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Database: UniProt
Entry: A7TJL8_VANPO
LinkDB: A7TJL8_VANPO
Original site: A7TJL8_VANPO 
ID   A7TJL8_VANPO            Unreviewed;       935 AA.
AC   A7TJL8;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   28-JAN-2026, entry version 82.
DE   RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN   ORFNames=Kpol_534p42 {ECO:0000313|EMBL:EDO17561.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO17561.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC       {ECO:0000256|ARBA:ARBA00004833}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; DS480402; EDO17561.1; -; Genomic_DNA.
DR   RefSeq; XP_001645419.1; XM_001645369.1.
DR   AlphaFoldDB; A7TJL8; -.
DR   FunCoup; A7TJL8; 992.
DR   STRING; 436907.A7TJL8; -.
DR   GeneID; 5545786; -.
DR   KEGG; vpo:Kpol_534p42; -.
DR   eggNOG; KOG1066; Eukaryota.
DR   HOGENOM; CLU_000631_7_0_1; -.
DR   InParanoid; A7TJL8; -.
DR   OMA; TVHQPLW; -.
DR   OrthoDB; 1334205at2759; -.
DR   PhylomeDB; A7TJL8; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR   GO; GO:0017177; C:glucosidase II complex; IEA:EnsemblFungi.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0106407; F:Glc2Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:EnsemblFungi.
DR   GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006491; P:N-glycan processing; IEA:EnsemblFungi.
DR   CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR   CDD; cd14752; GH31_N; 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; IPR048395; Glyco_hydro_31_C.
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:SF54; BCDNA.GH04962; 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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..935
FT                   /note="Glucosidase II subunit alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002715743"
FT   DOMAIN          97..330
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          373..697
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          706..797
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          822..857
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   935 AA;  107870 MW;  1DAD22428F6F8730 CRC64;
     MIFNNRFLII FLLPLYWATA FGFTEYLLKT CQQSGFCHRN KVYSQNILKT KNSYYSIDLS
     SINYEVEKSK SELNLFTANI IKTIPRPDVG DIKVVLPISI SFLKDTNSVR LTIDEDRHPE
     LDNSISEILN PYRYNETWKW AFDIDNKDIL QGDKLSFYEL KGSSNNVISL YNRDNSIKVE
     VYTNSFKIKV FYNDTLVFTV NDRLFMNLEH KRLKELNFQN INPEETPYNM FGDDFEYSKD
     DTLKFGPESV ALDFTFNNME NVYGIPEHAD SLKLKDTSNT EPYRLFNVDV FEYTIDSPMP
     MYGAIPFMIG TNKDTSAGIF WVNAADTWVD IAYEGSDTKT HWISETGIID VVLFLGKSPS
     DLTKNYIKLT GKPQLPLLSS IGYHQCRWNY NDEPDVLNVD SEMDKYQFPF DFIWLDLEYT
     DDKKYFTWKP NSFPNPKRLL NKLARLGRQL VVLIDPHLKL NYFVSDSVVE DQGCVYNSEG
     DPFIGHCWPG NSIWIDTLNP IGQKLWDGFF KKFIGSIKNL HIWNDMNEPS IFSGPETTAP
     KDLIHYAGFE ERSIHNIYGL SVHETTYDSL KEIKDGSGLR PFVLTRAFFA GSQRTAATWT
     GDNAANWDYL RISIPMCLTN NIVGMPFIGA DVAGFSGDPE PELLVRWYQA GIWYPFFRGH
     AHIDTKRREP YLLDEPDRSI VREAIQLRYA LLPMLYTSFF NAHRTGTPIM KPMFYDKTMY
     PELYAIDDQF YVGDSGLLVK PIVDKEATSV EMMFVPGIYY EYTNLSPLII NGIVPQSRNI
     DAPLDIIPMF IEGGHILTRR NKYRRSSKLM RHDPYTLVIA PDVYGNAFGD LYIDDGETFE
     FEKGEYLETN FSLNDGKVLK STVLNEPQFD NVLGNTDIYE IKIATAAIKK TVKKTVTIIS
     GSNKHEVPLH RSEDGNWVSI RYPKIKVDET WEITF
//
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