Full text data of MOGS
MOGS
(GCS1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Mannosyl-oligosaccharide glucosidase; 3.2.1.106 (Processing A-glucosidase I)
Mannosyl-oligosaccharide glucosidase; 3.2.1.106 (Processing A-glucosidase I)
UniProt
Q13724
ID MOGS_HUMAN Reviewed; 837 AA.
AC Q13724; A8K938; F5H6D0; Q17RN9; Q8TCT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 5.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Processing A-glucosidase I;
GN Name=MOGS; Synonyms=GCS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-236; ASN-239
RP AND SER-293.
RC TISSUE=Hippocampus;
RX PubMed=7635146; DOI=10.1111/j.1432-1033.1995.tb20706.x;
RA Kalz-Fueller B., Bieberich E., Bause E.;
RT "Cloning and expression of glucosidase I from human hippocampus.";
RL Eur. J. Biochem. 231:344-351(1995).
RN [2]
RP ERRATUM.
RA Kalz-Fueller B., Bieberich E., Bause E.;
RL Eur. J. Biochem. 249:912-912(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Voelker C.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.,
RA Buerckstuemmer T., 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 VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=10788335; DOI=10.1086/302948;
RA De Praeter C.M., Gerwig G.J., Bause E., Nuytinck L.K.,
RA Vliegenthart J.F.G., Breuer W., Kamerling J.P., Espeel M.F.,
RA Martin J.-J., De Paepe A.M., Chan N.W.C., Dacremont G.A.,
RA Van Coster R.N.;
RT "A novel disorder caused by defective biosynthesis of N-linked
RT oligosaccharides due to glucosidase I deficiency.";
RL Am. J. Hum. Genet. 66:1744-1756(2000).
RN [10]
RP CHARACTERIZATION OF VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=12145188; DOI=10.1093/glycob/cwf050;
RA Voelker C., De Praeter C.M., Hardt B., Breuer W., Kalz-Fueller B.,
RA Van Coster R.N., Bause E.;
RT "Processing of N-linked carbohydrate chains in a patient with
RT glucosidase I deficiency (CDG type IIb).";
RL Glycobiology 12:473-483(2002).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from
CC the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly
CC specific manner.
CC -!- CATALYTIC ACTIVITY: Exohydrolysis of the non-reducing terminal
CC glucose residues in the mannosyl-oligosaccharide
CC Glc(3)Man(9)GlcNAc(2).
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13724-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13724-2; Sequence=VSP_046921;
CC Note=Gene prediction based on EST data;
CC -!- DISEASE: Type IIb congenital disorder of glycosylation (CDGIIb)
CC [MIM:606056]: Characterized by marked generalized hypotonia and
CC hypomotility of the neonate, dysmorphic features, including a
CC prominent occiput, short palpebral fissures, retrognathia, high
CC arched palate, generalized edema, and hypoplastic genitalia.
CC Symptoms of the infant included hepatomegaly, hypoventilation,
CC feeding problems and seizures. The clinical course was progressive
CC and the infant did not survive more than a few months. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/GCS1";
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DR EMBL; X87237; CAA60683.1; -; mRNA.
DR EMBL; AJ422288; CAD19636.1; -; Genomic_DNA.
DR EMBL; AK292553; BAF85242.1; -; mRNA.
DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99653.1; -; Genomic_DNA.
DR EMBL; BC117252; AAI17253.1; -; mRNA.
DR EMBL; BC117250; AAI17251.1; -; mRNA.
DR PIR; S66258; S66258.
DR RefSeq; NP_001139630.1; NM_001146158.1.
DR RefSeq; NP_006293.2; NM_006302.2.
DR UniGene; Hs.516119; -.
DR ProteinModelPortal; Q13724; -.
DR SMR; Q13724; 94-830.
DR IntAct; Q13724; 6.
DR MINT; MINT-1414631; -.
DR STRING; 9606.ENSP00000233616; -.
DR ChEMBL; CHEMBL4684; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR PhosphoSite; Q13724; -.
