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Database: UniProt/SWISS-PROT
Entry: ALG8_COCIM
LinkDB: ALG8_COCIM
Original site: ALG8_COCIM 
ID   ALG8_COCIM              Reviewed;         501 AA.
AC   Q1DJR8; J3K343;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE            EC=2.4.1.265;
DE   AltName: Full=Asparagine-linked glycosylation protein 8;
DE   AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase;
DE   AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN   Name=ALG8; ORFNames=CIMG_09445;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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 (By similarity).
CC       {ECO:0000250}.
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   -!- 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; GG704915; EAS28241.3; -; Genomic_DNA.
DR   RefSeq; XP_001239824.1; XM_001239823.2.
DR   AlphaFoldDB; Q1DJR8; -.
DR   SMR; Q1DJR8; -.
DR   STRING; 246410.Q1DJR8; -.
DR   GeneID; 4559127; -.
DR   KEGG; cim:CIMG_09445; -.
DR   VEuPathDB; FungiDB:CIMG_09445; -.
DR   InParanoid; Q1DJR8; -.
DR   OMA; YHSTDFD; -.
DR   OrthoDB; 5488939at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12413:SF2; DOLICHYL PYROPHOSPHATE GLC1MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE-RELATED; 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..501
FT                   /note="Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-
FT                   glucosyltransferase"
FT                   /id="PRO_0000278331"
FT   TOPO_DOM        1..3
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..142
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..220
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..252
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..319
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..364
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        411..412
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..446
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..476
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        477..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        498..501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  57019 MW;  B77A42190D384D83 CRC64;
     MAEFFPSLTQ CALVAAAFKV LLFPAYKSTD FEVHRNWLAI THSLPVQDWY YEKTSEWTLD
     YPPFFAGLEW LLSKVAFFVD PAMLQLGNLN YDSWQTIYFQ RSSVIFLELM LVYALNRYIK
     SVPAPSKHLA HAASLSILLS PGLLIIDHIH FQYNGFLYGI LILSIVLARK QSTLLYSGVT
     FAILLCLKHI YLYLSLAYFV YLLRAYCLDP NSVFRPRFGN IIKLGIGVTS VFAAAFGPFV
     YWGQLNQIKE RLFPFSRGLC HAYWAPNIWA MYSFVDRVLI PVAPRLGLPI KADALTSVTR
     GLVGDTSFAI LPEVKKEHTF ALTLFFQLLP LLKLWLQPNW DNFVGSITLC AYAAFLFGWH
     VHEKAILLII LPFSLLALKD LRYLGAFRPL AVAGHVSLFP LLFTAAEFPV KTVYTVLWLV
     LFLFTFERLA PVPARPRVFL LDRFSLLYDT VSIPLIVYCS LVHGWLFGGR MEFLPLMFTS
     SYAALGVVGS WVGFMVVYFT S
//
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