GANAB_MACFA
ID GANAB_MACFA Reviewed; 944 AA.
AC Q4R4N7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Neutral alpha-glucosidase AB;
DE EC=3.2.1.207 {ECO:0000250|UniProtKB:Q8BHN3};
DE AltName: Full=Alpha-glucosidase 2;
DE AltName: Full=Glucosidase II subunit alpha;
DE Flags: Precursor;
GN Name=GANAB; ORFNames=QccE-15075;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of glucosidase II that cleaves sequentially
CC the 2 innermost alpha-1,3-linked glucose residues from the
CC Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature
CC glycoproteins. Required for PKD1/Polycystin-1 and PKD2/Polycystin-2
CC maturation and localization to the cell surface and cilia.
CC {ECO:0000250|UniProtKB:Q14697, ECO:0000250|UniProtKB:Q8BHN3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] = beta-D-glucose + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC [protein] (N-glucan mannose isomer 9A1,2,3B1,2,3);
CC Xref=Rhea:RHEA:56000, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59080,
CC ChEBI:CHEBI:139493; EC=3.2.1.207;
CC Evidence={ECO:0000250|UniProtKB:Q8BHN3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-
CC asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc)-L-asparaginyl-[protein]; Xref=Rhea:RHEA:55996,
CC Rhea:RHEA-COMP:14355, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:59082;
CC EC=3.2.1.207; Evidence={ECO:0000250|UniProtKB:Q8BHN3};
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000250|UniProtKB:Q8BHN3}.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta
CC subunit (PRKCSH). Binds glycosylated PTPRC.
CC {ECO:0000250|UniProtKB:Q8BHN3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q14697}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P79403}. Melanosome
CC {ECO:0000250|UniProtKB:Q14697}.
CC -!- PTM: Contains sialylated polysaccharide chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; AB169857; BAE01938.1; -; mRNA.
DR RefSeq; NP_001272004.1; NM_001285075.1.
DR AlphaFoldDB; Q4R4N7; -.
DR SMR; Q4R4N7; -.
DR STRING; 9541.XP_005577635.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR GeneID; 101865428; -.
DR CTD; 23193; -.
DR eggNOG; KOG1066; Eukaryota.
DR UniPathway; UPA00957; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0017177; C:glucosidase II complex; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0090599; F:alpha-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Golgi apparatus; Hydrolase; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..944
FT /note="Neutral alpha-glucosidase AB"
FT /id="PRO_0000328192"
FT REGION 181..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /note="Nucleophile"
FT ACT_SITE 618
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT BINDING 602
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT BINDING 676
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14697"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..47
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
FT DISULFID 633..644
FT /evidence="ECO:0000250|UniProtKB:Q8BHN3"
SQ SEQUENCE 944 AA; 106890 MW; F01221F50170ABCE CRC64;
MAEVAAVAAR RRRSWASLVL VFLGVCLGIT LAVDRSNFKT CEESSFCKRQ RSIRPGLSPY
RALLDSLQLG PDSLTVHLNH EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV
ADPPIARLSV SGRDDNSVEL TMAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLEFEH
QRAPRVSQGS KDPAEGDGAQ PEETPRDGDK PEETQGKAEK DEPGAWEETF KTHSDSKPYG
PMSVGLDFSL PGMEHVYGIP EHADNLRLKV TEGGEPYRLY NLDVFQYELY NPMALYGSVP
VLLAHNPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMMD YLQGSGETPQ TDVRWMSETG
IIDVFLLLGP SISDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVDQGFDEHN
LPCDVIWLDI EHADGKRYFT WDPSRFPQPR TMLERLASKR RKLVAIVDPH IKVDSGYRVH
DELRNLGLYV KTRDGSDYEG WCWPGSAGYP DFTNPTMRAW WANMFSYDNY EGSAPNLFVW
NDMNEPSVFN GPEVTMLKDA QHYGGWEHRD VHNIYGLYVH MATADGLRQR SGGMERPFVL
ARAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG LSFCGADVGG FFKNPEPELL
VRWYQMGAYQ PFFRAHAHLD TGRRGPWLLP SQHNDIIRDA LGQRYSLLPF WYTLFYQAHR
EGIPIMRPLW VQYPQDVTTF SIDDQYLLGD ALLVHPVSDS GAHGVQVYLP GQGEVWYDIQ
SYQKHHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS ECMKDDPITL FVALSPQGTA
EGELFLDDGH TFNYETRQEF LLRRFLFSGN TLVSSSADPE GHFETPIWIE RVVIIGAGKP
AAVVLQTKGS PESRLSFQHD PETSVLVLRK PGINVASDWS IHLR