DR DMDM; 116242490; -.
DR PaxDb; Q13724; -.
DR PeptideAtlas; Q13724; -.
DR PRIDE; Q13724; -.
DR Ensembl; ENST00000233616; ENSP00000233616; ENSG00000115275.
DR Ensembl; ENST00000452063; ENSP00000388201; ENSG00000115275.
DR GeneID; 7841; -.
DR KEGG; hsa:7841; -.
DR UCSC; uc010ffh.3; human.
DR CTD; 7841; -.
DR GeneCards; GC02M074688; -.
DR H-InvDB; HIX0002184; -.
DR HGNC; HGNC:24862; MOGS.
DR HPA; HPA011969; -.
DR MIM; 601336; gene.
DR MIM; 606056; phenotype.
DR neXtProt; NX_Q13724; -.
DR Orphanet; 79330; GCS1-CDG syndrome.
DR PharmGKB; PA164723075; -.
DR eggNOG; NOG305138; -.
DR HOGENOM; HOG000201473; -.
DR InParanoid; Q13724; -.
DR KO; K01228; -.
DR OMA; WKAPLYT; -.
DR OrthoDB; EOG7XSTD6; -.
DR PhylomeDB; Q13724; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00280; -.
DR ChiTaRS; MOGS; human.
DR GeneWiki; GCS1; -.
DR GenomeRNAi; 7841; -.
DR NextBio; 30249; -.
DR PRO; PR:Q13724; -.
DR ArrayExpress; Q13724; -.
DR Bgee; Q13724; -.
DR Genevestigator; Q13724; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015926; F:glucosidase activity; TAS:ProtInc.
DR GO; GO:0004573; F:mannosyl-oligosaccharide glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Disease mutation;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Polymorphism; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 837 Mannosyl-oligosaccharide glucosidase.
FT /FTId=PRO_0000057710.
FT TOPO_DOM 1 38 Cytoplasmic (Potential).
FT TRANSMEM 39 59 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 60 837 Lumenal (Potential).
FT REGION 76 137 Required for endoplasmic reticulum
FT targeting (By similarity).
FT MOTIF 3 9 Endoplasmic reticulum targeting.
FT CARBOHYD 657 657 N-linked (GlcNAc...).
FT VAR_SEQ 1 106 Missing (in isoform 2).
FT /FTId=VSP_046921.
FT VARIANT 222 222 G -> R (in dbSNP:rs3213671).
FT /FTId=VAR_049233.
FT VARIANT 236 236 E -> Q (in dbSNP:rs1063587).
FT /FTId=VAR_019361.
FT VARIANT 239 239 D -> N (in dbSNP:rs1063588).
FT /FTId=VAR_019362.
FT VARIANT 293 293 P -> S (in dbSNP:rs2268416).
FT /FTId=VAR_049234.
FT VARIANT 486 486 R -> T (in CDGIIb; loss of activity).
FT /FTId=VAR_018966.
FT VARIANT 495 495 R -> P (in dbSNP:rs34075781).
FT /FTId=VAR_049235.
FT VARIANT 652 652 F -> L (in CDGIIb; loss of activity).
FT /FTId=VAR_018967.
FT VARIANT 785 785 G -> S (in dbSNP:rs35533773).
FT /FTId=VAR_049236.
FT CONFLICT 330 330 I -> F (in Ref. 1; CAA60683).
FT CONFLICT 389 389 V -> A (in Ref. 1; CAA60683).
FT CONFLICT 605 605 A -> G (in Ref. 1; CAA60683).
FT CONFLICT 818 818 Missing (in Ref. 1; CAA60683).
SQ SEQUENCE 837 AA; 91918 MW; 11C5B09301B50DEE CRC64;
MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV LSLALGMSGR
WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR PHVYFGMKTR SPKPLLTGLM
WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF HDGLSFGRQH IQDGALRLTT EFVKRPGGQH
GGDWSWRVTV EPQDSGTSAL PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF
RFTLLPPTSP GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL
PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP RLAGSLLTQA
LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG GIGYFYGQGL VLPDIGVEGS
EQKVDPALFP PVPLFTAVPS RSFFPRGFLW DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA
DGWIGREQIL GDEARARVPP EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR
LHAWFSWLHQ SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL
RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG VFADFGNHTK
AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR LLDPTSSRLG PLLDILADSR
HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW RGAVWLNVNY LALGALHHYG HLEGPHQARA
AKLHGELRAN VVGNVWRQYQ ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY
//
ID MOGS_HUMAN Reviewed; 837 AA.
AC Q13724; A8K938; F5H6D0; Q17RN9; Q8TCT5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 5.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Mannosyl-oligosaccharide glucosidase;
DE EC=3.2.1.106;
DE AltName: Full=Processing A-glucosidase I;
GN Name=MOGS; Synonyms=GCS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-236; ASN-239
RP AND SER-293.
RC TISSUE=Hippocampus;
RX PubMed=7635146; DOI=10.1111/j.1432-1033.1995.tb20706.x;
RA Kalz-Fueller B., Bieberich E., Bause E.;
RT "Cloning and expression of glucosidase I from human hippocampus.";
RL Eur. J. Biochem. 231:344-351(1995).
RN [2]
RP ERRATUM.
RA Kalz-Fueller B., Bieberich E., Bause E.;
RL Eur. J. Biochem. 249:912-912(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Voelker C.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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.,
RA Buerckstuemmer T., 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 VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=10788335; DOI=10.1086/302948;
RA De Praeter C.M., Gerwig G.J., Bause E., Nuytinck L.K.,
RA Vliegenthart J.F.G., Breuer W., Kamerling J.P., Espeel M.F.,
RA Martin J.-J., De Paepe A.M., Chan N.W.C., Dacremont G.A.,
RA Van Coster R.N.;
RT "A novel disorder caused by defective biosynthesis of N-linked
RT oligosaccharides due to glucosidase I deficiency.";
RL Am. J. Hum. Genet. 66:1744-1756(2000).
RN [10]
RP CHARACTERIZATION OF VARIANTS CDGIIB THR-486 AND LEU-652.
RX PubMed=12145188; DOI=10.1093/glycob/cwf050;
RA Voelker C., De Praeter C.M., Hardt B., Breuer W., Kalz-Fueller B.,
RA Van Coster R.N., Bause E.;
RT "Processing of N-linked carbohydrate chains in a patient with
RT glucosidase I deficiency (CDG type IIb).";
RL Glycobiology 12:473-483(2002).
CC -!- FUNCTION: Cleaves the distal alpha 1,2-linked glucose residue from
CC the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly
CC specific manner.
CC -!- CATALYTIC ACTIVITY: Exohydrolysis of the non-reducing terminal
CC glucose residues in the mannosyl-oligosaccharide
CC Glc(3)Man(9)GlcNAc(2).
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13724-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13724-2; Sequence=VSP_046921;
CC Note=Gene prediction based on EST data;
CC -!- DISEASE: Type IIb congenital disorder of glycosylation (CDGIIb)
CC [MIM:606056]: Characterized by marked generalized hypotonia and
CC hypomotility of the neonate, dysmorphic features, including a
CC prominent occiput, short palpebral fissures, retrognathia, high
CC arched palate, generalized edema, and hypoplastic genitalia.
CC Symptoms of the infant included hepatomegaly, hypoventilation,
CC feeding problems and seizures. The clinical course was progressive
CC and the infant did not survive more than a few months. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/GCS1";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X87237; CAA60683.1; -; mRNA.
DR EMBL; AJ422288; CAD19636.1; -; Genomic_DNA.
DR EMBL; AK292553; BAF85242.1; -; mRNA.
DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99653.1; -; Genomic_DNA.
DR EMBL; BC117252; AAI17253.1; -; mRNA.
DR EMBL; BC117250; AAI17251.1; -; mRNA.
DR PIR; S66258; S66258.
