Alpha-amylase 1 precursor - Mus musculus (Mouse)

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P00687 (AMY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-amylase 1
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Salivary and hepatic alpha-amylase

Gene names

Name:	Amy1
Synonyms:	Amy-1-a, Amy1a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. Binds 1 chloride ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted.
Tissue specificity	Expressed in liver and saliva.
Miscellaneous	Hepatic and salivary alpha-amylases are encoded by the same gene; however, their mRNAs have different 5'-UTR sequences.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from direct assay. Source: MGI
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

Chain

16 – 511

496

Alpha-amylase 1

PRO_0000001403

Sites

Active site

212

Nucleophile By similarity

Active site

248

Proton donor By similarity

Metal binding

115

Calcium By similarity

Metal binding

173

Calcium; via carbonyl oxygen By similarity

Metal binding

182

Calcium By similarity

Metal binding

216

Calcium; via carbonyl oxygen By similarity

Binding site

210

Chloride By similarity

Binding site

313

Chloride By similarity

Binding site

352

Chloride By similarity

Site

315

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid

Disulfide bond

43 ↔ 101

By similarity

Disulfide bond

85 ↔ 130

By similarity

Disulfide bond

156 ↔ 175

By similarity

Disulfide bond

393 ↔ 399

By similarity

Disulfide bond

465 ↔ 477

By similarity

Experimental info

Sequence conflict

V → I in AAA37221. Ref.1

Sequence conflict

V → I in CAA24097. Ref.1

Sequence conflict

V → I in CAA24099. Ref.2

Sequence conflict

V → I in CAA24100. Ref.2

Sequence conflict

V → I in AAA37219. Ref.6

Sequence conflict

229

L → Q in CAA24099. Ref.2

Sequence conflict

229

L → Q in CAA24100. Ref.2

Sequence conflict

441

F → L in AAA37221. Ref.1

Sequence conflict

441

F → L in CAA24097. Ref.1

Sequence conflict

441

F → L in CAA24099. Ref.2

Sequence conflict

441

F → L in CAA24100. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P00687 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: CC5399F4C23E1105
Show »

FASTA

511

57,644

        10         20         30         40         50         60 
MKFFLLLSLI GFCWAQYDPH TQYGRTAIVH LFEWRWVDIA KECERYLAPN GFAGVQVSPP 

        70         80         90        100        110        120 
NENIVVHSPS RPWWERYQPI SYKICSRSGN EDEFRDMVNR CNNVGVRIYV DAVINHMCGV 

       130        140        150        160        170        180 
GAQAGQSSTC GSYFNPNNRD FPGVPYSGFD FNDGKCRTAS GGIENYQDAA QVRDCRLSGL 

       190        200        210        220        230        240 
LDLALEKDYV RTKVADYMNH LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNTKWFSQG 

       250        260        270        280        290        300 
SRPFIFQEVI DLGGEAVSSN EYFGNGRVTE FKYGAKLGKV MRKWDGEKMS YLKNWGEGWG 

       310        320        330        340        350        360 
LMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYYWP 

       370        380        390        400        410        420 
RNFQNGKDVN DWVGPPNNNG KTKEVSINPD STCGNDWICE HRWRQIRNMV AFRNVVNGQP 

       430        440        450        460        470        480 
FANWWDNDSN QVAFGRGNKG FIVFNNDDWA LSETLQTGLP AGTYCDVISG DKVDGNCTGI 

       490        500        510 
KVYVGNDGKA HFSISNSAED PFIAIHAESK I

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue-specific expression of mouse-alpha-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland." Hagenbuechle O., Bovey R., Young R.A. Cell 21:179-187(1980) [PubMed: 6157477] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Salivary gland.
[2]	"Mouse liver and salivary gland alpha-amylase mRNAs differ only in 5' non-translated sequences." Hagenbuechle O., Tosi M., Schibler U., Bovey R., Wellauer P.K., Young R.A. Nature 289:643-646(1981) [PubMed: 6162108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver and Salivary gland.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[6]	"A single mouse alpha-amylase gene specifies two different tissue-specific mRNAs." Young R.A., Hagenbuechle O., Schibler U. Cell 23:451-458(1981) [PubMed: 6162570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94. Strain: A/J. Tissue: Liver and Salivary gland.
[7]	"The mouse alpha-amylase multigene family. Sequence organization of members expressed in the pancreas, salivary gland and liver." Schibler U., Pittet A.-C., Young R.A., Hagenbuechle O., Tosi M., Gellman S., Wellauer P.K. J. Mol. Biol. 155:247-266(1982) [PubMed: 6176715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-292. Strain: A/J. Tissue: Liver and Salivary gland.
[8]	"Characterization of the amino termini of mouse salivary and pancreatic amylases." Karn R.C., Petersen T.E., Hjorth J.P., Nieles J.T., Roepstorff P. FEBS Lett. 126:292-296(1981) Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLN-16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J00356 mRNA. Translation: AAA37221.1. V00717 mRNA. Translation: CAA24097.1. V00719 mRNA. Translation: CAA24099.1. V00720 mRNA. Translation: CAA24100.1. AK029642 mRNA. Translation: BAC26543.1. CH466532 Genomic DNA. Translation: EDL12410.1. CH466532 Genomic DNA. Translation: EDL12411.1. CH466532 Genomic DNA. Translation: EDL12412.1. BC009121 mRNA. Translation: AAH09121.1. J00353 Genomic DNA. Translation: AAA37219.1. J00354 Genomic DNA. Translation: AAA37220.1.
IPI	IPI00315893.
PIR	ALMSS. A90798.
RefSeq	NP_001103975.1. NM_001110505.1. NP_031472.2. NM_007446.2.
UniGene	Mm.439727.
3D structure databases
ProteinModelPortal	P00687.
SMR	P00687. Positions 17-511.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00687. 16 interactions.
STRING	P00687.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
PTM databases
PhosphoSite	P00687.
Proteomic databases
PRIDE	P00687.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067980; ENSMUSP00000070368; ENSMUSG00000074264. ENSMUST00000106540; ENSMUSP00000102150; ENSMUSG00000074264.
GeneID	11722.
KEGG	mmu:11722.
Organism-specific databases
CTD	11722.
MGI	MGI:88019. Amy1.
Phylogenomic databases
eggNOG	roNOG12919.
HOGENOM	HBG404170.
HOVERGEN	HBG000061.
InParanoid	P00687.
OrthoDB	EOG4RV2R1.
Gene expression databases
ArrayExpress	P00687.
Bgee	P00687.
CleanEx	MM_AMY1.
Genevestigator	P00687.
GermOnline	ENSMUSG00000074264. Mus musculus.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01176.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	279401.
SOURCE	Search...

Entry information

Entry name

AMY1_MOUSE

Accession

Primary (citable) accession number: P00687
Secondary accession number(s): Q921Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents