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-APR-2013, entry version 57.
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 Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oriol R., Martinez-Duncker R.I., Mollicone R., Chantret I.,
RA 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.,
RA Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA Plachy J., Carninci P., 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
CC glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the
CC lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Dolichyl beta-D-glucosyl phosphate + D-Man-
CC alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-
CC (1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-
CC D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-
CC GlcNAc-diphosphodolichol = D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-
CC D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-
CC alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-
CC (1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-
CC diphosphodolichol + dolichyl phosphate.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (Potential).
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
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DR EMBL; AJ535824; CAD60191.1; -; mRNA.
DR EMBL; AJ719772; CAG31431.1; -; mRNA.
DR IPI; IPI00822734; -.
DR RefSeq; NP_989766.1; NM_204435.1.
DR UniGene; Gga.5118; -.
DR STRING; 9031.ENSGALP00000017880; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q802T2; -.
DR GeneID; 395078; -.
DR KEGG; gga:395078; -.
DR CTD; 29929; -.
DR eggNOG; NOG287760; -.
DR HOGENOM; HOG000195048; -.
DR HOVERGEN; HBG024331; -.
DR KO; K03848; -.
DR UniPathway; UPA00378; -.
DR NextBio; 20815171; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Endoplasmic reticulum; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 507 Dolichyl pyrophosphate Man9GlcNAc2 alpha-
FT 1,3-glucosyltransferase.
FT /FTId=PRO_0000284134.
FT TRANSMEM 4 24 Helical; (Potential).
FT TRANSMEM 115 135 Helical; (Potential).
FT TRANSMEM 144 164 Helical; (Potential).
FT TRANSMEM 173 193 Helical; (Potential).
FT TRANSMEM 227 247 Helical; (Potential).
FT TRANSMEM 298 318 Helical; (Potential).
FT TRANSMEM 324 344 Helical; (Potential).
FT TRANSMEM 362 382 Helical; (Potential).
FT TRANSMEM 388 408 Helical; (Potential).
FT TRANSMEM 438 458 Helical; (Potential).
FT TRANSMEM 473 493 Helical; (Potential).
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
//
