AMYP_RAT
ID AMYP_RAT Reviewed; 508 AA.
AC P00689;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 158.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA MacDonald R.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-508.
RX PubMed=6159531; DOI=10.1038/287117a0;
RA McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Thomas G.,
RA Rutter W.J.;
RT "Structure of a family of rat amylase genes.";
RL Nature 287:117-122(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-508.
RX PubMed=6168351;
RX DOI=10.1002/1097-0142(19810315)47:6+<1497::aid-cncr2820471410>3.0.co;2-a;
RA McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Rutter W.J.;
RT "Pancreas-specific genes: structure and expression.";
RL Cancer 47:1497-1504(1981).
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; J00703; AAA40725.2; -; mRNA.
DR PIR; A00840; ALRTP.
DR RefSeq; NP_113690.1; NM_031502.1.
DR AlphaFoldDB; P00689; -.
DR SMR; P00689; -.
DR IntAct; P00689; 1.
DR STRING; 10116.ENSRNOP00000022268; -.
DR BindingDB; P00689; -.
DR ChEMBL; CHEMBL2699; -.
DR DrugCentral; P00689; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; P00689; -.
DR PhosphoSitePlus; P00689; -.
DR PaxDb; P00689; -.
DR GeneID; 497039; -.
DR KEGG; rno:497039; -.
DR UCSC; RGD:1593187; rat.
DR CTD; 100043686; -.
DR RGD; 1593187; Amy2.
DR eggNOG; KOG2212; Eukaryota.
DR InParanoid; P00689; -.
DR OrthoDB; 665362at2759; -.
DR PhylomeDB; P00689; -.
DR Reactome; R-RNO-189085; Digestion of dietary carbohydrate.
DR PRO; PR:P00689; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:CACAO.
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 2: Evidence at transcript 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 CHAIN 16..508
FT /note="Pancreatic alpha-amylase"
FT /id="PRO_0000001400"
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:0000250|UniProtKB:P04746"
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"
SQ SEQUENCE 508 AA; 57177 MW; 8AA0EA5D45A7CBFC CRC64;
MKFVLLLSLI GFCWAQYDPH TADGRTAIVH LFEWRWADIA KECERYLAPK GFGGVQVSPP
NENIIINNPS RPWWERYQPI SYKICSRSGN ENEFKDMVTR CNNVGVRIYV DAVINHMCGS
GNSAGTHSTC GSYFNPNNRE FSAVPYSAWY FNDNKCNGEI NNYNDANQVR NCRLSGLLDL
ALDKDYVRTK VADYMNNLID IGVAGFRLDA AKHMWPGDIK AVLDKLHNLN TKWFSQGSRP
FIFQEVIDLG GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGFVP
TDRALVFVDN HDNQRGHGAG GASILTFWDA RMYKMAVGFM LAHPYGFTRV MSSYRRTRNF
QNGKDVNDWI GPPNNNGVTK EVTINPDTTC GNDWVCEHRW RQIRNMVAFR NVVNGQPFAN
WWDNGSNQVA FSRGNRGFIV FNNDDWALSS TLQTGLPAGT YCDVISGDKV NGNCTGLKVN
VGSDGKAHFS ISNSAEDPFI AIHADSKL
