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P70699 (LYAG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. 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:
Lysosomal alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Acid maltase
Gene names
Name:Gaa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for the degradation of glygogen to glucose in lysosomes.

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Subcellular location

Lysosome. Lysosome membrane By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Contains 1 P-type (trefoil) domain.

Ontologies

Keywords
   Cellular componentLysosome
Membrane
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

diaphragm contraction

Inferred from mutant phenotype PubMed 15169761. Source: MGI

glycogen catabolic process

Inferred from mutant phenotype PubMed 10838256PubMed 11328962PubMed 11785984. Source: MGI

glycogen metabolic process

Inferred from mutant phenotype PubMed 10547605PubMed 11590121PubMed 12115977PubMed 15169761PubMed 15207257PubMed 9384603PubMed 9668092. Source: MGI

heart morphogenesis

Inferred from mutant phenotype PubMed 9384603. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 10547605PubMed 10838256PubMed 9668092. Source: MGI

lysosome organization

Inferred from mutant phenotype PubMed 10547605PubMed 11328962PubMed 12115977PubMed 15169761PubMed 9384603PubMed 9668092. Source: MGI

muscle cell cellular homeostasis

Inferred from mutant phenotype PubMed 10547605PubMed 10838256PubMed 12115977PubMed 15674828PubMed 9668092. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 10838256. Source: MGI

neuromuscular process controlling posture

Inferred from mutant phenotype PubMed 10547605. Source: MGI

regulation of the force of heart contraction

Inferred from mutant phenotype PubMed 11328962. Source: MGI

striated muscle contraction

Inferred from mutant phenotype PubMed 12115977PubMed 15674828. Source: MGI

tissue development

Inferred from mutant phenotype PubMed 10547605. Source: MGI

tongue morphogenesis

Inferred from electronic annotation. Source: Ensembl

vacuolar sequestering

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle tissue morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentlysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from mutant phenotype PubMed 15207257. Source: MGI

   Molecular_functionalpha-glucosidase activity

Inferred from direct assay PubMed 7323947. Source: MGI

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 6942 By similarity
PRO_0000018569
Chain70 – 953884Lysosomal alpha-glucosidase
PRO_0000018570

Regions

Domain80 – 13152P-type

Sites

Active site5181Nucleophile By similarity
Active site5211 By similarity

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Ref.5
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Ref.5
Glycosylation8831N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation9331N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 109 By similarity
Disulfide bond92 ↔ 108 By similarity
Disulfide bond103 ↔ 127 By similarity

Experimental info

Sequence conflict621K → E in AAB06943. Ref.1
Sequence conflict2541S → A in AAB06943. Ref.1
Sequence conflict430 – 4312EL → DV in AAB06943. Ref.1
Sequence conflict4341D → G Ref.1
Sequence conflict4341D → G Ref.3
Sequence conflict4811W → C in AAB06943. Ref.1
Sequence conflict6151G → E in AAB06943. Ref.1
Sequence conflict6191S → T in AAB06943. Ref.1
Sequence conflict7321P → R in AAB06943. Ref.1
Sequence conflict7771M → V Ref.1
Sequence conflict7771M → V Ref.3
Sequence conflict8711R → H in AAB06943. Ref.1
Sequence conflict9031R → K in AAB06943. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70699 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 956B89685FB5FF81

FASTA953106,248
        10         20         30         40         50         60 
MNIRKPLCSN SVVGACTLIS LTTAVILGHL MLRELMLLPQ DLHESSSGLW KTYRPHHQEG 

        70         80         90        100        110        120 
YKPGPLHIQE QTEQPKEAPT QCDVPPSSRF DCAPDKGISQ EQCEARGCCY VPAGQVLKEP 

       130        140        150        160        170        180 
QIGQPWCFFP PSYPSYRLEN LSSTESGYTA TLTRTSPTFF PKDVLTLQLE VLMETDSRLH 

       190        200        210        220        230        240 
FKIKDPASKR YEVPLETPRV LSQAPSPLYS VEFSEEPFGV IVRRKLGGRV LLNTTVAPLF 

       250        260        270        280        290        300 
FADQFLQLST SLPSQHITGL GEHLSPLMLS TDWARITLWN RDTPPSQGTN LYGSHPFYLA 

