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Q8BHN3 (GANAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutral alpha-glucosidase AB

EC=3.2.1.84
Alternative name(s):
Alpha-glucosidase 2
Glucosidase II subunit alpha
Gene names
Name:Ganab
Synonyms:G2an, Kiaa0088
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length944 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins.

Catalytic activity

Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.

Pathway

Glycan metabolism; N-glycan metabolism.

Subunit structure

Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH). Binds glycosylated PTPRC. Ref.1

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Melanosome By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Sequence caution

The sequence BAC65483.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BHN3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BHN3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     187-187: P → PFSDKVSLALGSVWDKIKNLFSR
Isoform 3 (identifier: Q8BHN3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.
Note: May be due to an intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Ref.1
Chain33 – 944912Neutral alpha-glucosidase AB
PRO_0000018572

Sites

Active site5421Nucleophile By similarity
Active site5451 By similarity
Active site6181Proton donor By similarity

Amino acid modifications

Glycosylation971N-linked (GlcNAc...)

Natural variations

Alternative sequence1 – 252252Missing in isoform 3.
VSP_010675
Alternative sequence1871P → PFSDKVSLALGSVWDKIKNL FSR in isoform 2.
VSP_010676

Experimental info

Sequence conflict6471D → N in BAB30982. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 01489861A537416E

FASTA944106,911
        10         20         30         40         50         60 
MAAIAAVAAR RRRSWLSLVL AYLGVCLGIT LAVDRSNFKT CDESSFCKRQ RSIRPGLSPY 

        70         80         90        100        110        120 
RALLDTLQLG PDALTVHLIH EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV 

       130        140        150        160        170        180 
ADPPTARLSV SGRDDNSVEL TVAEGPYKII LTAQPFRLDL LEDRSLLLSV NARGLMAFEH 

       190        200        210        220        230        240 
QRAPRVPQES KDPAEGNGAQ PEATPGDGDK PEETQEKAEK DEPGAWEETF KTHSDSKPYG 

       250        260        270        280        290        300 
PTSVGLDFSL PGMEHVYGIP EHADSLRLKV TEGGEPYRLY NLDVFQYELN NPMALYGSVP 

       310        320        330        340        350        360 
VLLAHSFHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMLD YLQGSGETPQ TDIRWMSESG 

       370        380        390        400        410        420 
IIDVFLMLGP SVFDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDDHN 

       430        440        450        460        470        480 
MPCDVIWLDI EHADGKRYFT WDPTRFPQPL NMLEHLASKR RKLVAIVDPH IKVDSGYRVH 

       490        500        510        520        530        540 
EELRNHGLYV KTRDGSDYEG WCWPGSASYP DFTNPRMRAW WSNMFSFDNY EGSAPNLYVW 

       550        560        570        580        590        600 
NDMNEPSVFN GPEVTMLKDA VHYGGWEHRD IHNIYGLYVH MATADGLIQR SGGIERPFVL 

       610        620        630        640        650        660 
SRAFFSGSQR FGAVWTGDNT AEWDHLKISI PMCLSLALVG LSFCGADVGG FFKNPEPELL 

       670        680        690        700        710        720 
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLA SQYQDAIRDA LFQRYSLLPF WYTLFYQAHK 

       730        740        750        760        770        780 
EGFPVMRPLW VQYPEDMSTF SIEDQFMLGD ALLIHPVSDA GAHGVQVYLP GQEEVWYDIQ 

       790        800        810        820        830        840 
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS DCMKDDPITL FVALSPQGTA 

       850        860        870        880        890        900 
QGELFLDDGH TFNYQTRHEF LLRRFSFSGS TLVSSSADPK GHLETPIWIE RVVIMGAGKP 

       910        920        930        940 
AAVVLQTKGS PESRLSFQHD PETSVLILRK PGVSVASDWS IHLR 

« Hide

Isoform 2 [UniParc].

Checksum: E3E507E2E2E68C75
Show »

FASTA966109,404
Isoform 3 [UniParc].

Checksum: E4877A7B38966E3C
Show »

FASTA69279,082

References

« Hide 'large scale' references
[1]"Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."
Arendt C.W., Ostergaard H.L.
J. Biol. Chem. 272:13117-13125(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 33-50; 176-187; 823-839 AND 895-905, HETERODIMERIZATION WITH PRKCSH.
Tissue: T-cell lymphoma.
[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] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo and Head.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[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] (ISOFORM 1).
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 62-96; 134-173; 338-354; 378-400; 438-459; 591-610; 654-662; 685-698; 785-805; 864-880; 892-908 AND 915-944, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Specific isoforms of the resident endoplasmic reticulum protein glucosidase II associate with the CD45 protein-tyrosine phosphatase via a lectin-like interaction."
Baldwin T.A., Gogela-Spehar M., Ostergaard H.L.
J. Biol. Chem. 275:32071-32076(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GLYCOSYLATED PTPRC, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92793 mRNA. Translation: AAC53182.1.
AK017873 mRNA. Translation: BAB30982.1.
AK030722 mRNA. Translation: BAC27099.1.
AK081915 mRNA. Translation: BAC38370.1.
AK122201 mRNA. Translation: BAC65483.1. Different initiation.
BC094437 mRNA. Translation: AAH94437.1.
BC117888 mRNA. Translation: AAI17889.1.
BC117889 mRNA. Translation: AAI17890.1.
RefSeqNP_032086.1. NM_008060.1.
XP_006526739.1. XM_006526676.1.
UniGeneMm.3196.

3D structure databases

ProteinModelPortalQ8BHN3.
SMRQ8BHN3. Positions 38-943.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199786. 1 interaction.
IntActQ8BHN3. 6 interactions.
MINTMINT-1863945.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSiteQ8BHN3.

Proteomic databases

PaxDbQ8BHN3.
PRIDEQ8BHN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000096246; ENSMUSP00000093965; ENSMUSG00000071650. [Q8BHN3-2]
GeneID14376.
KEGGmmu:14376.
UCSCuc008gnx.1. mouse. [Q8BHN3-1]

Organism-specific databases

CTD23193.
MGIMGI:1097667. Ganab.
RougeSearch...

Phylogenomic databases

eggNOGCOG1501.
GeneTreeENSGT00740000115152.
HOGENOMHOG000115864.
HOVERGENHBG051683.
KOK05546.
OMAAIDDQLY.
OrthoDBEOG7VQJDS.
PhylomeDBQ8BHN3.
TreeFamTF300337.

Enzyme and pathway databases

UniPathwayUPA00957.

Gene expression databases

ArrayExpressQ8BHN3.
BgeeQ8BHN3.
CleanExMM_GANAB.
GenevestigatorQ8BHN3.

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 2 hits.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285877.
PROQ8BHN3.
SOURCESearch...

Entry information

Entry nameGANAB_MOUSE
AccessionPrimary (citable) accession number: Q8BHN3
Secondary accession number(s): O08794 expand/collapse secondary AC list , Q149A6, Q80U81, Q9CS53
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 97 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries