ALG10_NEUCR
ID ALG10_NEUCR Reviewed; 771 AA.
AC Q7SA35; V5INS8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase;
DE EC=2.4.1.256;
DE AltName: Full=Alpha-1,2-glucosyltransferase alg-10;
DE AltName: Full=Alpha-2-glucosyltransferase alg-10;
DE AltName: Full=Asparagine-linked glycosylation protein 10;
DE AltName: Full=Dolichyl-phosphoglucose-dependent glucosyltransferase alg-10;
GN Name=alg-10; ORFNames=NCU16845;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Adds the third 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(2)Man(9)GlcNAc(2)-PP-Dol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CM002239; ESA43000.1; -; Genomic_DNA.
DR RefSeq; XP_011394421.1; XM_011396119.1.
DR AlphaFoldDB; Q7SA35; -.
DR STRING; 367110.Q7SA35; -.
DR EnsemblFungi; ESA43000; ESA43000; NCU16845.
DR GeneID; 23569685; -.
DR KEGG; ncr:NCU16845; -.
DR VEuPathDB; FungiDB:NCU16845; -.
DR HOGENOM; CLU_017053_0_0_1; -.
DR InParanoid; Q7SA35; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..771
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_0000215459"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 392..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 86360 MW; 5A869287E42012D1 CRC64;
MMDALRVLLE TSTFNEVLRG LAISILLAKL TQSTTSSSKS QGSTFITASG FILIYFFARS
WLALVNHYAP EPYLDEVFHI PQAQTYCEGR YHEWDNKITT PPGLYLLSVG WHKLVRLVEC
TPSSLRSNNL VATLLIALIA LSCRRRIEAQ TAVGIEKSAV SFYAYHTAIN IALFPVIFFF
SGLYYTDVAS TLVMLVAYWN HLNRVASHSE KPGFLNGLWT VVLGVAALFM RQTNVFWVVV
YMGGLEAAHV VKGLKPKPVS KNDTPDFVLE NIRDSFGFWL RRYAVGDVHD PPVDMAWPDD
WALCLLSIGI AALCNPLRVL RQVWPHITIM GLFAGFVAWN GGVVLGDKSN HIATIHLPQM
LYIWPFFAFF SAPLLIPRVL STLADLITHA RTPTPSHTTT KDPGRSSWRF TKPSITSKKS
STTKPPQRSG PTPASSSSSS SSFSPDTNSS GRGFRFILDL VLSRKLYYPF YLLATILLSA
AIIHYNTIIH PFTLADNRHY MFYIFRYTIL RSSLVRLALV AAYTLSRWLI WKRLEGNNPP
LRDLAGETGL KITKNKLGWR DEFSASPFVT QDFYGPKTIK TDEQKNIKDK QKEVEEEEEE
EEKEDWLIGG AYTTLSLSST QPSPATSSPP TSTVLLWLLT TTLSLVTAPL VEPRYFILPW
VFYRLLVPAM PVSSSLVSSS SSSSFASSTT ESGNGDGNDA ATAARQQQNG NGKRGLLWNI
IRRTDAALAL ETVWFLAINI GTMYMFLFKP FYWKTASGEM LDGGRLQRFM W
