ID A0A8C3X765_9CETA Unreviewed; 852 AA.
AC A0A8C3X765;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Neutral alpha-glucosidase AB {ECO:0000256|ARBA:ARBA00069533};
DE EC=3.2.1.207 {ECO:0000256|ARBA:ARBA00067008};
DE AltName: Full=Alpha-glucosidase 2 {ECO:0000256|ARBA:ARBA00080367};
DE AltName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN Name=GANAB {ECO:0000313|Ensembl:ENSCWAP00000025102.1};
OS Catagonus wagneri (Chacoan peccary).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Tayassuidae; Catagonus.
OX NCBI_TaxID=51154 {ECO:0000313|Ensembl:ENSCWAP00000025102.1, ECO:0000313|Proteomes:UP000694540};
RN [1] {ECO:0000313|Ensembl:ENSCWAP00000025102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCWAP00000025102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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:0000256|ARBA:ARBA00058913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=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)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] + H2O = N(4)-(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)-beta-D-GlcNAc)-L-
CC asparaginyl-[protein] + beta-D-glucose; 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:0000256|ARBA:ARBA00052396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=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)-beta-D-GlcNAc)-L-asparaginyl-
CC [protein] + H2O = N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + beta-D-glucose; Xref=Rhea:RHEA:56000,
CC Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC EC=3.2.1.207; Evidence={ECO:0000256|ARBA:ARBA00050632};
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000256|ARBA:ARBA00004833}.
CC -!- SUBUNIT: Heterodimer of a catalytic alpha subunit (GANAB) and a beta
CC subunit (PRKCSH). Binds glycosylated PTPRC.
CC {ECO:0000256|ARBA:ARBA00066172}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8C3X765; -.
DR Ensembl; ENSCWAT00000027211.1; ENSCWAP00000025102.1; ENSCWAG00000018894.1.
DR GeneTree; ENSGT00940000159139; -.
DR Proteomes; UP000694540; Unplaced.
DR GO; GO:0017177; C:glucosidase II complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0106407; F:Glc2Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IEA:TreeGrafter.
DR CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR CDD; cd14752; GH31_N; 1.
DR FunFam; 3.20.20.80:FF:000046; Glucosidase alpha, neutral C; 1.
DR FunFam; 3.20.20.80:FF:000039; Glucosidase, alpha neutral C; 1.
DR FunFam; 2.60.40.1180:FF:000004; neutral alpha-glucosidase AB isoform X1; 1.
DR FunFam; 2.60.40.1760:FF:000002; neutral alpha-glucosidase AB isoform X1; 1.
DR FunFam; 2.60.40.1180:FF:000023; neutral alpha-glucosidase AB isoform X2; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF162; NEUTRAL ALPHA-GLUCOSIDASE AB; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694540};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 14..232
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 295..622
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 630..718
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 735..793
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 96..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 96444 MW; B427053C90455416 CRC64;
MAAVAAVAAR RRRLSVSGQD DNSVEVTVAE GPYKIILTAR PFRLDLLEDR SLLLSVNARG
LLNFEHQRAP RVSFSDKVSL TLGSIWDKIK NLFSRQGSKD PAEGEGAQPE ETPTDGDKPE
EIQGKAEKDE PGAWEETFKT HSDSKPYGPT SVGLDFSLPG MEHVYGIPEH ADNLRLKVTE
GGEPYRLYNL DVFQYELYNP MALYGSVPVL LAHSPHRDLG IFWLNAAETW VDISSNTAGK
TLFGKMLDYL QGSGETPQTD VRWMSESGII DVFLLLGPSV FDVFRQYASL TGTQALPPLF
SLGYHQSRWN YRDEADVLEV SQGFDDHNLP CDFIWLDIEH ADGKRYFTWD PSRFPQPLTM
LEHLASKRRK LVAIVDPHIK VDSGYRVHEE LKNLGLYMKT RDGSDYEGWC WPGAAGYPDF
TNPKMRAWWA NMFRFENYEG SSSNLFVWND MNEPSVFNGP EVTMLKDTQH YGGWEHRDVH
NIYGFYVHMA TADGLVLRSG GVERPFVLSR AFFAGSQRFG AVWTGDNTAE WDHLKISIPM
CLSLGLVGLS FCGADVGGFF KNPEPELLVR WYQMGAYQPF FRAHAHLDTG RREPWLLPSQ
YQDMIRDALG QRYSLLPFWY TLFYQAHREG LPVMRPLWVH YPQDVTTFSI DDEFLLGDAL
LVHPVTDSEA HGVQVYLPGQ GEVWYDVQSY QKYHGPQTLY LPVTLSSIPV FQRGGTIVPR
WMRVRRSSDC MKNDPITLFV ALSPQGTAQG ELFLDDGHTF NYQTGHEFLL RRFSFSGNTL
VSSSADPKGH FKTPIWIERV VIIGAGKPAT VVLQTKGSPE SRLSFQHDPE TSVLILRKPG
VNVASDWSIH LR
//
