ALG1_HUMAN
ID ALG1_HUMAN Reviewed; 464 AA.
AC Q9BT22; B4DP08; Q6UVZ9; Q8N5Y4; Q9P2Y2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.142 {ECO:0000269|PubMed:14973778};
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;
DE AltName: Full=Mannosyltransferase-1;
DE Short=MT-1;
DE Short=hMat-1;
GN Name=ALG1 {ECO:0000312|HGNC:HGNC:18294}; Synonyms=HMAT1, HMT1;
GN ORFNames=PSEC0061, UNQ861/PRO1870;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Fetal brain;
RX PubMed=10704531; DOI=10.1093/glycob/10.3.321;
RA Takahashi T., Honda R., Nishikawa Y.;
RT "Cloning of the human cDNA which can complement the defect of the yeast
RT mannosyltransferase I-deficient mutant alg 1.";
RL Glycobiology 10:321-327(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-267;
RP MET-325 AND ARG-455.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-464 (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP VARIANT CDG1K LEU-258, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=14973778; DOI=10.1086/382492;
RA Schwarz M., Thiel C., Luebbehusen J., Dorland B., de Koning T.,
RA von Figura K., Lehle L., Koerner C.;
RT "Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes
RT congenital disorder of glycosylation type Ik.";
RL Am. J. Hum. Genet. 74:472-481(2004).
RN [11]
RP VARIANTS CDG1K LEU-258 AND PRO-342.
RX PubMed=14973782; DOI=10.1086/382493;
RA Kranz C., Denecke J., Lehle L., Sohlbach K., Jeske S., Meinhardt F.,
RA Rossi R., Gudowius S., Marquardt T.;
RT "Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of
RT mannosyltransferase I.";
RL Am. J. Hum. Genet. 74:545-551(2004).
RN [12]
RP VARIANTS CDG1K ARG-150 AND LEU-258, AND VARIANT GLU-429.
RX PubMed=14709599; DOI=10.1093/hmg/ddh050;
RA Grubenmann C.E., Frank C.G., Huelsmeier A.J., Schollen E., Matthijs G.,
RA Mayatepek E., Berger E.G., Aebi M., Hennet T.;
RT "Deficiency of the first mannosylation step in the N-glycosylation pathway
RT causes congenital disorder of glycosylation type Ik.";
RL Hum. Mol. Genet. 13:535-542(2004).
RN [13]
RP INVOLVEMENT IN CDG1K, FUNCTION, VARIANTS CDG1K ARG-50; PHE-71; LEU-74;
RP VAL-88; LEU-98; PHE-114; ARG-150; SER-209; LEU-258; TRP-276; PHE-281;
RP GLY-289; VAL-291; ASP-353; ARG-358; LEU-359; VAL-360; ALA-363; GLN-366;
RP GLN-367; LYS-382; ARG-384; SER-388 AND TRP-438, CHARACTERIZATION OF
RP VARIANTS CDG1K ARG-50; PHE-71; LEU-74; VAL-88; LEU-98; PHE-114; ARG-150;
RP SER-209; LEU-258; TRP-276; PHE-281; GLY-289; VAL-291; ASP-353; ARG-358;
RP LEU-359; VAL-360; ALA-363; GLN-366; GLN-367; LYS-382; ARG-384; SER-388 AND
RP TRP-438, AND CHARACTERIZATION OF VARIANT ASN-267.
RX PubMed=26931382; DOI=10.1002/humu.22983;
RG University of Washington Center for Mendelian Genomics;
RA Ng B.G., Shiryaev S.A., Rymen D., Eklund E.A., Raymond K., Kircher M.,
RA Abdenur J.E., Alehan F., Midro A.T., Bamshad M.J., Barone R., Berry G.T.,
RA Brumbaugh J.E., Buckingham K.J., Clarkson K., Cole F.S., O'Connor S.,
RA Cooper G.M., Van Coster R., Demmer L.A., Diogo L., Fay A.J., Ficicioglu C.,
RA Fiumara A., Gahl W.A., Ganetzky R., Goel H., Harshman L.A., He M.,
RA Jaeken J., James P.M., Katz D., Keldermans L., Kibaek M., Kornberg A.J.,
RA Lachlan K., Lam C., Yaplito-Lee J., Nickerson D.A., Peters H.L., Race V.,
RA Regal L., Rush J.S., Rutledge S.L., Shendure J., Souche E., Sparks S.E.,
RA Trapane P., Sanchez-Valle A., Vilain E., Voello A., Waechter C.J.,
RA Wang R.Y., Wolfe L.A., Wong D.A., Wood T., Yang A.C., Matthijs G.,
RA Freeze H.H.;
RT "ALG1-CDG: Clinical and Molecular Characterization of 39 Unreported
RT Patients.";
RL Hum. Mutat. 37:653-660(2016).
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:0000269|PubMed:10704531,
CC ECO:0000269|PubMed:14973778, ECO:0000269|PubMed:26931382}.
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:0000269|PubMed:14973778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13866;
CC Evidence={ECO:0000305|PubMed:14973778};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:14973778}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT22-2; Sequence=VSP_056931;
CC -!- DISEASE: Congenital disorder of glycosylation 1K (CDG1K) [MIM:608540]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. {ECO:0000269|PubMed:14709599,
CC ECO:0000269|PubMed:14973778, ECO:0000269|PubMed:14973782,
CC ECO:0000269|PubMed:26931382}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 33 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89432.1; Type=Erroneous initiation; Evidence={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; AB019038; BAA90748.1; -; mRNA.
DR EMBL; AK298144; BAG60420.1; -; mRNA.
DR EMBL; AK075373; BAC11576.1; -; mRNA.
DR EMBL; AC026458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004402; AAH04402.1; -; mRNA.
DR EMBL; BC031095; AAH31095.1; -; mRNA.
DR EMBL; AY359073; AAQ89432.1; ALT_INIT; mRNA.
DR CCDS; CCDS10528.1; -. [Q9BT22-1]
DR CCDS; CCDS81946.1; -. [Q9BT22-2]
DR RefSeq; NP_001317433.1; NM_001330504.1. [Q9BT22-2]
DR RefSeq; NP_061982.3; NM_019109.4. [Q9BT22-1]
DR RefSeq; XP_016878947.1; XM_017023458.1. [Q9BT22-2]
DR AlphaFoldDB; Q9BT22; -.
DR BioGRID; 121033; 43.
DR IntAct; Q9BT22; 14.
DR MINT; Q9BT22; -.
DR STRING; 9606.ENSP00000262374; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR GlyGen; Q9BT22; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BT22; -.
DR PhosphoSitePlus; Q9BT22; -.
DR SwissPalm; Q9BT22; -.
DR BioMuta; ALG1; -.
DR DMDM; 73921663; -.
DR EPD; Q9BT22; -.
DR jPOST; Q9BT22; -.
DR MassIVE; Q9BT22; -.
DR MaxQB; Q9BT22; -.
DR PaxDb; Q9BT22; -.
DR PeptideAtlas; Q9BT22; -.
DR PRIDE; Q9BT22; -.
DR ProteomicsDB; 4740; -.
DR ProteomicsDB; 78943; -. [Q9BT22-1]
DR Antibodypedia; 24484; 140 antibodies from 26 providers.
DR DNASU; 56052; -.
DR Ensembl; ENST00000262374.10; ENSP00000262374.5; ENSG00000033011.14. [Q9BT22-1]
DR Ensembl; ENST00000544428.1; ENSP00000440019.1; ENSG00000033011.14. [Q9BT22-2]
DR Ensembl; ENST00000588623.5; ENSP00000468118.1; ENSG00000033011.14. [Q9BT22-2]
DR Ensembl; ENST00000683739.1; ENSP00000507002.1; ENSG00000033011.14. [Q9BT22-2]
DR GeneID; 56052; -.
DR KEGG; hsa:56052; -.
DR MANE-Select; ENST00000262374.10; ENSP00000262374.5; NM_019109.5; NP_061982.3.
DR UCSC; uc002cyj.4; human. [Q9BT22-1]
DR CTD; 56052; -.
DR DisGeNET; 56052; -.
DR GeneCards; ALG1; -.
DR HGNC; HGNC:18294; ALG1.
DR HPA; ENSG00000033011; Low tissue specificity.
DR MalaCards; ALG1; -.
DR MIM; 605907; gene.
DR MIM; 608540; phenotype.
DR neXtProt; NX_Q9BT22; -.
DR OpenTargets; ENSG00000033011; -.
DR Orphanet; 79327; ALG1-CDG.
DR PharmGKB; PA134979319; -.
DR VEuPathDB; HostDB:ENSG00000033011; -.
DR eggNOG; KOG2941; Eukaryota.
DR GeneTree; ENSGT00390000008647; -.
DR HOGENOM; CLU_012079_0_0_1; -.
DR InParanoid; Q9BT22; -.
DR OMA; PLKVLWQ; -.
DR OrthoDB; 816895at2759; -.
DR PhylomeDB; Q9BT22; -.
DR TreeFam; TF314121; -.
DR BRENDA; 2.4.1.142; 2681.
DR PathwayCommons; Q9BT22; -.
DR Reactome; R-HSA-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR Reactome; R-HSA-4549380; Defective ALG1 causes CDG-1k.
DR SignaLink; Q9BT22; -.
DR SIGNOR; Q9BT22; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 56052; 695 hits in 1091 CRISPR screens.
DR ChiTaRS; ALG1; human.
DR GeneWiki; ALG1; -.
DR GenomeRNAi; 56052; -.
DR Pharos; Q9BT22; Tbio.
DR PRO; PR:Q9BT22; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BT22; protein.
DR Bgee; ENSG00000033011; Expressed in stromal cell of endometrium and 118 other tissues.
DR ExpressionAtlas; Q9BT22; baseline and differential.
DR Genevisible; Q9BT22; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /id="PRO_0000080249"
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 243..262
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:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056931"
FT VARIANT 50
FT /note="Q -> R (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs794726944)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077187"
FT VARIANT 71
FT /note="S -> F (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs200605408)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077188"
FT VARIANT 74
FT /note="H -> L (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs201337379)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077189"
FT VARIANT 88
FT /note="L -> V (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs794727301)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077190"
FT VARIANT 98
FT /note="P -> L (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596252105)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077191"
FT VARIANT 114
FT /note="L -> F (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596252196)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077192"
FT VARIANT 150
FT /note="S -> R (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs121908340)"
FT /evidence="ECO:0000269|PubMed:14709599,
FT ECO:0000269|PubMed:26931382"
FT /id="VAR_023364"
FT VARIANT 209
FT /note="I -> S (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596256204)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077193"
FT VARIANT 258
FT /note="S -> L (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs28939378)"
FT /evidence="ECO:0000269|PubMed:14709599,
FT ECO:0000269|PubMed:14973778, ECO:0000269|PubMed:14973782,
FT ECO:0000269|PubMed:26931382"
FT /id="VAR_023365"
FT VARIANT 267
FT /note="S -> N (no effect on function in protein
FT glycosylation; dbSNP:rs17849848)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:26931382"
FT /id="VAR_038425"
FT VARIANT 276
FT /note="R -> W (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs151173406)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077194"
FT VARIANT 281
FT /note="V -> F (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs553396382)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077195"
FT VARIANT 289
FT /note="D -> G (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1180515976)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077196"
FT VARIANT 291
FT /note="D -> V (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs192564717)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077197"
FT VARIANT 325
FT /note="L -> M (in dbSNP:rs17852920)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038426"
FT VARIANT 342
FT /note="Q -> P (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs267606651)"
FT /evidence="ECO:0000269|PubMed:14973782"
FT /id="VAR_023366"
FT VARIANT 353
FT /note="Y -> D (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596259672)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077198"
FT VARIANT 358
FT /note="G -> R (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs886042742)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077199"
FT VARIANT 359
FT /note="S -> L (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1299775990)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077200"
FT VARIANT 360
FT /note="A -> V (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs398124348)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077201"
FT VARIANT 363
FT /note="G -> A (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596261161)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077202"
FT VARIANT 366
FT /note="L -> Q (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596261208)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077203"
FT VARIANT 367
FT /note="H -> Q (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1428414601)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077204"
FT VARIANT 382
FT /note="M -> K (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1596261268)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077205"
FT VARIANT 384
FT /note="G -> R (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs1057520122)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077206"
FT VARIANT 388
FT /note="P -> S (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs398124349)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_077207"
FT VARIANT 429
FT /note="D -> E (no effect on function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs9745522)"
FT /evidence="ECO:0000269|PubMed:14709599"
FT /id="VAR_023367"
FT VARIANT 438
FT /note="R -> W (in CDG1K; decreased function in protein
FT glycosylation as shown by rescue assays in an ALG1-
FT deficient yeast strain; dbSNP:rs16835020)"
FT /evidence="ECO:0000269|PubMed:26931382"
FT /id="VAR_049350"
FT VARIANT 455
FT /note="Q -> R (in dbSNP:rs17856919)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038427"
SQ SEQUENCE 464 AA; 52518 MW; 83F55FD12CFDDBE9 CRC64;
MAASCLVLLA LCLLLPLLLL GGWKRWRRGR AARHVVAVVL GDVGRSPRMQ YHALSLAMHG
FSVTLLGFCN SKPHDELLQN NRIQIVGLTE LQSLAVGPRV FQYGVKVVLQ AMYLLWKLMW
REPGAYIFLQ NPPGLPSIAV CWFVGCLCGS KLVIDWHNYG YSIMGLVHGP NHPLVLLAKW
YEKFFGRLSH LNLCVTNAMR EDLADNWHIR AVTVYDKPAS FFKETPLDLQ HRLFMKLGSM
HSPFRARSEP EDPVTERSAF TERDAGSGLV TRLRERPALL VSSTSWTEDE DFSILLAALE
KFEQLTLDGH NLPSLVCVIT GKGPLREYYS RLIHQKHFQH IQVCTPWLEA EDYPLLLGSA
DLGVCLHTSS SGLDLPMKVV DMFGCCLPVC AVNFKCLHEL VKHEENGLVF EDSEELAAQL
QMLFSNFPDP AGKLNQFRKN LRESQQLRWD ESWVQTVLPL VMDT
