ID E9GMP9_DAPPU Unreviewed; 506 AA.
AC E9GMP9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Alpha-1,3-glucosyltransferase {ECO:0000256|RuleBase:RU363110};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363110};
GN ORFNames=DAPPUDRAFT_304939 {ECO:0000313|EMBL:EFX79136.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX79136.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX79136.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + 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-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
CC Evidence={ECO:0000256|ARBA:ARBA00034048};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU363110}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363110}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363110}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008715, ECO:0000256|RuleBase:RU363110}.
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DR EMBL; GL732553; EFX79136.1; -; Genomic_DNA.
DR AlphaFoldDB; E9GMP9; -.
DR STRING; 6669.E9GMP9; -.
DR EnsemblMetazoa; EFX79136; EFX79136; DAPPUDRAFT_304939.
DR KEGG; dpx:DAPPUDRAFT_304939; -.
DR eggNOG; KOG2576; Eukaryota.
DR HOGENOM; CLU_022045_2_0_1; -.
DR InParanoid; E9GMP9; -.
DR OMA; YLAPPFG; -.
DR PhylomeDB; E9GMP9; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR12413:SF2; DOLICHYL PYROPHOSPHATE GLC1MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE-RELATED; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU363110};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363110};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363110};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363110};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363110};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363110}.
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 171..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 216..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 337..354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 360..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 382..401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 407..424
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 444..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 474..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
SQ SEQUENCE 506 AA; 57708 MW; AC1AA137575E163E CRC64;
MLWRIFASIT FGKLLFIPSY RSTDFEVHRN WLAVTHSLPL NKWYVDDTSQ WTLDYPPLFA
WFEYLLSWVA CLFDPEMLKV ENLNYASQNT VLFQRISVIF TDVVYALGVQ KCLYSIGSTQ
GGNSPTILAF LLLCNVGLFI VDHIHFQYNG FLTGILLLSV GSILQKENLK AAFWFSVLLN
LKHIYLYIAP VYFVYLFRSY CIEIQKSRLT FHFKRLIKLG MVVVTTFGVA YGPFVGQFQQ
VMSRLFPFEN RGLCHAYWAP NFWAIYNIVD KILAVSARLF GWTTVSTTTA SMTGGLVQEF
EHAILPSVGP KTTLICTLLA LIPAIVILLR QPNQPRVFVR AIVLCAFASF LFGWHVHEKA
ILIVITPLTL LAVSSHEDCR LFLLLSITGH VSLFPLLFTP FENVSKIFLV LTYSLASYSF
LSALHYDPKS KSTLVKFRSW ERLFLYGLVA VALFESFIHS MVDPSGKLPF LPLLIMSVYC
AVGVIYVWLL FVIASLKTEK KISKQK
//
