ID   ALG11_NEUCR             Reviewed;         556 AA.
AC   Q8X092; Q1K8Z1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE            EC=2.4.1.131;
DE   AltName: Full=Alpha-1,2-mannosyltransferase alg-11;
DE   AltName: Full=Asparagine-linked glycosylation protein 11;
DE   AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN   Name=alg-11; ORFNames=B14D6.360, NCU06779;
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=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
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: Required for N-linked oligosaccharide assembly. Has a role in
CC       the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC       oligosaccharide on the cytoplasmic face of the endoplasmic reticulum
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC         D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC         Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC         ChEBI:CHEBI:132515; EC=2.4.1.131;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AL356173; CAB91745.2; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34384.1; -; Genomic_DNA.
DR   RefSeq; XP_963620.1; XM_958527.3.
DR   AlphaFoldDB; Q8X092; -.
DR   SMR; Q8X092; -.
DR   STRING; 367110.Q8X092; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   GlyCosmos; Q8X092; 3 sites, No reported glycans.
DR   PaxDb; 5141-EFNCRP00000006879; -.
DR   EnsemblFungi; EAA34384; EAA34384; NCU06779.
DR   GeneID; 3879830; -.
DR   KEGG; ncr:NCU06779; -.
DR   VEuPathDB; FungiDB:NCU06779; -.
DR   HOGENOM; CLU_017896_1_1_1; -.
DR   InParanoid; Q8X092; -.
DR   OMA; ARLYGWV; -.
DR   OrthoDB; 197751at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
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   CDD; cd03806; GT4_ALG11-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR038013; ALG11.
DR   InterPro; IPR031814; ALG11_N.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR   Pfam; PF15924; ALG11_N; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..556
FT                   /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080277"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..556
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          64..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   556 AA;  62533 MW;  3D59DA2B140B287A CRC64;
     MANGLFTYVA ISLFTIGPLL ALFIPFVWRL VGSSLGWYLR RKTDGRRCHI LEVVEADERK
     YRDSKSAKGR KAEKEDRDTF NNTEATGTSD GKVYDKDWDG IVGFFHPFCN AGGGGERVLW
     AAIRATQKRW PKAKCVVYTG DHDVSKEAIL SRVEQRFNIH LHPPTVNFLY LSTRRWVLAS
     TWPYFTLAGQ SFGSLIMAWD AFSLLVPDIF VDTMGYAFAL GFSRFLFRDV PTAAYVHYPT
     ISTDMLESLD PASAVGSQGV NAGKGTGAKG RAKKIYWQLF ARLYSLMGAS VDVVMTNSTW
     TQAHIEKLWG PVRNLTGAVP GIKSKVNPIA VVYPPVAVEE LEQEVEVSPE SEKRRENVLL
     YIAQFRPEKN HQLIVQAFAE FLKSGSEAAR DAKLVLVGSV RDDYDSKRVY KLRLLVNELH
     IKDRVEFHLD ASWPDILEWL RRASVGVNGM WNEHFGIGVV EYQAAGLISV VHDSGGPKLD
     IVVEVDGEPT GFHATTSKEF AEGFEKALSL PNPYAVRLRA RKSAKRFTEE EFARRWIEQL
     EKCVAIKAVE KPKSRQ
//