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Protein

Alpha-amylase 1

Gene

Amy1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl(-) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151CalciumBy similarity
Metal bindingi173 – 1731Calcium; via carbonyl oxygenBy similarity
Metal bindingi182 – 1821CalciumBy similarity
Binding sitei210 – 2101ChlorideBy similarity
Active sitei212 – 2121NucleophileBy similarity
Metal bindingi216 – 2161Calcium; via carbonyl oxygenBy similarity
Active sitei248 – 2481Proton donorBy similarity
Binding sitei313 – 3131ChlorideBy similarity
Sitei315 – 3151Transition state stabilizerBy similarity
Binding sitei352 – 3521ChlorideBy similarity

GO - Molecular functioni

  • alpha-amylase activity Source: MGI
  • amylase activity Source: MGI
  • calcium ion binding Source: MGI
  • chloride ion binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_340477. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Amy1
Synonyms:Amy-1-a, Amy1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88019. Amy1.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Chaini16 – 511496Alpha-amylase 1PRO_0000001403Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acid1 Publication
Disulfide bondi43 ↔ 101By similarity
Disulfide bondi85 ↔ 130By similarity
Disulfide bondi156 ↔ 175By similarity
Disulfide bondi393 ↔ 399By similarity
Disulfide bondi465 ↔ 477By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP00687.
PaxDbiP00687.
PRIDEiP00687.

PTM databases

PhosphoSiteiP00687.

Expressioni

Tissue specificityi

Expressed in liver and saliva.

Gene expression databases

BgeeiP00687.
CleanExiMM_AMY1.
ExpressionAtlasiP00687. baseline and differential.
GenevestigatoriP00687.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi198093. 1 interaction.
IntActiP00687. 16 interactions.

Structurei

3D structure databases

ProteinModelPortaliP00687.
SMRiP00687. Positions 17-511.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00687.
KOiK01176.
OMAiKNMIDTC.
OrthoDBiEOG7RJPR2.
TreeFamiTF312850.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFFLLLSLI GFCWAQYDPH TQYGRTAIVH LFEWRWVDIA KECERYLAPN
60 70 80 90 100
GFAGVQVSPP NENIVVHSPS RPWWERYQPI SYKICSRSGN EDEFRDMVNR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGV GAQAGQSSTC GSYFNPNNRD FPGVPYSGFD
160 170 180 190 200
FNDGKCRTAS GGIENYQDAA QVRDCRLSGL LDLALEKDYV RTKVADYMNH
210 220 230 240 250
LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNTKWFSQG SRPFIFQEVI
260 270 280 290 300
DLGGEAVSSN EYFGNGRVTE FKYGAKLGKV MRKWDGEKMS YLKNWGEGWG
310 320 330 340 350
LMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYYWP RNFQNGKDVN DWVGPPNNNG KTKEVSINPD STCGNDWICE
410 420 430 440 450
HRWRQIRNMV AFRNVVNGQP FANWWDNDSN QVAFGRGNKG FIVFNNDDWA
460 470 480 490 500
LSETLQTGLP AGTYCDVISG DKVDGNCTGI KVYVGNDGKA HFSISNSAED
510
PFIAIHAESK I
Length:511
Mass (Da):57,644
Last modified:July 27, 2011 - v2
Checksum:iCC5399F4C23E1105
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291V → I in AAA37221 (PubMed:6157477).Curated
Sequence conflicti29 – 291V → I in CAA24097 (PubMed:6157477).Curated
Sequence conflicti29 – 291V → I in CAA24099 (PubMed:6162108).Curated
Sequence conflicti29 – 291V → I in CAA24100 (PubMed:6162108).Curated
Sequence conflicti29 – 291V → I in AAA37219 (PubMed:6162570).Curated
Sequence conflicti229 – 2291L → Q in CAA24099 (PubMed:6162108).Curated
Sequence conflicti229 – 2291L → Q in CAA24100 (PubMed:6162108).Curated
Sequence conflicti441 – 4411F → L in AAA37221 (PubMed:6157477).Curated
Sequence conflicti441 – 4411F → L in CAA24097 (PubMed:6157477).Curated
Sequence conflicti441 – 4411F → L in CAA24099 (PubMed:6162108).Curated
Sequence conflicti441 – 4411F → L in CAA24100 (PubMed:6162108).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17776.1.
PIRiA90798. ALMSS.
RefSeqiNP_001103975.1. NM_001110505.1.
NP_031472.2. NM_007446.2.
UniGeneiMm.439727.

Genome annotation databases

EnsembliENSMUST00000067980; ENSMUSP00000070368; ENSMUSG00000074264.
ENSMUST00000106540; ENSMUSP00000102150; ENSMUSG00000074264.
GeneIDi11722.
KEGGimmu:11722.
UCSCiuc008rba.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17776.1.
PIRiA90798. ALMSS.
RefSeqiNP_001103975.1. NM_001110505.1.
NP_031472.2. NM_007446.2.
UniGeneiMm.439727.

3D structure databases

ProteinModelPortaliP00687.
SMRiP00687. Positions 17-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198093. 1 interaction.
IntActiP00687. 16 interactions.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteiP00687.

Proteomic databases

MaxQBiP00687.
PaxDbiP00687.
PRIDEiP00687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067980; ENSMUSP00000070368; ENSMUSG00000074264.
ENSMUST00000106540; ENSMUSP00000102150; ENSMUSG00000074264.
GeneIDi11722.
KEGGimmu:11722.
UCSCiuc008rba.2. mouse.

Organism-specific databases

CTDi11722.
MGIiMGI:88019. Amy1.

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00687.
KOiK01176.
OMAiKNMIDTC.
OrthoDBiEOG7RJPR2.
TreeFamiTF312850.

Enzyme and pathway databases

ReactomeiREACT_340477. Digestion of dietary carbohydrate.

Miscellaneous databases

NextBioi279401.
PROiP00687.
SOURCEiSearch...

Gene expression databases

BgeeiP00687.
CleanExiMM_AMY1.
ExpressionAtlasiP00687. baseline and differential.
GenevestigatoriP00687.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAMY1_MOUSE
AccessioniPrimary (citable) accession number: P00687
Secondary accession number(s): Q921Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: May 27, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Hepatic and salivary alpha-amylases are encoded by the same gene; however, their mRNAs have different 5'-UTR sequences.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.