ALG6_HUMAN
ID ALG6_HUMAN Reviewed; 507 AA.
AC Q9Y672; B3KMU2; Q5SXR9; Q9H3I0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267;
DE AltName: Full=Asparagine-linked glycosylation protein 6 homolog;
DE AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=ALG6; ORFNames=My046;
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], VARIANT CDG1C VAL-333, AND VARIANT PHE-304.
RX PubMed=10359825; DOI=10.1073/pnas.96.12.6982;
RA Imbach T., Burda P., Kuhnert P., Wevers R.A., Aebi M., Berger E.G.,
RA Hennet T.;
RT "A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene
RT causes carbohydrate-deficient glycoprotein syndrome type-Ic.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6982-6987(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-304.
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-304.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-304.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-304.
RC TISSUE=Placenta;
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 [7]
RP VARIANTS CDG1C HIS-131; ARG-308 AND VAL-333.
RX PubMed=11106564; DOI=10.1016/s0002-9440(10)64830-4;
RA Westphal V., Murch S., Kim S., Srikrishna G., Winchester B., Day R.,
RA Freeze H.H.;
RT "Reduced heparan sulfate accumulation in enterocytes contributes to
RT protein-losing enteropathy in a congenital disorder of glycosylation.";
RL Am. J. Pathol. 157:1917-1925(2000).
RN [8]
RP VARIANTS CDG1C VAL-333 AND PRO-478, AND VARIANT PHE-304.
RX PubMed=10914684; DOI=10.1007/s004390000293;
RA Imbach T., Gruenewald S., Schenk B., Burda P., Schollen E., Wevers R.A.,
RA Jaeken J., de Klerk J.B.C., Berger E.G., Matthijs G., Aebi M., Hennet T.;
RT "Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic.";
RL Hum. Genet. 106:538-545(2000).
RN [9]
RP VARIANT CDG1C ILE-299 DEL, AND VARIANT PHE-304.
RX PubMed=10924277; DOI=10.1006/mgme.2000.3017;
RA Westphal V., Schottstaedt C., Marquardt T., Freeze H.H.;
RT "Analysis of multiple mutations in the hALG6 gene in a patient with
RT congenital disorder of glycosylation Ic.";
RL Mol. Genet. Metab. 70:219-223(2000).
RN [10]
RP VARIANT PHE-304.
RX PubMed=11558905; DOI=10.1007/s100380170038;
RA Vuillaumier-Barrot S., Le Bizec C., Durand G., Seta N.;
RT "The T911C (F304S) substitution in the human ALG6 gene is a common
RT polymorphism and not a causal mutation of CDG-Ic.";
RL J. Hum. Genet. 46:547-548(2001).
RN [11]
RP VARIANTS CDG1C ILE-170 AND LEU-444 DEL.
RX PubMed=11134235; DOI=10.1136/jmg.38.1.14;
RA de Lonlay P., Seta N., Barrot S., Chabrol B., Drouin V., Gabriel B.M.,
RA Journel H., Kretz M., Laurent J., Le Merrer M., Leroy A., Pedespan D.,
RA Sarda P., Villeneuve N., Schmitz J., van Schaftingen E., Matthijs G.,
RA Jaeken J., Koerner C., Munnich A., Saudubray J.-M., Cormier-Daire V.;
RT "A broad spectrum of clinical presentations in congenital disorders of
RT glycosylation I: a series of 26 cases.";
RL J. Med. Genet. 38:14-19(2001).
RN [12]
RP VARIANT CDG1C GLU-227.
RX PubMed=12357336; DOI=10.1038/sj.ejhg.5200858;
RA Schollen E., Martens K., Geuzens E., Matthijs G.;
RT "DHPLC analysis as a platform for molecular diagnosis of congenital
RT disorders of glycosylation (CDG).";
RL Eur. J. Hum. Genet. 10:643-648(2002).
RN [13]
RP CHARACTERIZATION OF VARIANT PHE-304.
RX PubMed=11875054; DOI=10.1093/hmg/11.5.599;
RA Westphal V., Kjaergaard S., Schollen E., Martens K., Gruenewald S.,
RA Schwartz M., Matthijs G., Freeze H.H.;
RT "A frequent mild mutation in ALG6 may exacerbate the clinical severity of
RT patients with congenital disorder of glycosylation Ia (CDG-Ia) caused by
RT phosphomannomutase deficiency.";
RL Hum. Mol. Genet. 11:599-604(2002).
RN [14]
RP VARIANT CDG1C HIS-131.
RX PubMed=14517965; DOI=10.1002/humu.9195;
RA Westphal V., Xiao M., Kwok P.-Y., Freeze H.H.;
RT "Identification of a frequent variant in ALG6, the cause of congenital
RT disorder of glycosylation-Ic.";
RL Hum. Mutat. 22:420-421(2003).
CC -!- FUNCTION: Adds the first glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Man(9)GlcNAc(2)-PP-Dol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DISEASE: Congenital disorder of glycosylation 1C (CDG1C) [MIM:603147]:
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:10359825,
CC ECO:0000269|PubMed:10914684, ECO:0000269|PubMed:10924277,
CC ECO:0000269|PubMed:11106564, ECO:0000269|PubMed:11134235,
CC ECO:0000269|PubMed:12357336, ECO:0000269|PubMed:14517965}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF102851; AAD41466.1; -; mRNA.
DR EMBL; AF063604; AAG43163.1; -; mRNA.
DR EMBL; AK022700; BAG51104.1; -; mRNA.
DR EMBL; AL592218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06571.1; -; Genomic_DNA.
DR EMBL; BC001253; AAH01253.1; -; mRNA.
DR CCDS; CCDS30735.1; -.
DR RefSeq; NP_037471.2; NM_013339.3.
DR AlphaFoldDB; Q9Y672; -.
DR SMR; Q9Y672; -.
DR BioGRID; 118970; 34.
DR IntAct; Q9Y672; 11.
DR MINT; Q9Y672; -.
DR STRING; 9606.ENSP00000360149; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR iPTMnet; Q9Y672; -.
DR PhosphoSitePlus; Q9Y672; -.
DR SwissPalm; Q9Y672; -.
DR BioMuta; ALG6; -.
DR DMDM; 21263380; -.
DR EPD; Q9Y672; -.
DR jPOST; Q9Y672; -.
DR MassIVE; Q9Y672; -.
DR PaxDb; Q9Y672; -.
DR PeptideAtlas; Q9Y672; -.
DR PRIDE; Q9Y672; -.
DR ProteomicsDB; 86610; -.
DR Antibodypedia; 33348; 111 antibodies from 23 providers.
DR DNASU; 29929; -.
DR Ensembl; ENST00000263440.6; ENSP00000263440.5; ENSG00000088035.18.
DR GeneID; 29929; -.
DR KEGG; hsa:29929; -.
DR MANE-Select; ENST00000263440.6; ENSP00000263440.5; NM_013339.4; NP_037471.2.
DR UCSC; uc021oof.1; human.
DR CTD; 29929; -.
DR DisGeNET; 29929; -.
DR GeneCards; ALG6; -.
DR HGNC; HGNC:23157; ALG6.
DR HPA; ENSG00000088035; Low tissue specificity.
DR MalaCards; ALG6; -.
DR MIM; 603147; phenotype.
DR MIM; 604566; gene.
DR neXtProt; NX_Q9Y672; -.
DR OpenTargets; ENSG00000088035; -.
DR Orphanet; 79320; ALG6-CDG.
DR PharmGKB; PA134925619; -.
DR VEuPathDB; HostDB:ENSG00000088035; -.
DR eggNOG; KOG2575; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_008110_3_0_1; -.
DR InParanoid; Q9Y672; -.
DR OMA; RQWYFNT; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q9Y672; -.
DR TreeFam; TF314522; -.
DR BRENDA; 2.4.1.267; 2681.
DR PathwayCommons; Q9Y672; -.
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-4724289; Defective ALG6 causes CDG-1c.
DR SignaLink; Q9Y672; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 29929; 89 hits in 1084 CRISPR screens.
DR ChiTaRS; ALG6; human.
DR GeneWiki; ALG6; -.
DR GenomeRNAi; 29929; -.
DR Pharos; Q9Y672; Tbio.
DR PRO; PR:Q9Y672; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y672; protein.
DR Bgee; ENSG00000088035; Expressed in secondary oocyte and 182 other tissues.
DR ExpressionAtlas; Q9Y672; baseline and differential.
DR Genevisible; Q9Y672; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004583; F:dolichyl-phosphate-glucose-glycolipid alpha-glucosyltransferase activity; TAS:Reactome.
DR GO; GO:0046527; F:glucosyltransferase activity; IDA:MGI.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:MGI.
DR InterPro; IPR039488; ALG6.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF1; PTHR12413:SF1; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 1: Evidence at protein level;
KW Congenital disorder of glycosylation; Disease variant;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..507
FT /note="Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
FT glucosyltransferase"
FT /id="PRO_0000174156"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 131
FT /note="Y -> H (in CDG1C; dbSNP:rs35383149)"
FT /evidence="ECO:0000269|PubMed:11106564,
FT ECO:0000269|PubMed:14517965"
FT /id="VAR_022511"
FT VARIANT 170
FT /note="S -> I (in CDG1C)"
FT /evidence="ECO:0000269|PubMed:11134235"
FT /id="VAR_022512"
FT VARIANT 226
FT /note="K -> N (in dbSNP:rs35604168)"
FT /id="VAR_055493"
FT VARIANT 227
FT /note="G -> E (in CDG1C; dbSNP:rs372079206)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022513"
FT VARIANT 299
FT /note="Missing (in CDG1C)"
FT /evidence="ECO:0000269|PubMed:10924277"
FT /id="VAR_013441"
FT VARIANT 304
FT /note="S -> F (may act as disease modifier and exacerbate
FT clinical severity in patients with a congenital disorder of
FT glycosylation; slightly decreased function as shown by
FT rescue experiments of defective glycosylation in an alg6-
FT deficient S.cerevisiae strain; dbSNP:rs4630153)"
FT /evidence="ECO:0000269|PubMed:10914684,
FT ECO:0000269|PubMed:10924277, ECO:0000269|PubMed:11558905,
FT ECO:0000269|PubMed:11875054"
FT /id="VAR_013442"
FT VARIANT 308
FT /note="S -> R (in CDG1C)"
FT /evidence="ECO:0000269|PubMed:11106564"
FT /id="VAR_022514"
FT VARIANT 333
FT /note="A -> V (in CDG1C; dbSNP:rs121908443)"
FT /evidence="ECO:0000269|PubMed:10359825,
FT ECO:0000269|PubMed:10914684, ECO:0000269|PubMed:11106564"
FT /id="VAR_013443"
FT VARIANT 444
FT /note="Missing (in CDG1C)"
FT /evidence="ECO:0000269|PubMed:11134235"
FT /id="VAR_022515"
FT VARIANT 478
FT /note="S -> P (in CDG1C; dbSNP:rs121908444)"
FT /evidence="ECO:0000269|PubMed:10914684"
FT /id="VAR_013444"
FT CONFLICT 111
FT /note="F -> L (in Ref. 2; AAG43163)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="T -> P (in Ref. 2; AAG43163)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="T -> P (in Ref. 2; AAG43163)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="T -> A (in Ref. 2; AAG43163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 58121 MW; 8BAC4BA9B8E366B9 CRC64;
MEKWYLMTVV VLIGLTVRWT VSLNSYSGAG KPPMFGDYEA QRHWQEITFN LPVKQWYFNS
SDNNLQYWGL DYPPLTAYHS LLCAYVAKFI NPDWIALHTS RGYESQAHKL FMRTTVLIAD
LLIYIPAVVL YCCCLKEIST KKKIANALCI LLYPGLILID YGHFQYNSVS LGFALWGVLG
ISCDCDLLGS LAFCLAINYK QMELYHALPF FCFLLGKCFK KGLKGKGFVL LVKLACIVVA
SFVLCWLPFF TEREQTLQVL RRLFPVDRGL FEDKVANIWC SFNVFLKIKD ILPRHIQLIM
SFCSTFLSLL PACIKLILQP SSKGFKFTLV SCALSFFLFS FQVHEKSILL VSLPVCLVLS
EIPFMSTWFL LVSTFSMLPL LLKDELLMPS VVTTMAFFIA CVTSFSIFEK TSEEELQLKS
FSISVRKYLP CFTFLSRIIQ YLFLISVITM VLLTLMTVTL DPPQKLPDLF SVLVCFVSCL
NFLFFLVYFN IIIMWDSKSG RNQKKIS
