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P04746 (AMYP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pancreatic alpha-amylase

Short name=PA
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 chloride ion per subunit.

Subunit structure

Monomer.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Chain16 – 511496Pancreatic alpha-amylase
PRO_0000001397

Sites

Active site2121Nucleophile
Active site2481Proton donor
Metal binding1151Calcium
Metal binding1731Calcium; via carbonyl oxygen
Metal binding1821Calcium
Metal binding2161Calcium; via carbonyl oxygen
Binding site2101Chloride
Binding site3131Chloride
Binding site3521Chloride
Site3151Transition state stabilizer By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid
Glycosylation4761N-linked (GlcNAc...)
Disulfide bond43 ↔ 101
Disulfide bond85 ↔ 130
Disulfide bond156 ↔ 175
Disulfide bond393 ↔ 399
Disulfide bond465 ↔ 477

Experimental info

Mutagenesis2101R → A or Q: Abolishes chloride binding; strongly reduces activity. Ref.12
Mutagenesis2121D → A or N: Abolishes activity. Ref.10 Ref.13
Mutagenesis2481E → A or Q: Reduces activity. Ref.13
Mutagenesis3131N → S: Reduces affinity for chloride; reduces activity. Ref.12
Mutagenesis3151D → A or N: Strongly reduces activity. Ref.13
Mutagenesis3521R → A: Abolishes chloride binding; has only slight effect on activity. Ref.12

Secondary structure

............................................................................................................... 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04746 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: A77B1A34EACB3C2A

FASTA51157,707
        10         20         30         40         50         60 
MKFFLLLFTI GFCWAQYSPN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP 

        70         80         90        100        110        120 
NENVAIYNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN 

       130        140        150        160        170        180 
AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLTGL 

       190        200        210        220        230        240 
LDLALEKDYV RSKIAEYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNSNWFPAG 

       250        260        270        280        290        300 
SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG 

       310        320        330        340        350        360 
FVPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP 

       370        380        390        400        410        420 
RQFQNGNDVN DWVGPPNNNG VIKEVTINPD TTCGNDWVCE HRWRQIRNMV IFRNVVDGQP 

       430        440        450        460        470        480 
FTNWYDNGSN QVAFGRGNRG FIVFNNDDWS FSLTLQTGLP AGTYCDVISG DKINGNCTGI 

       490        500        510 
KIYVSDDGKA HFSISNSAED PFIAIHAESK L 

« Hide

References

« Hide 'large scale' references
[1]"Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases."
Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., Matsubara K.
Gene 28:263-270(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Nakamura Y., Ogawa M., Nishide T., Emi M., Kosaki G., Himeno S., Matsubara K.
Gene 50:371-372(1986)
Cited for: SEQUENCE REVISION.
[3]"Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene."
Horii A., Emi M., Tomita N., Nishide T., Ogawa M., Mori T., Matsubara K.
Gene 60:57-64(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Pancreas.
[4]"A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A."
Wise R.J., Karn R.C., Larsen S.H., Hodes M.E., Gardell S.J., Rutter W.J.
Mol. Biol. Med. 2:307-322(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Pancreas.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[6]"Human pancreatic amylase is encoded by two different genes."
Groot P.C., Bleeker M.J., Pronk J.C., Arwert F., Mager W.H., Planta R.J., Eriksson A.W., Frants R.R.
Nucleic Acids Res. 16:4724-4724(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[7]"Concerted evolution of human amylase genes."
Gumucio D.L., Wiebauer K., Caldwell R.M., Samuelson L.C., Meisler M.H.
Mol. Cell. Biol. 8:1197-1205(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
[8]"The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution."
Qian M., Haser R., Buisson G., Duee E., Payan F.
Biochemistry 33:6284-6294(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[9]"The structure of human pancreatic alpha-amylase at 1.8-A resolution and comparisons with related enzymes."
Brayer G.D., Luo Y., Withers S.G.
Protein Sci. 4:1730-1742(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), PYROGLUTAMATE FORMATION AT GLU-16.
[10]"Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris."
Rydberg E.H., Sidhu G., Vo H.C., Hewitt J., Cote H.C.F., Wang Y., Numao S., MacGillivray R.T.A., Overall C.M., Brayer G.D., Withers S.G.
Protein Sci. 8:635-643(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF ASP-212.
[11]"Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques."
Brayer G.D., Sidhu G., Maurus R., Rydberg E.H., Braun C., Wang Y., Nguyen N.T., Overall C.M., Withers S.G.
Biochemistry 39:4778-4791(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[12]"Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase."
Numao S., Maurus R., Sidhu G., Wang Y., Overall C.M., Brayer G.D., Withers S.G.
Biochemistry 41:215-225(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF ARG-210; ASN-313 AND ARG-352.
[13]"Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids."
Rydberg E.H., Li C., Maurus R., Overall C.M., Brayer G.D., Withers S.G.
Biochemistry 41:4492-4502(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF ASP-212; GLU-248 AND ASP-315.
+Additional computationally mapped references.

