ALG8_BOVIN
ID ALG8_BOVIN Reviewed; 526 AA.
AC Q0P5D9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase {ECO:0000250|UniProtKB:P40351};
DE EC=2.4.1.265 {ECO:0000250|UniProtKB:P40351};
DE AltName: Full=Asparagine-linked glycosylation protein 8 homolog;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase {ECO:0000250|UniProtKB:P40351};
DE AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase {ECO:0000250|UniProtKB:P40351};
GN Name=ALG8 {ECO:0000250|UniProtKB:P40351};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 before it is transferred
CC to the nascent peptide (By similarity). Required for PKD1/Polycystin-1
CC maturation and localization to the plasma membrane of the primary cilia
CC (By similarity). {ECO:0000250|UniProtKB:P40351,
CC ECO:0000250|UniProtKB:Q6P8H8}.
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:0000250|UniProtKB:P40351};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC120179; AAI20180.1; -; mRNA.
DR RefSeq; NP_001069593.1; NM_001076125.2.
DR AlphaFoldDB; Q0P5D9; -.
DR SMR; Q0P5D9; -.
DR STRING; 9913.ENSBTAP00000049035; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q0P5D9; -.
DR GeneID; 538731; -.
DR KEGG; bta:538731; -.
DR CTD; 79053; -.
DR eggNOG; KOG2576; Eukaryota.
DR InParanoid; Q0P5D9; -.
DR OrthoDB; 595382at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR InterPro; IPR039487; ALG8.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 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..526
FT /note="Probable dolichyl pyrophosphate Glc1Man9GlcNAc2
FT alpha-1,3-glucosyltransferase"
FT /id="PRO_0000281997"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 526 AA; 59964 MW; 75C49BD44E1A5F92 CRC64;
MAAFGIATGG SNWFSALALG VTLLKCLLIP TYHSTDFEVH RNWLAITHSL PISQWYYEAT
SEWTLDYPPF FAWFEYALSH VAKYFDQEML NVRNLNYSSS RTLLFQRFSV IFTDALFVYA
VHECCKCIDG KKAGKELTEK PKFILSALLL WNFGLLIVDH IHFQYNGFLS GLMLLSIARF
FQKRHMEGAF LFAVLLHFKH IYLYVAPAYG VYLLRSYCFT ANKQDGSIRW NSFSFVRLIS
LGLIVFLVSA LSLGPFLALN QLPQVFSRLF PFKRGLCHAY WAPNFWALYS AFDKVLSVIG
LELKLLDPNK IPKASMTSGL VQQFQHTVLP SVTPLATFIC TLIAMLPSVF CLWCKPQGPR
GFLRCLILCA LSSFMFGWHV HEKAILLAVL PMSLLSVGKA VDASIFLILT TTGHYSPFPL
LFTAPELPIK IILMLLFTIY SISSLKTLFR KEKPLFNWME TFYLLGLGPL EVFCEFVFPF
TSWNLKYPFI PLLLTSVYCA VGITYAWLKL YVSVLIDPPV GKTKKQ
