UniProtKB - P00690 (AMYP_PIG)
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- BLAST
>sp|P00690|AMYP_PIG Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3 MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPP NENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGS GAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGL LDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAG SRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWG FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWA RNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQP FANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGI KVYVSSDGTAQFSISNSAEDPFIAIHAESKL
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Protein
Pancreatic alpha-amylase
Gene
AMY2
Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Miscellaneous
The two forms of this enzyme, I and II, show very similar activities, molecular masses, and compositions and differ only in their isoelectric points. As no evidence for two variants were in the cDNA library of PubMed:10082956, it is most likely that isoform I (PPAI) and isoform II (PPAII) are two forms of the same protein.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- Ca2+9 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.7"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 (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, COFACTOR. - Ref.8"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.9"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose."
Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.
Eur. J. Biochem. 238:561-569(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM, SEQUENCE REVISION, COFACTOR, DISULFIDE BONDS. - Ref.11"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex."
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.
Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR AND CALCIUM, COFACTOR, DISULFIDE BONDS. - Ref.12"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.14"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Manual assertion based on experiment ini
- Ref.5"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.7"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 (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, COFACTOR. - Ref.8"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.9"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose."
Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.
Eur. J. Biochem. 238:561-569(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM, SEQUENCE REVISION, COFACTOR, DISULFIDE BONDS. - Ref.11"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex."
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.
Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR AND CALCIUM, COFACTOR, DISULFIDE BONDS. - Ref.12"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.14"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
- chloride6 Publications
Manual assertion based on experiment ini
- Ref.5"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.8"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.9"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.12"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.14"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Manual assertion based on experiment ini
- Ref.5"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.8"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.9"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.12"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.14"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 115 | Calcium8 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 173 | Calcium; via carbonyl oxygen8 Publications Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 182 | Calcium8 Publications Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 210 | Chloride5 Publications Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 212 | Nucleophile | 1 | |
| Metal bindingi | 216 | Calcium; via carbonyl oxygen8 Publications Manual assertion based on experiment ini
| 1 | |
| Active sitei | 248 | Proton donor | 1 | |
| Binding sitei | 313 | ChlorideCurated | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 315 | Transition state stabilizerBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Binding sitei | 352 | Chloride5 Publications Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alpha-amylase activity Source: UniProtKB
- alpha-amylase activity (releasing maltohexaose) Source: UniProtKB-EC
- calcium ion binding Source: UniProtKB
- chloride ion binding Source: UniProtKB
GO - Biological processi
- carbohydrate catabolic process Source: UniProtKB
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Glycosidase, Hydrolase |
| Biological process | Carbohydrate metabolism |
| Ligand | Calcium, Chloride, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.1.1 6170 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00690 |
Protein family/group databases
Carbohydrate-Active enZymes More...CAZyi | GH13 Glycoside Hydrolase Family 13 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Pancreatic alpha-amylase (EC:3.2.1.1By similarityManual assertion inferred from sequence similarity toi )Short name: PA Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:AMY2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Sus scrofa (Pig) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9823 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: UniProtKB
Keywords - Cellular componenti
Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Protein family/group databases
Allergome; a platform for allergen knowledge More...Allergomei | 970 Sus s Amylase |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5730 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 15 | 1 Publication Manual assertion based on experiment ini
