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ALG6_DICDI
ID   ALG6_DICDI              Reviewed;         518 AA.
AC   Q54QG6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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 homolog;
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=DDB_G0283841;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000057; EAL65535.1; -; Genomic_DNA.
DR   RefSeq; XP_638905.1; XM_633813.1.
DR   AlphaFoldDB; Q54QG6; -.
DR   SMR; Q54QG6; -.
DR   STRING; 44689.DDB0231451; -.
DR   PaxDb; Q54QG6; -.
DR   EnsemblProtists; EAL65535; EAL65535; DDB_G0283841.
DR   GeneID; 8624302; -.
DR   KEGG; ddi:DDB_G0283841; -.
DR   dictyBase; DDB_G0283841; alg6.
DR   eggNOG; KOG2575; Eukaryota.
DR   HOGENOM; CLU_008110_3_0_1; -.
DR   InParanoid; Q54QG6; -.
DR   OMA; RQWYFNT; -.
DR   PhylomeDB; Q54QG6; -.
DR   Reactome; R-DDI-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q54QG6; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
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; 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..518
FT                   /note="Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-
FT                   1,3-glucosyltransferase"
FT                   /id="PRO_0000327819"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   518 AA;  60799 MW;  5A36BD8D62E83251 CRC64;
     MKSLNNKVGF SSLNISIVLL ILMISLLARY LVSLNGYSGQ SKPPMFGDYE AQRHWMEITT
     NLDIHQWYFN STDNDLMYWG LDYPPLTAYL SWVFGKIGEF IEPKSMELFT SRGYETDSGK
     LFMRMTVIVS DLFIWLPSVW FFVKTFYKQR NISQQISAFL FISLQPGLLL IDHGHFQYNG
     VSLGLGLFAI TFIIRDQQLL ASFFFVLSLN YKQMCLYYSP AFFFYLLLSN FEFTLKFSKI
     FSSIFKILKI GIVVIFTFIL CWIPFLSIEQ ASQVLFRLFP FARGLYEDKV ANFWCFISII
     INVKNLFTTD QLIKICLILT LVTMLPLVYG IKRIPKNKFV FIHSLINSSF SFFLFSFQVH
     EKTILLVSLP ISLLILHHPN MVWWFILIST FSMFPLLFKD GLVIPYFAIM ILYIVIGYQF
     KNSITRSNNQ FKHQNSQENL LASSDKSFYS IYLNYWFYLN IIGMVVCHLL YQFAPHPPHL
     PSLWLLLVCN FSFIHFILTF FYFIKEMTTF SPIKIKSN
 
 
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