ID L5KQE8_PTEAL Unreviewed; 966 AA.
AC L5KQE8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 28-JAN-2026, entry version 38.
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 ORFNames=PAL_GLEAN10011478 {ECO:0000313|EMBL:ELK13445.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13445.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}.
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DR EMBL; KB030625; ELK13445.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KQE8; -.
DR STRING; 9402.L5KQE8; -.
DR eggNOG; KOG1066; Eukaryota.
DR InParanoid; L5KQE8; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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; 2.
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:UP000010552};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..966
FT /note="Neutral alpha-glucosidase AB"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969443"
FT DOMAIN 89..346
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 409..736
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 744..832
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 849..907
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 210..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 108950 MW; F20A9D4166840909 CRC64;
MAAVPAVAAR RRRSRAGLVL ACLGVCLGIT LAVDRSNFKT CEESSFCRRQ RSIRPGLSPY
RALLDSLQLG PDALTVHLIN EVTKVLLVLE LQGLQKNMTR IRIDELEPRR PRYRVPDVLV
ADPPTARLSV SGRDDNSVEL TVAEGPYKII LTARPFRLDL LEDRSLLLSV NARGLLAFEH
QRAPRVSFSD KVSLTLGSIW DKIKNLFSRQ GSKDPAEGDG AQPEETPGDG DKAKETQGKA
EKDEPGAWEE TFKTHTDTKP YGPTSVGLDF SLPGMEHVYG IPEHADNLRL KVTEGGEPYR
LYNLDVFQYE LYNPMALYGS VPVLLGHSPH RDLGIFWLNA AETWVDISSN TAGKTLFGKM
LDYLQGSGET PQTDVRWMSE SGIIDVFLLL GPSVFDIFRQ YASLTGTQAL PPLFSLGYHQ
SRWNYRDEAD VLEVSQGFDD HNLPCDVIWL DIEHADGKRY FTWDSSRFPQ PLTMLEHLAS
KKRKLVAIVD PHIKVDSGYR IHEELQSLHL YVKTRDGFDY EGWCWPGAAS YPDFTNPTMR
AWWANMFSFD NYEGSAPNLY VWNDMNEPSV FNGPEVTMLK DAKHYGGWEH RDVHNIYGLY
VHMATAEGLV LRSGGVERPF VLSRAFFSGS QRYGAVWTGD NTAEWDHLKI SIPMCLSLGL
VGISFCGADV GGFFKNPAPE LLVRWYQMGA YQPFFRAHAH LDTGRREPWL LPSQYQDIIR
DALDQRYALL PFWYTLLYQA HREGIPVMRP LWVHYPQDVT TFSIDDQFLL GDALLVHPVS
DSGAHGVQVY LPGQGEVWYD VHSYQKHHGP QTLYLPVTLS SIPAFQRGGT IIPRWMRVRR
SSECMKEDPI TLFVALSPQG TAQGELYLDD GHTFNYQTRH EFLLRRFSFS GNTLVSSSAD
PKGHFETPVW IERVVIIGAG KPAAVVLQTK GSPESHLSFQ HDPETSVLIL RKPGVNVASD
WSIHLR
//