| 15 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000001399 | 16 – 511 | Pancreatic alpha-amylaseAdd BLAST | 496 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 16 | Pyrrolidone carboxylic acidBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 43 ↔ 101 | 1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
| Disulfide bondi | 85 ↔ 130 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
| Disulfide bondi | 156 ↔ 175 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
| Disulfide bondi | 393 ↔ 399 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 427 | N-linked (GlcNAc...) asparagine | 1 | |
| Disulfide bondi | 465 ↔ 477 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
|
Keywords - PTMi
Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acidProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00690 |
PeptideAtlas More...PeptideAtlasi | P00690 |
PRoteomics IDEntifications database More...PRIDEi | P00690 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
Protein-protein interaction databases
Molecular INTeraction database More...MINTi | P00690 |
STRING: functional protein association networks More...STRINGi | 9823.ENSSSCP00000026998 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00690 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 27 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 46 – 51 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 54 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 67 – 70 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 73 – 77 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 78 – 80 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 84 – 86 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 91 – 103 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 107 – 112 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 115 – 119 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 124 – 126 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 128 – 130 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 136 – 138 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 142 – 145 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 148 – 150 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 153 – 155 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 158 – 162 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 169 – 174 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 175 – 177 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 180 – 183 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 188 – 204 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 208 – 211 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 214 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 219 – 226 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Turni | 234 – 236 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 244 – 247 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 253 – 257 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 259 – 262 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 263 – 265 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 266 – 269 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 272 – 281 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 289 – 294 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 297 – 299 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 304 – 306 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 307 – 309 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 316 – 318 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 319 – 321 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 324 – 326 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 330 – 332 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 333 – 345 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 348 – 355 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 363 – 366 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 369 – 372 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 375 – 378 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 400 – 402 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 404 – 415 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 416 – 418 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 421 – 426 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 428 – 436 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Turni | 437 – 439 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 440 – 445 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 447 – 449 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 451 – 456 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 461 – 465 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 467 – 469 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 476 – 479 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 481 – 484 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 488 – 494 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 498 – 500 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 502 – 506 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 507 – 509 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P00690 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00690 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00690 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the glycosyl hydrolase 13 family.Curated
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2212 Eukaryota COG0366 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000253313 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000061 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00690 |
