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Reviewed, UniProtKB/Swiss-Prot P00689 (AMYP_RAT)

Last modified October 13, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Amy2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 chloride ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

chloride ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Chain16 – 508493Pancreatic alpha-amylase
PRO_0000001400

Sites

Active site2091Nucleophile By similarity
Active site2451Proton donor By similarity
Active site3121 By similarity
Metal binding1151Calcium By similarity
Metal binding1701Calcium; via carbonyl oxygen By similarity
Metal binding1791Calcium By similarity
Metal binding2131Calcium; via carbonyl oxygen By similarity
Binding site2071Chloride By similarity
Binding site3101Chloride By similarity
Binding site3491Chloride By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid By similarity
Disulfide bond43 ↔ 101 By similarity
Disulfide bond85 ↔ 130 By similarity
Disulfide bond156 ↔ 172 By similarity
Disulfide bond390 ↔ 396 By similarity
Disulfide bond462 ↔ 474 By similarity

Sequences

Sequence LengthMass (Da)Tools
P00689-1 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 8AA0EA5D45A7CBFC

FASTA50857,177
        10         20         30         40         50         60 
MKFVLLLSLI GFCWAQYDPH TADGRTAIVH LFEWRWADIA KECERYLAPK GFGGVQVSPP 

        70         80         90        100        110        120 
NENIIINNPS RPWWERYQPI SYKICSRSGN ENEFKDMVTR CNNVGVRIYV DAVINHMCGS 

       130        140        150        160        170        180 
GNSAGTHSTC GSYFNPNNRE FSAVPYSAWY FNDNKCNGEI NNYNDANQVR NCRLSGLLDL 

       190        200        210        220        230        240 
ALDKDYVRTK VADYMNNLID IGVAGFRLDA AKHMWPGDIK AVLDKLHNLN TKWFSQGSRP 

       250        260        270        280        290        300 
FIFQEVIDLG GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGFVP 

       310        320        330        340        350        360 
TDRALVFVDN HDNQRGHGAG GASILTFWDA RMYKMAVGFM LAHPYGFTRV MSSYRRTRNF 

       370        380        390        400        410        420 
QNGKDVNDWI GPPNNNGVTK EVTINPDTTC GNDWVCEHRW RQIRNMVAFR NVVNGQPFAN 

       430        440        450        460        470        480 
WWDNGSNQVA FSRGNRGFIV FNNDDWALSS TLQTGLPAGT YCDVISGDKV NGNCTGLKVN 

       490        500 
VGSDGKAHFS ISNSAEDPFI AIHADSKL 

« Hide

References

[1]MacDonald R.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of a family of rat amylase genes."
McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Thomas G., Rutter W.J.
Nature 287:117-122(1980) [PubMed: 6159531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-508.
[3]"Pancreas-specific genes: structure and expression."
McDonald R.J., Crerar M.M., Swain W.F., Pictet R.L., Rutter W.J.
Cancer 47:1497-1504(1981) [PubMed: 6168351] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-508.
+Additional computationally mapped references.

Cross-references

Sequence databases

J00703 mRNA. Translation: AAA40725.2.
IPIIPI00211904.
PIRALRTP. A00840.
RefSeqNP_113690.1.
UniGeneRn.67070

3D structure databases

HSSPHSSP built from PDB template 1KXQ based on UniProtKB P00690.
SMRP00689. Positions 16-508.
ModBaseSearch...

Protein-protein interaction databases

STRINGP00689.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEP00689.

Genome annotation databases

EnsemblENSRNOT00000022268; ENSRNOP00000022268; ENSRNOG00000030590; Rattus norvegicus. [Genome view]
GeneID497039.
KEGGrno:497039.

Organism-specific databases

CTD497039.
RGD1593187. Amy2.

Phylogenomic databases

HOVERGENP00689.

Enzyme and pathway databases

BRENDA3.2.1.1. 248.

Gene expression databases

GenevestigatorP00689.
GermOnlineENSRNOG00000030590. Rattus norvegicus.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
ProtoNetSearch...

Other Resources

NextBio697675.

Entry information

Entry nameAMYP_RAT
AccessionPrimary (citable) accession number: P00689
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 20, 2002
Last modified: October 13, 2009
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents