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 27-MAR-2024, entry version 190. 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. DR AlphaFoldDB; Q9BT22; -. DR BioGRID; 121033; 58. DR IntAct; Q9BT22; 19. 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; 9606-ENSP00000262374; -. DR PeptideAtlas; Q9BT22; -. DR ProteomicsDB; 4740; -. DR ProteomicsDB; 78943; -. [Q9BT22-1] DR Pumba; Q9BT22; -. DR Antibodypedia; 24484; 151 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 AGR; HGNC:18294; -. 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; CKLIIDW; -. DR OrthoDB; 1219598at2759; -. 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; 729 hits in 1169 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 120 other cell types or 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: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 CDD; cd03816; GT33_ALG1-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR InterPro; IPR026051; ALG1-like. DR InterPro; IPR001296; Glyco_trans_1. DR PANTHER; PTHR13036; BETA1,4 MANNOSYLTRANSFERASE; 1. DR PANTHER; PTHR13036:SF1; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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 //