Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00687

- AMY1_MOUSE

UniProt

P00687 - AMY1_MOUSE

Protein

Alpha-amylase 1

Gene

Amy1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 calcium ion per subunit.By similarity
    Binds 1 chloride 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

    1. alpha-amylase activity Source: UniProtKB-EC
    2. amylase activity Source: MGI
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Chloride, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_217960. 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: Chromosome 3

    Organism-specific databases

    MGIiMGI:88019. Amy1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: MGI

    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

    ArrayExpressiP00687.
    BgeeiP00687.
    CleanExiMM_AMY1.
    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.
    InParanoidiQ921Y7.
    KOiK01176.
    OMAiDANDWIG.
    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

    MKFFLLLSLI GFCWAQYDPH TQYGRTAIVH LFEWRWVDIA KECERYLAPN    50
    GFAGVQVSPP NENIVVHSPS RPWWERYQPI SYKICSRSGN EDEFRDMVNR 100
    CNNVGVRIYV DAVINHMCGV GAQAGQSSTC GSYFNPNNRD FPGVPYSGFD 150
    FNDGKCRTAS GGIENYQDAA QVRDCRLSGL LDLALEKDYV RTKVADYMNH 200
    LIDIGVAGFR LDASKHMWPG DIKAILDKLH NLNTKWFSQG SRPFIFQEVI 250
    DLGGEAVSSN EYFGNGRVTE FKYGAKLGKV MRKWDGEKMS YLKNWGEGWG 300
    LMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF 350
    TRVMSSYYWP RNFQNGKDVN DWVGPPNNNG KTKEVSINPD STCGNDWICE 400
    HRWRQIRNMV AFRNVVNGQP FANWWDNDSN QVAFGRGNKG FIVFNNDDWA 450
    LSETLQTGLP AGTYCDVISG DKVDGNCTGI KVYVGNDGKA HFSISNSAED 500
    PFIAIHAESK I 511
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17776.1.
    PIRi A90798. ALMSS.
    RefSeqi NP_001103975.1. NM_001110505.1.
    NP_031472.2. NM_007446.2.
    UniGenei Mm.439727.

    3D structure databases

    ProteinModelPortali P00687.
    SMRi P00687. Positions 17-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198093. 1 interaction.
    IntActi P00687. 16 interactions.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    PTM databases

    PhosphoSitei P00687.

    Proteomic databases

    MaxQBi P00687.
    PaxDbi P00687.
    PRIDEi P00687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067980 ; ENSMUSP00000070368 ; ENSMUSG00000074264 .
    ENSMUST00000106540 ; ENSMUSP00000102150 ; ENSMUSG00000074264 .
    GeneIDi 11722.
    KEGGi mmu:11722.
    UCSCi uc008rba.2. mouse.

    Organism-specific databases

    CTDi 11722.
    MGIi MGI:88019. Amy1.

    Phylogenomic databases

    eggNOGi COG0366.
    GeneTreei ENSGT00390000002882.
    HOGENOMi HOG000253313.
    HOVERGENi HBG000061.
    InParanoidi Q921Y7.
    KOi K01176.
    OMAi DANDWIG.
    OrthoDBi EOG7RJPR2.
    TreeFami TF312850.

    Enzyme and pathway databases

    Reactomei REACT_217960. Digestion of dietary carbohydrate.

    Miscellaneous databases

    ChiTaRSi AMY1A. mouse.
    NextBioi 279401.
    PROi P00687.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00687.
    Bgeei P00687.
    CleanExi MM_AMY1.
    Genevestigatori P00687.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 140 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