ID   ALG1_ARTBC              Reviewed;         447 AA.
AC   D4AZD1;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000250|UniProtKB:Q9BT22};
DE            EC=2.4.1.142 {ECO:0000250|UniProtKB:Q9BT22};
GN   ORFNames=ARB_01551;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC       oligosaccharide for N-glycosylation. Involved in assembling the
CC       dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC       surface of the ER. {ECO:0000250|UniProtKB:Q9BT22}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC         diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC         Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472; EC=2.4.1.142;
CC         Evidence={ECO:0000250|UniProtKB:Q9BT22};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9BT22}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 33 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABSU01000020; EFE31651.1; -; Genomic_DNA.
DR   RefSeq; XP_003012291.1; XM_003012245.1.
DR   AlphaFoldDB; D4AZD1; -.
DR   SMR; D4AZD1; -.
DR   STRING; 663331.D4AZD1; -.
DR   EnsemblFungi; EFE31651; EFE31651; ARB_01551.
DR   GeneID; 9519940; -.
DR   KEGG; abe:ARB_01551; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_1_0_1; -.
DR   OMA; CWLCARI; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
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:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR026051; ALG1-like.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR13036; PTHR13036; 1.
DR   Pfam; PF13579; Glyco_trans_4_4; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434499"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..447
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   447 AA;  49105 MW;  025959A1791CBAEE CRC64;
     MTLVLLLSIF AICFSSVAFI QLLPTRREKK SSEAHDAVSV QIDTIVCLLR PPRSSSNSPT
     LNRVADSTPN QELLDHPLIS IVALPSPPAL LQTKKKFLFP VAAILKVLQQ AWHLWAALGY
     RTGPAHWILV QNPPAAPTLA LALLACHLRH SRLIIDWHNF GYSILALKLG SGHPMVKLME
     WYEKAFSCYA TAHFCVSNAM ARILREQFEI KKPLMVLHDR PSSAFSPIFD EKQRLAILSS
     IPETSQSAID IIEGRCRLLV SSTSWTPDED FSLLLDALCR YSTSAKSSGL PSVPLLVIIT
     GKGPLKDMYL SQIDKLKAEG KLFNVFIKTA WLSFEDYAQL LACATLGVCL HTSSSGVDLP
     MKVVDMFGAG LPVVGWDQYE AWPELVTEGV TGLGFDSADR LSGLLKSVLG GDGSALKVLR
     EGAVKESRNR WDQTWDPIAG TFLGLVT