ALG6_CHICK
ID ALG6_CHICK Reviewed; 507 AA.
AC Q802T2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=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=RCJMB04_6f21;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oriol R., Martinez-Duncker R.I., Mollicone R., Chantret I., Codogno P.;
RT "A novel function for mannosyltransferases.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(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; AJ535824; CAD60191.1; -; mRNA.
DR EMBL; AJ719772; CAG31431.1; -; mRNA.
DR RefSeq; NP_989766.1; NM_204435.1.
DR AlphaFoldDB; Q802T2; -.
DR SMR; Q802T2; -.
DR STRING; 9031.ENSGALP00000017880; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q802T2; -.
DR GeneID; 395078; -.
DR KEGG; gga:395078; -.
DR CTD; 29929; -.
DR VEuPathDB; HostDB:geneid_395078; -.
DR eggNOG; KOG2575; Eukaryota.
DR InParanoid; Q802T2; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q802T2; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q802T2; -.
DR Proteomes; UP000000539; Unplaced.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
FT glucosyltransferase"
FT /id="PRO_0000284134"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 57437 MW; 66FD4727DEC9A99F CRC64;
MEKWSLMTIT VLLALTVRWT VSLGSYSGAG KPPMYGDYEA QRHWQEVTYN LPIRQWYFNT
SDNNLLYWGL DYPPLTAYHS FLCAYVAKLI NPDWIALHTS RGYESQSHKL FMRTTVFVAD
LLIYIPAVIL YCCSLKETST KKKVSSALCI LLYPGLILID HGHFQYNSVS LGFALWGVLC
LSYDWDLLGS AAFCLALNYK QMELYHSLPF FCYLLGKCFK KGLKGKGLLL LIKLAGTVVA
SFAVCWLPFC TDVEQIMQVL RRLFPIDRGL FEDKVANIWC SLSVLIKIKN VVSPQTQLKL
SFAVTFLSLL PTCIKLTVQP SLRGFKLTLV SCALSFFLFS FQVHEKSILL VSVPVCLIIN
EVPFMATWFL LVSTFSMLPL LLKDGLLLPY AVTTLAFLSA CVASFAIFEK TSAKDLQLKP
FSQSLRGYVS WFKLFPKIVR SLFLLSVTLM GVLSVMSAAV HPPQRFPDLF PVSVSSISCL
HFLFFLVYFN VIILWDSKNS RNQKKVS