       310        320        330        340        350        360 
LEDGGLAHGV FLLNSNAMDV ILQPSPALTW RSTGGILDVY VFLGPEPKSV VQQYLDVVGY 

       370        380        390        400        410        420 
PFMPPYWGLG FHLCRWGYSS TAIVRQVVEN MTRTHFPLDV QWNDLDYMDA RRDFTFNQDS 

       430        440        450        460        470        480 
FADFPDMVRE LHQDGRRYMM IVDPAISSAG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV 

       490        500        510        520        530        540 
WPGTTAFPDF TNPETLDWWQ DMVSEFHAQV PFDGMWLDMN EPSNFVRGSQ QGCPNNELEN 

       550        560        570        580        590        600 
PPYVPGVVGG ILQAATICAS SHQFLSTHYN LHNLYGLTEA IASSRALVKT RGTRPFVISR 

       610        620        630        640        650        660 
STFSGHGRYA GHWTGDVRSS WEHLAYSVPD ILQFNLLGVP LVGADICGFI GDTSEELCVR 

       670        680        690        700        710        720 
WTQLGAFYPF MRNHNDLNSV PQEPYRFSET AQQAMRKAFA LRYALLPYLY TLFHRAHVRG 

       730        740        750        760        770        780 
DTVARPLFLE FPEDPSTWSV DRQLLWGPAL LITPVLEPGK TEVTGYFPKG TWYNMQMVSV 

       790        800        810        820        830        840 
DSLGTLPSPS SASSFRSAVQ SKGQWLTLEA PLDTINVHLR EGYIIPLQGP SLTTTESRKQ 

       850        860        870        880        890        900 
PMALAVALTA SGEADGELFW DDGESLAVLE RGAYTLVTFS AKNNTIVNKL VRVTKEGAEL 

       910        920        930        940        950 
QLREVTVLGV ATAPTQVLSN GIPVSNFTYS PDNKSLAIPV SLLMGELFQI SWS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the mouse liver cDNA encoding lysosomal alpha-glucosidase."
Ding J.H., Yang B.Z., Reuser A.J.J., Roe C.R.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"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 and NOD.
Tissue: Bone marrow, Brain cortex, Heart and Thymus.
[3]"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.
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 376-385, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-470.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49351 mRNA. Translation: AAB06943.1.
AK052211 mRNA. Translation: BAC34888.1.
AK088481 mRNA. Translation: BAC40382.1.
AK139333 mRNA. Translation: BAE23960.1.
AK146538 mRNA. Translation: BAE27243.1.
AK150970 mRNA. Translation: BAE30001.1.
BC010210 mRNA. Translation: AAH10210.1.
RefSeqNP_001152796.1. NM_001159324.1.
NP_032090.3. NM_008064.3.
UniGeneMm.4793.

3D structure databases

ProteinModelPortalP70699.
SMRP70699. Positions 73-953.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP70699. 1 interaction.
MINTMINT-4100796.

Chemistry

BindingDBP70699.
ChEMBLCHEMBL1667668.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSiteP70699.

Proteomic databases

PaxDbP70699.
PRIDEP70699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026666; ENSMUSP00000026666; ENSMUSG00000025579.
ENSMUST00000106259; ENSMUSP00000101866; ENSMUSG00000025579.
GeneID14387.
KEGGmmu:14387.
UCSCuc007mqg.2. mouse.

Organism-specific databases

CTD2548.
MGIMGI:95609. Gaa.

Phylogenomic databases

eggNOGCOG1501.
GeneTreeENSGT00740000115444.
HOGENOMHOG000041175.
HOVERGENHBG006297.
InParanoidP70699.
KOK12316.
OMASSEMGYT.
OrthoDBEOG77HDD0.
PhylomeDBP70699.
TreeFamTF314577.

Gene expression databases

ArrayExpressP70699.
BgeeP70699.
CleanExMM_GAA.
GenevestigatorP70699.

Family and domain databases

Gene3D4.10.110.10. 1 hit.
InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR000519. P_trefoil.
IPR017957. P_trefoil_CS.
[Graphical view]
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
PF00088. Trefoil. 1 hit.
[Graphical view]
SMARTSM00018. PD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
PS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285901.
PROP70699.
SOURCESearch...

Entry information

Entry nameLYAG_MOUSE
AccessionPrimary (citable) accession number: P70699
Secondary accession number(s): Q3UJB2, Q8BGI6, Q91Z45
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 119 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