DR RefSeq; NP_001139630.1; NM_001146158.1.
DR RefSeq; NP_006293.2; NM_006302.2.
DR UniGene; Hs.516119; -.
DR ProteinModelPortal; Q13724; -.
DR SMR; Q13724; 94-830.
DR IntAct; Q13724; 6.
DR MINT; MINT-1414631; -.
DR STRING; 9606.ENSP00000233616; -.
DR ChEMBL; CHEMBL4684; -.
DR CAZy; GH63; Glycoside Hydrolase Family 63.
DR PhosphoSite; Q13724; -.
DR DMDM; 116242490; -.
DR PaxDb; Q13724; -.
DR PeptideAtlas; Q13724; -.
DR PRIDE; Q13724; -.
DR Ensembl; ENST00000233616; ENSP00000233616; ENSG00000115275.
DR Ensembl; ENST00000452063; ENSP00000388201; ENSG00000115275.
DR GeneID; 7841; -.
DR KEGG; hsa:7841; -.
DR UCSC; uc010ffh.3; human.
DR CTD; 7841; -.
DR GeneCards; GC02M074688; -.
DR H-InvDB; HIX0002184; -.
DR HGNC; HGNC:24862; MOGS.
DR HPA; HPA011969; -.
DR MIM; 601336; gene.
DR MIM; 606056; phenotype.
DR neXtProt; NX_Q13724; -.
DR Orphanet; 79330; GCS1-CDG syndrome.
DR PharmGKB; PA164723075; -.
DR eggNOG; NOG305138; -.
DR HOGENOM; HOG000201473; -.
DR InParanoid; Q13724; -.
DR KO; K01228; -.
DR OMA; WKAPLYT; -.
DR OrthoDB; EOG7XSTD6; -.
DR PhylomeDB; Q13724; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_17015; Metabolism of proteins.
DR UniPathway; UPA00280; -.
DR ChiTaRS; MOGS; human.
DR GeneWiki; GCS1; -.
DR GenomeRNAi; 7841; -.
DR NextBio; 30249; -.
DR PRO; PR:Q13724; -.
DR ArrayExpress; Q13724; -.
DR Bgee; Q13724; -.
DR Genevestigator; Q13724; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015926; F:glucosidase activity; TAS:ProtInc.
DR GO; GO:0004573; F:mannosyl-oligosaccharide glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR InterPro; IPR004888; Glycoside_hydrolase_63.
DR PANTHER; PTHR10412; PTHR10412; 1.
DR Pfam; PF03200; Glyco_hydro_63; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Disease mutation;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Polymorphism; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 837 Mannosyl-oligosaccharide glucosidase.
FT /FTId=PRO_0000057710.
FT TOPO_DOM 1 38 Cytoplasmic (Potential).
FT TRANSMEM 39 59 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 60 837 Lumenal (Potential).
FT REGION 76 137 Required for endoplasmic reticulum
FT targeting (By similarity).
FT MOTIF 3 9 Endoplasmic reticulum targeting.
FT CARBOHYD 657 657 N-linked (GlcNAc...).
FT VAR_SEQ 1 106 Missing (in isoform 2).
FT /FTId=VSP_046921.
FT VARIANT 222 222 G -> R (in dbSNP:rs3213671).
FT /FTId=VAR_049233.
FT VARIANT 236 236 E -> Q (in dbSNP:rs1063587).
FT /FTId=VAR_019361.
FT VARIANT 239 239 D -> N (in dbSNP:rs1063588).
FT /FTId=VAR_019362.
FT VARIANT 293 293 P -> S (in dbSNP:rs2268416).
FT /FTId=VAR_049234.
FT VARIANT 486 486 R -> T (in CDGIIb; loss of activity).
FT /FTId=VAR_018966.
FT VARIANT 495 495 R -> P (in dbSNP:rs34075781).
FT /FTId=VAR_049235.
FT VARIANT 652 652 F -> L (in CDGIIb; loss of activity).
FT /FTId=VAR_018967.
FT VARIANT 785 785 G -> S (in dbSNP:rs35533773).
FT /FTId=VAR_049236.
FT CONFLICT 330 330 I -> F (in Ref. 1; CAA60683).
FT CONFLICT 389 389 V -> A (in Ref. 1; CAA60683).
FT CONFLICT 605 605 A -> G (in Ref. 1; CAA60683).
FT CONFLICT 818 818 Missing (in Ref. 1; CAA60683).
SQ SEQUENCE 837 AA; 91918 MW; 11C5B09301B50DEE CRC64;
MARGERRRRA VPAEGVRTAE RAARGGPGRR DGRGGGPRST AGGVALAVVV LSLALGMSGR
WVLAWYRARR AVTLHSAPPV LPADSSSPAV APDLFWGTYR PHVYFGMKTR SPKPLLTGLM
WAQQGTTPGT PKLRHTCEQG DGVGPYGWEF HDGLSFGRQH IQDGALRLTT EFVKRPGGQH
GGDWSWRVTV EPQDSGTSAL PLVSLFFYVV TDGKEVLLPE VGAKGQLKFI SGHTSELGDF
RFTLLPPTSP GDTAPKYGSY NVFWTSNPGL PLLTEMVKSR LNSWFQHRPP GAPPERYLGL
PGSLKWEDRG PSGQGQGQFL IQQVTLKIPI SIEFVFESGS AQAGGNQALP RLAGSLLTQA
LESHAEGFRE RFEKTFQLKE KGLSSGEQVL GQAALSGLLG GIGYFYGQGL VLPDIGVEGS
EQKVDPALFP PVPLFTAVPS RSFFPRGFLW DEGFHQLVVQ RWDPSLTREA LGHWLGLLNA
DGWIGREQIL GDEARARVPP EFLVQRAVHA NPPTLLLPVA HMLEVGDPDD LAFLRKALPR
LHAWFSWLHQ SQAGPLPLSY RWRGRDPALP TLLNPKTLPS GLDDYPRASH PSVTERHLDL
RCWVALGARV LTRLAEHLGE AEVAAELGPL AASLEAAESL DELHWAPELG VFADFGNHTK
AVQLKPRPPQ GLVRVVGRPQ PQLQYVDALG YVSLFPLLLR LLDPTSSRLG PLLDILADSR
HLWSPFGLRS LAASSSFYGQ RNSEHDPPYW RGAVWLNVNY LALGALHHYG HLEGPHQARA
AKLHGELRAN VVGNVWRQYQ ATGFLWEQYS DRDGRGMGCR PFHGWTSLVL LAMAEDY
//
MIM
601336
*RECORD*
*FIELD* NO
601336
*FIELD* TI
*601336 GLUCOSIDASE I; GCS1
*FIELD* TX
DESCRIPTION
The processing of N-linked glycoproteins is initiated by the action of
read moreglucosidase I, which cleaves specifically the distal alpha-1,2-linked
glucose residue in the Glc(3)-Man(9)-GlcNAc(2) oligosaccharide precursor
after its en bloc transfer from dolichyl diphosphate to the nascent
polypeptide chain (Kornfeld and Kornfeld, 1985). The resulting
Glc(2)-Man(9)-GlcNAc(2) intermediate is then further modified by
glucosidase II and several ER- and Golgi-resident mannosidases and
glycosyltransferases, finally yielding a complex array of glycan
structures.
CLONING
Kalz-Fuller et al. (1995) used the amino acid sequence of tryptic
peptides of the pig liver glucosidase I enzyme to synthesize degenerate
oligonucleotides that were used to amplify a specific cDNA probe by PCR
with porcine cDNA. Screening of a human hippocampus cDNA library with
this probe resulted in the isolation of several glucosidase I-specific
clones, allowing the reconstruction of a full-length human cDNA of 2,881
bp. The oligonucleotide sequence showed no homology to other processing
enzymes cloned to that time.
