ID M7ZPD4_TRIUA Unreviewed; 1401 AA.
AC M7ZPD4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000256|ARBA:ARBA00038888, ECO:0000256|RuleBase:RU368089};
DE EC=3.2.1.106 {ECO:0000256|ARBA:ARBA00038888, ECO:0000256|RuleBase:RU368089};
GN ORFNames=TRIUR3_33564 {ECO:0000313|EMBL:EMS61972.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS61972.1};
RN [1] {ECO:0000313|EMBL:EMS61972.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from the
CC Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
CC {ECO:0000256|RuleBase:RU368089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC ChEBI:CHEBI:132537; EC=3.2.1.106;
CC Evidence={ECO:0000256|RuleBase:RU368089};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648,
CC ECO:0000256|RuleBase:RU368089}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family.
CC {ECO:0000256|ARBA:ARBA00010833, ECO:0000256|RuleBase:RU368089}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000256|ARBA:ARBA00010271}.
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DR EMBL; KD088513; EMS61972.1; -; Genomic_DNA.
DR STRING; 4572.M7ZPD4; -.
DR eggNOG; KOG1021; Eukaryota.
DR eggNOG; KOG2161; Eukaryota.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.110; Glycosyl hydrolase family 63, N-terminal domain; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR031335; Glyco_hydro_63_C.
DR InterPro; IPR031631; Glyco_hydro_63N.
DR InterPro; IPR038518; Glyco_hydro_63N_sf.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR PANTHER; PTHR10412:SF11; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR Pfam; PF16923; Glyco_hydro_63N; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368089};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU368089};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368089};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 26..197
FT /note="Glycosyl hydrolase family 63 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16923"
FT DOMAIN 269..796
FT /note="Glycosyl hydrolase family 63 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03200"
FT DOMAIN 1003..1337
FT /note="Exostosin GT47"
FT /evidence="ECO:0000259|Pfam:PF03016"
SQ SEQUENCE 1401 AA; 159621 MW; 7F6B84B44430D002 CRC64;
MARSVTPLDA PRMMDLPQFQ GDHKESLYWG TYRPNVYLGI RARTPLSLIA GLMWIGVKNG
QYFIRHVCQD SDELSKYGWA DHNGRDYGRQ ELTDHGLHLT TSFLKEKGDG SGYGGDWAVR
LDAKNEGSSL SEAQESTTHL FFYIADEAGK LITMGSHEPP SRGPVLLASG SHEEIGDWEL
YLRSEDNLEI HRAGFQTISM HNLSDLVQHA LVTNARQSGN LNLPDMTEDS SNAMIYQVSI
KLPAKIDMVF LSGAGSKNPM TAERVNRLTG PMLSTRLESK QKDFEERYDQ IFNVNNKIVS
KELSVGRAAL SSLLGGIGYF YGQSKIALPK GFSQKNGDKY IPYWPAALYT AVPSRSFFPR
GFLWDEGFHQ LVIWRWDAHI SMDIIGHWLD LINADGWIPR EQILGAEALS KVPEEFVLQY
PSNGNPPTLF LALRDLASAI HAHQFSDEEA EKISTFLKRA YVRLNSWFQW FNSTQSGKYE
GTFFWHGRDN MTTRELNPKT LTSGLDDYPR ASHPNDEERH VDLRCWMLLA TNCMRSIAGF
LKMDSSLEKD YYKLSDQLSD FETLNKMHLD DKTGAYFDFG NHTEKVRLRW YENREAMKRE
LLRETLEAPH LQLVPHVGYV SLFPFMMGAI PPESWVLEKQ LDLISNSSVL WTDYGLRSLS
RTSSMYMKRN TEHDAPYWRG AIWINMNYMI LSGLHHYAHG KLLEQCCEMY QYLPFTNFTV
CITLLTLRCP VEDGPYSVRA GELYDELRSN LIRNIVGNYQ ETGFFWENYD QKNKGKGKGA
RSFTGWTSLV VLIMAESYPS LHRLILLIYV SLHRRRILLW CAARFYGALA QRLLDCLPQQ
GLFDSGEPTC LRLTHIKKNL VSIKQQPTKK KNYSKPRGAK LVRRSRWRAV AQWEFDSALL
NPARQAGRGV YHFMGTNPKS KVRLTRGINR RSALLPGPVP PPHPKSTGDA GGRPPRGAAV
FGLLLLAFAL SSTVIYLASP ARAASPSSIL LNLRPFAARC PPTPPLRVFM YDLPPRFHVA
MMASSRNGGG GAEGNSTAFP AWPPSAGGIR RQHSVEYWMM ASLQQQRQQG GAAAEAVRVR
DPDAAEAFFV PFFSSLSFNV HGRNMTDPDT EADRLLQYVF VWFDLVRNSR LDMVELMDIL
WKSKYWQRSA GRDHVIPMHH PNAFRFLRDM VNASVLIVSD FGRYTKELAS LRKDVVAPYV
HVVDSFLNDD ASDPFEARPT LLFFRGRTVR KDEGKIRGKL AKLLKGKDGV RFENSLATGD
GIKISTDGMR SSKFCLHPAG DTPSSCRLFD AIVSHCIPVI ISSRIELPFE DEIDYSEFSL
FFSVEEALEP DYLLNQLRQM PKEKWVEMWS KLKNVSSHYE FQYPPRKDDA VNMIWRQVRN
KIPAVNLAIH RSRRLKVPDW W
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