KEGG Orthology (KO) More...KOi | K01176 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.60.40.1180, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR006048 A-amylase/branching_C IPR031319 A-amylase_C IPR006046 Alpha_amylase IPR006047 Glyco_hydro_13_cat_dom IPR013780 Glyco_hydro_b IPR017853 Glycoside_hydrolase_SF |
Pfam protein domain database More...Pfami | View protein in Pfam PF00128 Alpha-amylase, 1 hit PF02806 Alpha-amylase_C, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00110 ALPHAAMYLASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00642 Aamy, 1 hit SM00632 Aamy_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51445 SSF51445, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P00690-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK
60 70 80 90 100
GFGGVQVSPP NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGS GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD
160 170 180 190 200
FNDGKCKTAS GGIESYNDPY QVRDCQLVGL LDLALEKDYV RSMIADYLNK
210 220 230 240 250
LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG SRPFIFQEVI
260 270 280 290 300
DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG
310 320 330 340 350
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYRWA RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE
410 420 430 440 450
HRWRQIRNMV WFRNVVDGQP FANWWANGSN QVAFGRGNRG FIVFNNDDWQ
460 470 480 490 500
LSSTLQTGLP GGTYCDVISG DKVGNSCTGI KVYVSSDGTA QFSISNSAED
510
PFIAIHAESK L
Length:511
Mass (Da):57,086
Last modified:August 15, 2003 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i117489E020807378
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 138 | N → S AA sequence (PubMed:3484639).Curated | 1 | |
| Sequence conflicti | 367 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
| Sequence conflicti | 405 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
| Sequence conflicti | 419 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
| Sequence conflicti | 426 | A → D AA sequence (PubMed:3484639).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF064742 mRNA Translation: AAF02828.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A25412 ALPGP |
NCBI Reference Sequences More...RefSeqi | NP_999360.1, NM_214195.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Ssc.94418 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 397397 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ssc:397397 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P00690 | Alpha-amylase | 511 | UniRef90_P00690 | |||
| Alpha-amylase | 496 | |||||
| Alpha-amylase | 502 | |||||
| Alpha-amylase | 502 | |||||
| Alpha-amylase | 502 | |||||
| +14 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P00690 | Pancreatic alpha-amylase | 508 | UniRef50_P00688 | |||
| Pancreatic alpha-amylase | 508 | |||||
| Alpha-amylase | 514 | |||||
| Alpha-amylase | 508 | |||||
| Alpha-amylase | 450 | |||||
| +450 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Worthington enzyme manual |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF064742 mRNA Translation: AAF02828.1 |
| PIRi | A25412 ALPGP |
| RefSeqi | NP_999360.1, NM_214195.1 |
| UniGenei | Ssc.94418 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1BVN | X-ray | 2.50 | P | 16-511 | [»] | |
| 1DHK | X-ray | 1.85 | A | 17-511 | [»] | |
| 1HX0 | X-ray | 1.38 | A | 16-511 | [»] | |
| 1JFH | X-ray | 2.03 | A | 17-511 | [»] | |
| 1KXQ | X-ray | 1.60 | A/B/C/D | 16-511 | [»] | |
| 1KXT | X-ray | 2.00 | A/C/E | 16-511 | [»] | |
| 1KXV | X-ray | 1.60 | A/B | 16-511 | [»] | |
| 1OSE | X-ray | 2.30 | A | 17-511 | [»] | |
| 1PIF | X-ray | 2.30 | A | 17-511 | [»] | |
| 1PIG | X-ray | 2.20 | A | 17-511 | [»] | |
| 1PPI | X-ray | 2.20 | A | 16-511 | [»] | |
| 1UA3 | X-ray | 2.01 | A | 16-511 | [»] | |
| 1VAH | X-ray | 2.40 | A | 16-511 | [»] | |
| 1WO2 | X-ray | 2.01 | A | 16-511 | [»] | |
| 3L2L | X-ray | 2.11 | A | 16-511 | [»] | |
| 3L2M | X-ray | 1.97 | A | 16-511 | [»] | |
| 4X0N | X-ray | 2.60 | A | 17-511 | [»] | |
| ProteinModelPortali | P00690 | |||||
| SMRi | P00690 | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Protein-protein interaction databases
| MINTi | P00690 |
| STRINGi | 9823.ENSSSCP00000026998 |
Chemistry databases
| BindingDBi | P00690 |
| ChEMBLi | CHEMBL5730 |
Protein family/group databases
| Allergomei | 970 Sus s Amylase |
| CAZyi | GH13 Glycoside Hydrolase Family 13 |
Proteomic databases
| PaxDbi | P00690 |
| PeptideAtlasi | P00690 |
| PRIDEi | P00690 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
| GeneIDi | 397397 |
| KEGGi | ssc:397397 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 397397 |
Phylogenomic databases
| eggNOGi | KOG2212 Eukaryota COG0366 LUCA |
| HOGENOMi | HOG000253313 |
| HOVERGENi | HBG000061 |
| InParanoidi | P00690 |
| KOi | K01176 |
Enzyme and pathway databases
| BRENDAi | 3.2.1.1 6170 |
| SABIO-RKi | P00690 |
Miscellaneous databases
| EvolutionaryTracei | P00690 |
Protein Ontology More...PROi | PR:P00690 |
Family and domain databases
| Gene3Di | 2.60.40.1180, 1 hit |
| InterProi | View protein in InterPro IPR006048 A-amylase/branching_C IPR031319 A-amylase_C IPR006046 Alpha_amylase IPR006047 Glyco_hydro_13_cat_dom IPR013780 Glyco_hydro_b IPR017853 Glycoside_hydrolase_SF |
| Pfami | View protein in Pfam PF00128 Alpha-amylase, 1 hit PF02806 Alpha-amylase_C, 1 hit |
| PRINTSi | PR00110 ALPHAAMYLASE |
| SMARTi | View protein in SMART SM00642 Aamy, 1 hit SM00632 Aamy_C, 1 hit |
| SUPFAMi | SSF51445 SSF51445, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | AMYP_PIG | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P00690Primary (citable) accession number: P00690 Secondary accession number(s): Q9TUE4 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | August 15, 2003 | |
| Last modified: | September 12, 2018 | |
| This is version 162 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries
