP00000137025; ENSMUSG00000096770.
DR GeneID; 100043684; -.
DR GeneID; 100043686; -.
DR GeneID; 100043688; -.
DR GeneID; 109959; -.
DR KEGG; mmu:100043684; -.
DR KEGG; mmu:100043686; -.
DR KEGG; mmu:100043688; -.
DR KEGG; mmu:109959; -.
DR UCSC; uc008rav.2; mouse.
DR CTD; 100043684; -.
DR CTD; 100043686; -.
DR CTD; 100043688; -.
DR CTD; 109959; -.
DR MGI; MGI:88020; Amy2.
DR VEuPathDB; HostDB:ENSMUSG00000074268; -.
DR VEuPathDB; HostDB:ENSMUSG00000093931; -.
DR VEuPathDB; HostDB:ENSMUSG00000096569; -.
DR VEuPathDB; HostDB:ENSMUSG00000096770; -.
DR eggNOG; KOG2212; Eukaryota.
DR GeneTree; ENSGT00940000163532; -.
DR HOGENOM; CLU_013336_2_1_1; -.
DR InParanoid; P00688; -.
DR OMA; MPSGEYC; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; P00688; -.
DR TreeFam; TF312850; -.
DR Reactome; R-MMU-189085; Digestion of dietary carbohydrate.
DR BioGRID-ORCS; 100043684; 4 hits in 33 CRISPR screens.
DR BioGRID-ORCS; 100043686; 6 hits in 32 CRISPR screens.
DR BioGRID-ORCS; 100043688; 3 hits in 35 CRISPR screens.
DR BioGRID-ORCS; 109959; 4 hits in 33 CRISPR screens.
DR PRO; PR:P00688; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P00688; protein.
DR Bgee; ENSMUSG00000074268; Expressed in islet of Langerhans and 24 other tissues.
DR Genevisible; P00688; MM.
DR GO; GO:0005615; C:extracellular space; 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; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
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; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:6165618"
FT CHAIN 16..508
FT /note="Pancreatic alpha-amylase"
FT /id="PRO_0000001398"
FT ACT_SITE 209
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 245
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 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 207
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 310
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 349
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 312
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 16
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6165618"
FT DISULFID 43..101
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 85..130
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 156..172
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 390..396
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 462..474
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT VARIANT 64
FT /note="V -> I (in A1, B(C) and AMY-2.2Y)"
FT VARIANT 66
FT /note="V -> I (in AMY-2.2Y)"
FT VARIANT 120
FT /note="A -> S (in A1, B(A) and B(C))"
FT VARIANT 161
FT /note="D -> S (in A1, B(A) and B(C); requires 2 nucleotide
FT substitutions)"
FT VARIANT 174
FT /note="L -> V (in A1 and B(C))"
FT VARIANT 175
FT /note="T -> S (in B(A))"
FT VARIANT 254
FT /note="I -> V (in A1 and B(C))"
FT VARIANT 270..272
FT /note="YGA -> FGV (in A1 and B(C))"
FT VARIANT 298
FT /note="L -> M (in A1, B(A) and B(C))"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VARIANT 322
FT /note="S -> A (in B(A))"
FT VARIANT 419
FT /note="S -> A (in B1)"
FT VARIANT 450
FT /note="A -> E (in B(C))"
FT CONFLICT 70
FT /note="S -> T (in Ref. 5; AAA37228)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="C -> S (in Ref. 5; AAA37228)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="G -> R (in Ref. 1; CAA24098 and 2; CAA26413/
FT CAA26414/CAA26415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 57318 MW; B204B03768132593 CRC64;
MKFVLLLSLI GFCWAQYDPH TSDGRTAIVH LFEWRWVDIA KECERYLAPK GFGGVQVSPP
NENVVVHNPS RPWWERYQPI SYKICTRSGN EDEFRDMVTR CNNVGVRIYV DAVINHMCGA
GNPAGTSSTC GSYLNPNNRE FPAVPYSAWD FNDNKCNGEI DNYNDAYQVR NCRLTGLLDL
ALEKDYVRTK VADYMNHLID IGVAGFRLDA AKHMWPGDIK AVLDKLHNLN TKWFSQGSRP
FIFQEVIDLG GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGLVP
SDRALVFVDN HDNQRGHGAG GSSILTFWDA RMYKMAVGFM LAHPYGFTRV MSSYRWNRNF
QNGKDQNDWI GPPNNNGVTK EVTINADTTC GNDWVCEHRW RQIRNMVAFR NVVNGQPFSN
WWDNNSNQVA FSRGNRGFIV FNNDDWALSA TLQTGLPAGT YCDVISGDKV DGNCTGLRVN
VGSDGKAHFS ISNSAEDPFI AIHADSKL
