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P00688

- AMYP_MOUSE

UniProt

P00688 - AMYP_MOUSE

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Protein

Pancreatic alpha-amylase

Gene

Amy2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 Ca(2+) 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 bindingi170 – 1701Calcium; via carbonyl oxygenBy similarity
Metal bindingi179 – 1791CalciumBy similarity
Binding sitei207 – 2071ChlorideBy similarity
Active sitei209 – 2091NucleophileBy similarity
Metal bindingi213 – 2131Calcium; via carbonyl oxygenBy similarity
Active sitei245 – 2451Proton donorBy similarity
Binding sitei310 – 3101ChlorideBy similarity
Sitei312 – 3121Transition state stabilizerBy similarity
Binding sitei349 – 3491ChlorideBy similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. chloride ion binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB
Complete GO annotation...

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:
Pancreatic alpha-amylase (EC:3.2.1.1)
Short name:
PA
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:Amy2
Synonyms:Amy2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:88020. Amy2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Chaini16 – 508493Pancreatic alpha-amylasePRO_0000001398Add
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 ↔ 172By similarity
Disulfide bondi390 ↔ 396By similarity
Disulfide bondi462 ↔ 474By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP00688.
PaxDbiP00688.
PRIDEiP00688.

2D gel databases

SWISS-2DPAGEP00688.

PTM databases

PhosphoSiteiP00688.

Expressioni

Gene expression databases

GenevestigatoriP00688.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000096264.

Structurei

3D structure databases

ProteinModelPortaliP00688.
SMRiP00688. Positions 16-508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
GeneTreeiENSGT00390000002882.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00688.
KOiK01176.
OMAiSNTYITA.
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.

P00688-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFVLLLSLI GFCWAQYDPH TSDGRTAIVH LFEWRWVDIA KECERYLAPK
60 70 80 90 100
GFGGVQVSPP NENVVVHNPS RPWWERYQPI SYKICTRSGN EDEFRDMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGA GNPAGTSSTC GSYLNPNNRE FPAVPYSAWD
160 170 180 190 200
FNDNKCNGEI DNYNDAYQVR NCRLTGLLDL ALEKDYVRTK VADYMNHLID
210 220 230 240 250
IGVAGFRLDA AKHMWPGDIK AVLDKLHNLN TKWFSQGSRP FIFQEVIDLG
260 270 280 290 300
GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGLVP
310 320 330 340 350
SDRALVFVDN HDNQRGHGAG GSSILTFWDA RMYKMAVGFM LAHPYGFTRV
360 370 380 390 400
MSSYRWNRNF QNGKDQNDWI GPPNNNGVTK EVTINADTTC GNDWVCEHRW
410 420 430 440 450
RQIRNMVAFR NVVNGQPFSN WWDNNSNQVA FSRGNRGFIV FNNDDWALSA
460 470 480 490 500
TLQTGLPAGT YCDVISGDKV DGNCTGLRVN VGSDGKAHFS ISNSAEDPFI

AIHADSKL
Length:508
Mass (Da):57,318
Last modified:July 27, 2011 - v2
Checksum:iB204B03768132593
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701S → T in AAA37228. (PubMed:6176715)Curated
Sequence conflicti85 – 851C → S in AAA37228. (PubMed:6176715)Curated
Sequence conflicti217 – 2171G → R in CAA24098. (PubMed:6157477)Curated
Sequence conflicti217 – 2171G → R in CAA26413. (PubMed:6098446)Curated
Sequence conflicti217 – 2171G → R in CAA26414. (PubMed:6098446)Curated
Sequence conflicti217 – 2171G → R in CAA26415. (PubMed:6098446)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641V → I in A1, B(C) and AMY-2.2Y.
Natural varianti66 – 661V → I in AMY-2.2Y.
Natural varianti120 – 1201A → S in A1, B(A) and B(C).
Natural varianti161 – 1611D → S in A1, B(A) and B(C); requires 2 nucleotide substitutions.
Natural varianti174 – 1741L → V in A1 and B(C).
Natural varianti175 – 1751T → S in B(A).
Natural varianti254 – 2541I → V in A1 and B(C).
Natural varianti270 – 2723YGA → FGV in A1 and B(C).
Natural varianti298 – 2981L → M in A1, B(A) and B(C).
Natural varianti322 – 3221S → A in B(A).
Natural varianti419 – 4191S → A in B1.
Natural varianti450 – 4501A → E in B(C).

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00718 mRNA. Translation: CAA24098.1.
X02576 mRNA. Translation: CAA26413.1.
X02577 mRNA. Translation: CAA26414.1.
X02578 mRNA. Translation: CAA26415.1.
AK133526 mRNA. Translation: BAE21706.1.
BC094924 mRNA. Translation: AAH94924.1.
BC100579 mRNA. Translation: AAI00580.1.
J00357 Genomic DNA. Translation: AAA37228.1.
J00358 Genomic DNA. Translation: AAA37229.1.
J00361 Genomic DNA. Translation: AAA37233.1.
X02343 Genomic DNA. Translation: CAA26202.1.
M16540 Genomic DNA. Translation: AAA37223.1.
M15965 Genomic DNA. Translation: AAA37226.1.
M11895 mRNA. Translation: AAA37224.1.
M11896 mRNA. Translation: AAA37227.1.
M11891 Genomic DNA. Translation: AAA37222.1.
CCDSiCCDS17775.1.
PIRiA90995. ALMSP1.
B90798. ALMSP.
B90995. ALMSPC.
C90995. ALMSPA.
I49493.
I49494.
RefSeqiNP_001036176.1. NM_001042711.2.
NP_001153622.1. NM_001160150.1.
NP_001153623.1. NM_001160151.1.
NP_001153624.1. NM_001160152.1.
UniGeneiMm.275426.
Mm.443376.
Mm.462977.