MAPPING
By fluorescence in situ hybridization, Kalz-Fuller et al. (1996) mapped
the glucosidase I gene to 2p13-p12. They confirmed the localization with
PCR-based analysis of somatic cell hybrids.
MOLECULAR GENETICS
De Praeter et al. (2000) identified a glucosidase I defect in a neonate
with severe generalized hypotonia and dysmorphic features consistent
with congenital disorder of glycosylation type IIb (CDG2B; 606056).
Molecular studies showed that the patient was a compound heterozygote
for 2 missense mutations in the GCS1 gene (601336.0001-601336.0002).
*FIELD* AV
.0001
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb
GCS1, ARG486THR
In a neonate with CDG2B (606056), De Praeter et al. (2000) identified
compound heterozygosity for 2 missense mutations in the GCS1 gene: a
1587G-C transition resulting in an arg486-to-thr (R486T) substitution,
and a 2085T-C transition resulting in a phe652-to-leu (F652L;
601336.0002) substitution. The mother was heterozygous for the former
mutation, whereas the father was heterozygous for the latter. The
patient was the first child of second-cousin parents and presented with
severe generalized hypotonia and dysmorphic features.
.0002
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb
GCS1, PHE652LEU
See 601336.0001 and De Praeter et al. (2000).
*FIELD* RF
1. De Praeter, C. M.; Gerwig, G. J.; Bause, E.; Nuytinck, L. K.; Vliegenthart,
J. F. G.; Breuer, W.; Kamerling, J. P.; Espeel, M. F.; Martin, J.-J.
R.; De Paepe, A. M.; Chan, N. W. C.; Dacremont, G. A.; Van Coster,
R. N.: A novel disorder caused by defective biosynthesis of N-linked
oligosaccharides due to glucosidase I deficiency. Am. J. Hum. Genet. 66:
1744-1756, 2000.
2. Kalz-Fuller, B.; Bieberich, E.; Bause, E.: Cloning and expression
of glucosidase I from human hippocampus. Europ. J. Biochem. 231:
344-351, 1995. Note: Erratum: Europ. J. Biochem. 249: 912 only, 1997.
3. Kalz-Fuller, B.; Heidrich-Kaul, C.; Nothen, M.; Bause, E.; Schwanitz,
G.: Localization of the human glucosidase I gene to chromosome 2p12-p13
by fluorescence in situ hybridization and PCR analysis of somatic
cell hybrids. Genomics 34: 442-443, 1996.
4. Kornfeld, R.; Kornfeld, S.: Assembly of asparagine-linked oligosaccharides. Annu.
Rev. Biochem. 54: 631-664, 1985.
*FIELD* CN
Victor A. McKusick - updated: 7/25/2000
*FIELD* CD
Victor A. McKusick: 7/5/1996
*FIELD* ED
terry: 08/09/2012
carol: 6/27/2007
ckniffin: 6/22/2007
carol: 6/22/2001
carol: 8/2/2000
terry: 7/25/2000
terry: 7/24/1996
mark: 7/5/1996
*RECORD*
*FIELD* NO
601336
*FIELD* TI
*601336 GLUCOSIDASE I; GCS1
*FIELD* TX
DESCRIPTION
The processing of N-linked glycoproteins is initiated by the action of
read moreglucosidase I, which cleaves specifically the distal alpha-1,2-linked
glucose residue in the Glc(3)-Man(9)-GlcNAc(2) oligosaccharide precursor
after its en bloc transfer from dolichyl diphosphate to the nascent
polypeptide chain (Kornfeld and Kornfeld, 1985). The resulting
Glc(2)-Man(9)-GlcNAc(2) intermediate is then further modified by
glucosidase II and several ER- and Golgi-resident mannosidases and
glycosyltransferases, finally yielding a complex array of glycan
structures.
