ID D8PR27_SCHCM Unreviewed; 533 AA.
AC D8PR27;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Alpha-1,3-glucosyltransferase {ECO:0000256|RuleBase:RU363110};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363110};
GN ORFNames=SCHCODRAFT_63365 {ECO:0000313|EMBL:EFJ03119.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ03119.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- FUNCTION: Adds the second glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol.
CC {ECO:0000256|ARBA:ARBA00025507}.
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; GL377302; EFJ03119.1; -; Genomic_DNA.
DR RefSeq; XP_003038021.1; XM_003037975.1.
DR AlphaFoldDB; D8PR27; -.
DR STRING; 578458.D8PR27; -.
DR GeneID; 9586107; -.
DR KEGG; scm:SCHCO_02622631; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02622631; -.
DR eggNOG; KOG2576; Eukaryota.
DR HOGENOM; CLU_022045_1_1_1; -.
DR InParanoid; D8PR27; -.
DR OMA; YHSTDFD; -.
DR OrthoDB; 5488939at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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:UP000007431};
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 165..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 332..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 358..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 463..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 493..519
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
SQ SEQUENCE 533 AA; 60664 MW; 99F101298A1FEA1C CRC64;
MPAESTAVEA PKASRRWALP EFNASDWDIL VLSTTFKLLL FPTYRSTDFE VHRNWLAITH
SLPISQWYYD TTSEWTLDYP PFFAYFEKVL SIPASFIDPR IVDVNNLEYG AWSVIAYQRT
TVILTELVLG AACLRLIRNS VDPATQRIIA ASLFLHPGFI IVDHIHFQYN GFMFGILLWS
IIMAREGKRL ASGILFAILL NFKHIYMYLA PAYFVYLLRS FCLSPTGRLQ IKNFLSLANA
VIAVFVTSLG PFMLMGQIPQ LLSRLFPFKR GLNHAYWAPN VWALVTALDR VLLRYVQRTG
AEVTINDSGV ASSSRGLVGD TVFAVLPNVQ PIHTFIITIA FQIAFLVKLW FRPTYKSFLT
ALTLCGYTSF LFGWHVHEKA VLLVLVPLSL LAAERQAYFR TFLIASVAGI FSLFPLLFTP
TESVIEVVYS IAWLALVYLP LSRRVYEFPK SIFYVILDTL EKMYLAGFIP LQLFVTLYPV
WLSRRESSGG MEFLPLMLTS VYCAVGLVHA FVRLAYVYVN EERAYQGPLN EVQ
//