Web resources

Wikipedia

Amylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18785 expand/collapse EMBL AC list , M18714, M18716, M18718, M18720, M18722, M18724, M18726, M18783 Genomic DNA. Translation: AAA52280.1.
M28443 mRNA. Translation: AAA51724.1.
BC007060 mRNA. Translation: AAH07060.1.
M18669 Genomic DNA. Translation: AAA51723.1.
X07056 Genomic DNA. Translation: CAA30099.1.
CCDSCCDS783.1.
PIRALHUP. A29614.
RefSeqNP_000690.1. NM_000699.2.
UniGeneHs.654437.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B2YX-ray3.20A16-511[»]
1BSIX-ray2.00A17-511[»]
1CPUX-ray2.00A16-511[»]
1HNYX-ray1.80A17-511[»]
1KB3X-ray2.10A16-511[»]
1KBBX-ray1.90A16-511[»]
1KBKX-ray1.90A16-511[»]
1KGUX-ray2.00A16-511[»]
1KGWX-ray2.10A16-511[»]
1KGXX-ray2.00A16-511[»]
1U2YX-ray1.95A16-511[»]
1U30X-ray1.90A16-511[»]
1U33X-ray1.95A16-511[»]
1XCWX-ray2.00A16-511[»]
1XCXX-ray1.90A16-511[»]
1XD0X-ray2.00A16-511[»]
1XD1X-ray2.20A16-511[»]
1XGZX-ray2.00A16-511[»]
1XH0X-ray2.00A16-511[»]
1XH1X-ray2.03A16-511[»]
1XH2X-ray2.20A16-511[»]
2CPUX-ray2.00A17-511[»]
2QMKX-ray2.30A16-511[»]
2QV4X-ray1.97A16-511[»]
3BAIX-ray1.90A16-511[»]
3BAJX-ray2.10A16-511[»]
3BAKX-ray1.90A16-511[»]
3BAWX-ray2.00A16-511[»]
3BAXX-ray1.90A16-511[»]
3BAYX-ray1.99A16-511[»]
3CPUX-ray2.00A17-511[»]
3IJ7X-ray2.00A17-511[»]
3IJ8X-ray1.43A17-511[»]
3IJ9X-ray1.85A17-511[»]
3OLDX-ray2.00A16-511[»]
3OLEX-ray1.55A16-511[»]
3OLGX-ray2.30A16-511[»]
3OLIX-ray1.50A16-511[»]
4GQQX-ray1.35A17-511[»]
4GQRX-ray1.20A17-511[»]
ProteinModelPortalP04746.
SMRP04746. Positions 16-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106776. 3 interactions.
IntActP04746. 3 interactions.
STRING9606.ENSP00000377509.

Chemistry

BindingDBP04746.
ChEMBLCHEMBL2045.
DrugBankDB00284. Acarbose.
DB00522. Bentiromide.
DB00702. Icodextrin.
DB00491. Miglitol.
DB00085. Pancrelipase.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteP04746.

Polymorphism databases

DMDM113803.

Proteomic databases

PRIDEP04746.

Protocols and materials databases

DNASU279.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000414303; ENSP00000397582; ENSG00000243480.
GeneID279.
KEGGhsa:279.
UCSCuc001dut.3. human.

Organism-specific databases

CTD279.
GeneCardsGC01P104159.
HGNCHGNC:477. AMY2A.
HPACAB045960.
MIM104650. gene.
neXtProtNX_P04746.
PharmGKBPA24784.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000253313.
HOVERGENHBG000061.
InParanoidP04746.
KOK01176.
OMASNTYITA.
OrthoDBEOG7RJPR2.
PhylomeDBP04746.
TreeFamTF312850.

Enzyme and pathway databases

BRENDA3.2.1.1. 5538.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP04746.

Gene expression databases

BgeeP04746.
CleanExHS_AMY2A.
GenevestigatorP04746.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04746.
GeneWikiAMY2A.
GenomeRNAi279.
NextBio1129.
PROP04746.
SOURCESearch...

Entry information

Entry nameAMYP_HUMAN
AccessionPrimary (citable) accession number: P04746
Secondary accession number(s): Q9UBH3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries