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P00688 (AMYP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. 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:
Pancreatic alpha-amylase

Short name=PA
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:Amy2
Synonyms:Amy2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length508 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

Secretedextracellular space.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Chain16 – 508493Pancreatic alpha-amylase
PRO_0000001398

Sites

Active site2091Nucleophile By similarity
Active site2451Proton donor By similarity
Metal binding1151Calcium By similarity
Metal binding1701Calcium; via carbonyl oxygen By similarity
Metal binding1791Calcium By similarity
Metal binding2131Calcium; via carbonyl oxygen By similarity
Binding site2071Chloride By similarity
Binding site3101Chloride By similarity
Binding site3491Chloride By similarity
Site3121Transition state stabilizer By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid
Disulfide bond43 ↔ 101 By similarity
Disulfide bond85 ↔ 130 By similarity
Disulfide bond156 ↔ 172 By similarity
Disulfide bond390 ↔ 396 By similarity
Disulfide bond462 ↔ 474 By similarity

Natural variations

Natural variant641V → I in A1, B(C) and AMY-2.2Y.
Natural variant661V → I in AMY-2.2Y.
Natural variant1201A → S in A1, B(A) and B(C).
Natural variant1611D → S in A1, B(A) and B(C); requires 2 nucleotide substitutions.
Natural variant1741L → V in A1 and B(C).
Natural variant1751T → S in B(A).
Natural variant2541I → V in A1 and B(C).
Natural variant270 – 2723YGA → FGV in A1 and B(C).
Natural variant2981L → M in A1, B(A) and B(C).
Natural variant3221S → A in B(A).
Natural variant4191S → A in B1.
Natural variant4501A → E in B(C).

Experimental info

Sequence conflict701S → T in AAA37228. Ref.5
Sequence conflict851C → S in AAA37228. Ref.5
Sequence conflict2171G → R in CAA24098. Ref.1
Sequence conflict2171G → R in CAA26413. Ref.2
Sequence conflict2171G → R in CAA26414. Ref.2
Sequence conflict2171G → R in CAA26415. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00688 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: B204B03768132593

FASTA50857,318
        10         20         30         40         50         60 
MKFVLLLSLI GFCWAQYDPH TSDGRTAIVH LFEWRWVDIA KECERYLAPK GFGGVQVSPP 

        70         80         90        100        110        120 
NENVVVHNPS RPWWERYQPI SYKICTRSGN EDEFRDMVTR CNNVGVRIYV DAVINHMCGA 

       130        140        150        160        170        180 
GNPAGTSSTC GSYLNPNNRE FPAVPYSAWD FNDNKCNGEI DNYNDAYQVR NCRLTGLLDL 

       190        200        210        220        230        240 
ALEKDYVRTK VADYMNHLID IGVAGFRLDA AKHMWPGDIK AVLDKLHNLN TKWFSQGSRP 

       250        260        270        280        290        300 
FIFQEVIDLG GEAIKGSEYF GNGRVTEFKY GAKLGTVIRK WNGEKMSYLK NWGEGWGLVP 

       310        320        330        340        350        360 
SDRALVFVDN HDNQRGHGAG GSSILTFWDA RMYKMAVGFM LAHPYGFTRV MSSYRWNRNF 

       370        380        390        400        410        420 
QNGKDQNDWI GPPNNNGVTK EVTINADTTC GNDWVCEHRW RQIRNMVAFR NVVNGQPFSN 

       430        440        450        460        470        480 
WWDNNSNQVA FSRGNRGFIV FNNDDWALSA TLQTGLPAGT YCDVISGDKV DGNCTGLRVN 

       490        500 
VGSDGKAHFS ISNSAEDPFI AIHADSKL 

« 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 [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. 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: 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17775.1.
PIRALMSP1. A90995.
ALMSP. B90798.
ALMSPC. B90995.
ALMSPA. C90995.
I49493.
I49494.
RefSeqNP_001036176.1. NM_001042711.2.
NP_001153622.1. NM_001160150.1.
NP_001153623.1. NM_001160151.1.
NP_001153624.1. NM_001160152.1.
UniGeneMm.275426.
Mm.443376.
Mm.462977.

3D structure databases

ProteinModelPortalP00688.
SMRP00688. Positions 16-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000096264.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

PhosphoSiteP00688.

2D gel databases

SWISS-2DPAGEP00688.

Proteomic databases

MaxQBP00688.
PaxDbP00688.
PRIDEP00688.

Protocols and materials databases

DNASU109959.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098667; ENSMUSP00000096264; ENSMUSG00000096569.
ENSMUST00000098673; ENSMUSP00000096270; ENSMUSG00000074268.
ENSMUST00000179314; ENSMUSP00000136894; ENSMUSG00000093931.
ENSMUST00000179568; ENSMUSP00000137025; ENSMUSG00000096770.
GeneID100043684.
100043686.
100043688.
109959.
KEGGmmu:100043684.
mmu:100043686.
mmu:100043688.
mmu:109959.
UCSCuc008rav.2. mouse.

Organism-specific databases

CTD100043684.
100043686.
100043688.
109959.
MGIMGI:88020. Amy2.

Phylogenomic databases

eggNOGCOG0366.
GeneTreeENSGT00390000002882.
HOGENOMHOG000253313.
HOVERGENHBG000061.
InParanoidQ4VBW6.
KOK01176.
OMASNTYITA.
OrthoDBEOG7RJPR2.
TreeFamTF312850.

Gene expression databases

GenevestigatorP00688.

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

NextBio456822.
PROP00688.
SOURCESearch...

Entry information

Entry nameAMYP_MOUSE
AccessionPrimary (citable) accession number: P00688
Secondary accession number(s): Q4VBW6 expand/collapse secondary AC list , Q61295, Q61296, Q64301
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 143 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