ALG6_SCHPO
ID ALG6_SCHPO Reviewed; 506 AA.
AC O43053; Q9UUC4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267;
DE AltName: Full=Asparagine-linked glycosylation protein 6;
DE AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=alg6; ORFNames=SPBC342.01c, SPBC3F6.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Adds the first 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 Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA17695.1; -; Genomic_DNA.
DR PIR; T40396; T40396.
DR RefSeq; NP_596744.1; NM_001023764.2.
DR AlphaFoldDB; O43053; -.
DR SMR; O43053; -.
DR BioGRID; 277509; 53.
DR STRING; 4896.SPBC342.01c.1; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; O43053; -.
DR EnsemblFungi; SPBC342.01c.1; SPBC342.01c.1:pep; SPBC342.01c.
DR GeneID; 2540993; -.
DR KEGG; spo:SPBC342.01c; -.
DR PomBase; SPBC342.01c; alg6.
DR VEuPathDB; FungiDB:SPBC342.01c; -.
DR eggNOG; KOG2575; Eukaryota.
DR HOGENOM; CLU_008110_2_1_1; -.
DR InParanoid; O43053; -.
DR OMA; RQWYFNT; -.
DR PhylomeDB; O43053; -.
DR Reactome; R-SPO-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR PRO; PR:O43053; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IMP:PomBase.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:PomBase.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IMP:PomBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; EXP:PomBase.
DR InterPro; IPR039488; ALG6.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF1; PTHR12413:SF1; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-
FT 1,3-glucosyltransferase"
FT /id="PRO_0000174160"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 506 AA; 59203 MW; 0CD8ACC78BF49D6B CRC64;
MLSEFENGAP VQQFVSRFRS YSSKFLFFPC LIMSLVFMQW LISIGPYSGY NTPPMYGDFE
AQRHWMELTL HTPVSQWYFR DLQWWGLDYP PLTAYVSWFF GIIGHYFFNP EWFADVTSRG
FESLELKLFM RSTVIASHLL ILVPPLMFYS KWWSRRIPNF VDRNASLIMV LFQPALLLID
HGHFQYNCVM LGLVMYAIAN LLKNQYVAAT FFFCLALTFK QMALYFAPPI FFYLLGTCVK
PKIRFSRFIL LSVTVVFTFS LILFPWIYMD YKTLLPQILH RVFPFARGLW EDKVANFWCT
LNTVFKIREV FTLHQLQVIS LIFTLISILP SCVILFLYPR KRLLALGFAS ASWGFFLFSF
QVHEKSVLLP LLPTSILLCH GNITTKPWIA LANNLAVFSL WPLLKKDGLG LQYFTLVLMW
NWIGDMVVFS KNVLFRFIQL SFYVGMIVIL GIDLFIPPPS RYPDLWVILN VTLSFAGFFT
IYLWTLGRLL HISSKLSTDL RNKKEA