Genome annotation databases

EnsembliENSMUST00000098667; ENSMUSP00000096264; ENSMUSG00000096569.
ENSMUST00000098673; ENSMUSP00000096270; ENSMUSG00000074268.
ENSMUST00000179314; ENSMUSP00000136894; ENSMUSG00000093931.
ENSMUST00000179568; ENSMUSP00000137025; ENSMUSG00000096770.
GeneIDi100043684.
100043686.
100043688.
109959.
KEGGimmu:100043684.
mmu:100043686.
mmu:100043688.
mmu:109959.
UCSCiuc008rav.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00718 mRNA. Translation: CAA24098.1 .
X02576 mRNA. Translation: CAA26413.1 .
X02577 mRNA. Translation: CAA26414.1 .
X02578 mRNA. Translation: CAA26415.1 .
AK133526 mRNA. Translation: BAE21706.1 .
BC094924 mRNA. Translation: AAH94924.1 .
BC100579 mRNA. Translation: AAI00580.1 .
J00357 Genomic DNA. Translation: AAA37228.1 .
J00358 Genomic DNA. Translation: AAA37229.1 .
J00361 Genomic DNA. Translation: AAA37233.1 .
X02343 Genomic DNA. Translation: CAA26202.1 .
M16540 Genomic DNA. Translation: AAA37223.1 .
M15965 Genomic DNA. Translation: AAA37226.1 .
M11895 mRNA. Translation: AAA37224.1 .
M11896 mRNA. Translation: AAA37227.1 .
M11891 Genomic DNA. Translation: AAA37222.1 .
CCDSi CCDS17775.1.
PIRi A90995. ALMSP1.
B90798. ALMSP.
B90995. ALMSPC.
C90995. ALMSPA.
I49493.
I49494.
RefSeqi NP_001036176.1. NM_001042711.2.
NP_001153622.1. NM_001160150.1.
NP_001153623.1. NM_001160151.1.
NP_001153624.1. NM_001160152.1.
UniGenei Mm.275426.
Mm.443376.
Mm.462977.

3D structure databases

ProteinModelPortali P00688.
SMRi P00688. Positions 16-508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000096264.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSitei P00688.

2D gel databases

SWISS-2DPAGE P00688.

Proteomic databases

MaxQBi P00688.
PaxDbi P00688.
PRIDEi P00688.

Protocols and materials databases

DNASUi 109959.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098667 ; ENSMUSP00000096264 ; ENSMUSG00000096569 .
ENSMUST00000098673 ; ENSMUSP00000096270 ; ENSMUSG00000074268 .
ENSMUST00000179314 ; ENSMUSP00000136894 ; ENSMUSG00000093931 .
ENSMUST00000179568 ; ENSMUSP00000137025 ; ENSMUSG00000096770 .
GeneIDi 100043684.
100043686.
100043688.
109959.
KEGGi mmu:100043684.
mmu:100043686.
mmu:100043688.
mmu:109959.
UCSCi uc008rav.2. mouse.

Organism-specific databases

CTDi 100043684.
100043686.
100043688.
109959.
MGIi MGI:88020. Amy2.

Phylogenomic databases

eggNOGi COG0366.
GeneTreei ENSGT00390000002882.
HOGENOMi HOG000253313.
HOVERGENi HBG000061.
InParanoidi P00688.
KOi K01176.
OMAi SNTYITA.
OrthoDBi EOG7RJPR2.
TreeFami TF312850.

Enzyme and pathway databases

Reactomei REACT_217960. Digestion of dietary carbohydrate.

Miscellaneous databases

NextBioi 456822.
PROi P00688.
SOURCEi Search...

Gene expression databases

Genevestigatori P00688.

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

« 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 [GENOMIC DNA].
  2. "Multiple non-allelic genes encoding pancreatic alpha-amylase of mouse are expressed in a strain-specific fashion."
    Tosi M., Bovey R., Astolfi S., Bodary S., Meisler M.H., Wellauer P.K.
    EMBO J. 3:2809-2816(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOZYMES A1; B(A) AND B(C)).
    Strain: CE/J.
  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: Ovary and Uterus.
  4. "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].
    Tissue: Pancreas.
  5. "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 1-94 AND 267-290.
    Strain: A/J.
  6. "Members of the Amy-2 alpha-amylase gene family of mouse strain CE/J contain duplicated 5' termini."
    Bodary S., Grossi G., Hagenbuechle O., Wellauer P.K.
    J. Mol. Biol. 182:1-10(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
  7. "Tissue-specific and insulin-dependent expression of a pancreatic amylase gene in transgenic mice."
    Osborn L., Rosenberg M.P., Keller S.A., Meisler M.H.
    Mol. Cell. Biol. 7:326-334(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94 (ISOZYMES AMY-2.1Y AND AMY-2.2Y).
  8. "Evolution of the amylase multigene family. YBR/Ki mice express a pancreatic amylase gene which is silent in other strains."
    Gumucio D.L., Wiebauer K., Dranginis A., Samuelson L.C., Treisman L.O., Caldwell R.M., Antonucci T.K., Meisler M.H.
    J. Biol. Chem. 260:13483-13489(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 267-289 AND 388-470 (ISOZYMES A1 AND B1).
    Strain: YRB/KI.
  9. "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. 126:293-296(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLN-16.
  10. "Two distinct pancreatic amylase genes are active in YBR mice."
    Strahler J.R., Meisler M.
    Genetics 101:91-102(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 407-458.
    Strain: YBR.

Entry informationi

Entry nameiAMYP_MOUSE
AccessioniPrimary (citable) accession number: P00688
Secondary accession number(s): Q4VBW6
, Q61295, Q61296, Q64301
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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