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P00687 (AMY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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 processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular space

Inferred from direct assay PubMed 6163812. Source: MGI

   Molecular_functionalpha-amylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

amylase activity

Inferred from direct assay PubMed 6163812. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Chain16 – 511496Alpha-amylase 1
PRO_0000001403

Sites

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

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid
Disulfide bond43 ↔ 101 By similarity
Disulfide bond85 ↔ 130 By similarity
Disulfide bond156 ↔ 175 By similarity
Disulfide bond393 ↔ 399 By similarity
Disulfide bond465 ↔ 477 By similarity

Experimental info

Sequence conflict291V → I in AAA37221. Ref.1
Sequence conflict291V → I in CAA24097. Ref.1
Sequence conflict291V → I in CAA24099. Ref.2
Sequence conflict291V → I in CAA24100. Ref.2
Sequence conflict291V → I in AAA37219. Ref.6
Sequence conflict2291L → Q in CAA24099. Ref.2
Sequence conflict2291L → Q in CAA24100. Ref.2
Sequence conflict4411F → L in AAA37221. Ref.1
Sequence conflict4411F → L in CAA24097. Ref.1
Sequence conflict4411F → L in CAA24099. Ref.2
Sequence conflict4411F → L in CAA24100. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00687 [UniParc].

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

FASTA51157,644
        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' 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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS17776.1.
PIRALMSS. A90798.
RefSeqNP_001103975.1. NM_001110505.1.
NP_031472.2. NM_007446.2.
UniGeneMm.439727.

3D structure databases

ProteinModelPortalP00687.
SMRP00687. Positions 17-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198093. 1 interaction.
IntActP00687. 16 interactions.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteP00687.

Proteomic databases

MaxQBP00687.
PaxDbP00687.
PRIDEP00687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067980; ENSMUSP00000070368; ENSMUSG00000074264.
ENSMUST00000106540; ENSMUSP00000102150; ENSMUSG00000074264.
GeneID11722.
KEGGmmu:11722.
UCSCuc008rba.2. mouse.

Organism-specific databases

CTD11722.
MGIMGI:88019. Amy1.

Phylogenomic databases

eggNOGCOG0366.
GeneTreeENSGT00390000002882.
HOGENOMHOG000253313.
HOVERGENHBG000061.
InParanoidQ921Y7.
KOK01176.
OMADANDWIG.
OrthoDBEOG7RJPR2.
TreeFamTF312850.

Gene expression databases

ArrayExpressP00687.
BgeeP00687.
CleanExMM_AMY1.
GenevestigatorP00687.

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

ChiTaRSAMY1A. mouse.
NextBio279401.
PROP00687.
SOURCESearch...

Entry information

Entry nameAMY1_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries