GANAB_PIG
ID GANAB_PIG Reviewed; 944 AA.
AC P79403;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Flura T., Brada D., Ziak M., Roth J.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND SIALIC ACID CONTENT.
RX PubMed=2404989; DOI=10.1083/jcb.110.2.309;
RA Brada D., Kerjaschki D., Roth J.;
RT "Cell type-specific post-Golgi apparatus localization of a 'resident'
RT endoplasmic reticulum glycoprotein, glucosidase II.";
RL J. Cell Biol. 110:309-318(1990).
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:0000269|PubMed:2404989}. Golgi apparatus
CC {ECO:0000269|PubMed:2404989}. Melanosome
CC {ECO:0000250|UniProtKB:Q14697}.
CC -!- PTM: Contains sialylated polysaccharide chains.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; U71273; AAB49757.1; -; mRNA.
DR RefSeq; NP_999069.1; NM_213904.1.
DR AlphaFoldDB; P79403; -.
DR SMR; P79403; -.
DR STRING; 9823.ENSSSCP00000025647; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PaxDb; P79403; -.
DR PeptideAtlas; P79403; -.
DR PRIDE; P79403; -.
DR GeneID; 396938; -.
DR KEGG; ssc:396938; -.
DR CTD; 23193; -.
DR eggNOG; KOG1066; Eukaryota.
DR InParanoid; P79403; -.
DR OrthoDB; 100626at2759; -.
DR UniPathway; UPA00957; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
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 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Golgi apparatus; Hydrolase; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..944
FT /note="Neutral alpha-glucosidase AB"
FT /id="PRO_0000018573"
FT REGION 181..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
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; 106662 MW; EB3096829037AAA8 CRC64;
MAAVAAVAAR RRRSWTGLVL ACLGVCLGLT LAVDRSNFKT CEESSFCKRQ RSIRPGQSPY
RALLDSLQLG PDTLTIHLIN EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV
AEPPTARLSV SGQDDNSVEV TVAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLNFEH
QRAPRVSQGS KDPAEGDGAQ PEEAPGDGDK PEEIQGKAEK DEPGAWEETF KTHSDSKPYG
PTSVGLDFSL PGMEHVYGIP EHADSLRLKV TEGGDPYRLY NLDVFQYELY NPMALYGSVP
VLLAHSPHRD LGIFWLNAAE TWVDISSNTA GKTLFGKMLD YLQGSGETPQ TDVRWMSESG
IIDVFLLLGP SVFDVFRQYA SLTGTQALPP LFSLGYHQSR WNYRDEADVL EVNQGFDDHN
LPCDFIWLDI EHADGKRYFT WDPSRFPQPR TMLEHLASKR RKLVAIVDPH IKVDSSYRVH
EELQNLGLYV KTRDGSDYEG WCWPGAASYP DFTNPKMRAW WADMFRFENY EGSSSNLYVW
NDMNEPSVFN GPEVTMLKDA QHYGGWEHRD LHNIYGFYVH MATADGLVLR SGGVERPFVL
SRAFFAGSQR FGAVWTGDNT AEWDHLKISI PMCLSLGLVG VSFCGADVGG FFKNPEPELL
VRWYQMGAYQ PFFRAHAHLD TGRREPWLLP TQYQDMIRDA LGQRYSLLPF WYTLFYQAHR
EGVPVMRALW VHYPQDVTTF SIDDEFLLGD ALLVHPVTDS EAHGVQVYLP GQGEVWYDVH
SYQKYHGPQT LYLPVTLSSI PVFQRGGTIV PRWMRVRRSS DCMKDDPITL FVALSPQGTA
QGELFLDDGH TFNYQTGHEF LLRRFSFSGN TLVSSSADSK GHFETPVWIE RVVIIGAGKP
ATVVLQTKGS PESRLSFQHD PETSVLILRK PGVNVASDWS IHLR
