ID   ALG1_PONAB              Reviewed;         464 AA.
AC   Q5R7A2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000250|UniProtKB:Q9BT22};
DE            EC=2.4.1.142 {ECO:0000250|UniProtKB:Q9BT22};
DE   AltName: Full=Asparagine-linked glycosylation protein 1 homolog;
DE   AltName: Full=Beta-1,4-mannosyltransferase;
DE   AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE   AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN   Name=ALG1 {ECO:0000250|UniProtKB:Q9BT22};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of the first of nine mannose moieties
CC       to form a dolichol-lipid linked oligosaccharide intermediate required
CC       for proper N-linked glycosylation. {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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13866;
CC         Evidence={ECO:0000250|UniProtKB:Q9BT22};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9BT22}.
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 33 subfamily. {ECO:0000305}.
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DR   EMBL; CR860216; CAH92358.1; -; mRNA.
DR   RefSeq; NP_001126389.1; NM_001132917.2.
DR   AlphaFoldDB; Q5R7A2; -.
DR   STRING; 9601.ENSPPYP00000008002; -.
DR   CAZy; GT33; Glycosyltransferase Family 33.
DR   GeneID; 100173370; -.
DR   CTD; 56052; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_0_0_1; -.
DR   InParanoid; Q5R7A2; -.
DR   OMA; PLKVLWQ; -.
DR   OrthoDB; 816895at2759; -.
DR   TreeFam; TF314121; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Chromosome 16.
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; ISS:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR026051; ALG1-like.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR13036; PTHR13036; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Phosphoprotein;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..464
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080251"
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..464
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          242..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BT22"
SQ   SEQUENCE   464 AA;  52505 MW;  12CCBEC1ACA1BCA5 CRC64;
     MAASCLVLLA LCLLLPLLLL GGWKRWRRGR TARHVVAVVL GDVGRSPRMQ YHALSLAMHG
     FSVTLLGFCN SKPHDELLQN NRIQIVGLTE LQSLAVGPRV FQYGVKVVFQ AMYLLWKLMW
     REPGAYIFLQ NPPGLPSIAV CWFVGCLCGS KLVIDWHNYG YSIMGLVHGP NHPLVLLAKW
     YERFFGRLSH LNLCVTNAMR EDLAENWHIR AVTVYDKPAS FFKETPLDLQ HRLFMKLGGT
     HSPFRARSEP EDPATERSAF TERDAGSGLV TRLHERPALL VSSTSWTEDE DFSILLAALE
     KFEQLTLDGH SLPSLVCVIT GKGPLREYYS HLIHQKHFQH IQVCTPWLEA EDYPLLLGSA
     DLGVCLHTSS SGLDLPMKVV DMFGCHLPVC AVNFKCLHEL VKHEENGLVF EDSEELAAQL
     QMLFSNFPDP AGKLNQFRKN LRESQQLRWD ESWVQTVLPL VMDT