CLONING
Kalz-Fuller et al. (1995) used the amino acid sequence of tryptic
peptides of the pig liver glucosidase I enzyme to synthesize degenerate
oligonucleotides that were used to amplify a specific cDNA probe by PCR
with porcine cDNA. Screening of a human hippocampus cDNA library with
this probe resulted in the isolation of several glucosidase I-specific
clones, allowing the reconstruction of a full-length human cDNA of 2,881
bp. The oligonucleotide sequence showed no homology to other processing
enzymes cloned to that time.
MAPPING
By fluorescence in situ hybridization, Kalz-Fuller et al. (1996) mapped
the glucosidase I gene to 2p13-p12. They confirmed the localization with
PCR-based analysis of somatic cell hybrids.
MOLECULAR GENETICS
De Praeter et al. (2000) identified a glucosidase I defect in a neonate
with severe generalized hypotonia and dysmorphic features consistent
with congenital disorder of glycosylation type IIb (CDG2B; 606056).
Molecular studies showed that the patient was a compound heterozygote
for 2 missense mutations in the GCS1 gene (601336.0001-601336.0002).
*FIELD* AV
.0001
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb
GCS1, ARG486THR
In a neonate with CDG2B (606056), De Praeter et al. (2000) identified
compound heterozygosity for 2 missense mutations in the GCS1 gene: a
1587G-C transition resulting in an arg486-to-thr (R486T) substitution,
and a 2085T-C transition resulting in a phe652-to-leu (F652L;
601336.0002) substitution. The mother was heterozygous for the former
mutation, whereas the father was heterozygous for the latter. The
patient was the first child of second-cousin parents and presented with
severe generalized hypotonia and dysmorphic features.
.0002
CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb
GCS1, PHE652LEU
See 601336.0001 and De Praeter et al. (2000).
*FIELD* RF
1. De Praeter, C. M.; Gerwig, G. J.; Bause, E.; Nuytinck, L. K.; Vliegenthart,
J. F. G.; Breuer, W.; Kamerling, J. P.; Espeel, M. F.; Martin, J.-J.
R.; De Paepe, A. M.; Chan, N. W. C.; Dacremont, G. A.; Van Coster,
R. N.: A novel disorder caused by defective biosynthesis of N-linked
oligosaccharides due to glucosidase I deficiency. Am. J. Hum. Genet. 66:
1744-1756, 2000.
2. Kalz-Fuller, B.; Bieberich, E.; Bause, E.: Cloning and expression
of glucosidase I from human hippocampus. Europ. J. Biochem. 231:
344-351, 1995. Note: Erratum: Europ. J. Biochem. 249: 912 only, 1997.
3. Kalz-Fuller, B.; Heidrich-Kaul, C.; Nothen, M.; Bause, E.; Schwanitz,
G.: Localization of the human glucosidase I gene to chromosome 2p12-p13
by fluorescence in situ hybridization and PCR analysis of somatic
cell hybrids. Genomics 34: 442-443, 1996.
4. Kornfeld, R.; Kornfeld, S.: Assembly of asparagine-linked oligosaccharides. Annu.
Rev. Biochem. 54: 631-664, 1985.
*FIELD* CN
Victor A. McKusick - updated: 7/25/2000
*FIELD* CD
Victor A. McKusick: 7/5/1996
*FIELD* ED
terry: 08/09/2012
carol: 6/27/2007
ckniffin: 6/22/2007
carol: 6/22/2001
carol: 8/2/2000
terry: 7/25/2000
terry: 7/24/1996
mark: 7/5/1996
MIM
606056
*RECORD*
*FIELD* NO
606056
*FIELD* TI
#606056 CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb; CDG2B
;;CDG IIb; CDGIIb;;
GLUCOSIDASE I DEFICIENCY
read more*FIELD* TX
A number sign (#) is used with this entry because the disorder is caused
by mutation in the gene encoding glucosidase I (GCS1; 601336).
For an overview of congenital disorders of glycosylation (CDG), see
CDG1A (212065) and CDG2A (212066).
CLINICAL FEATURES
De Praeter et al. (2000) reported a neonate with severe generalized
hypotonia and dysmorphic features. The patient was born at 36 weeks'
gestation after an uneventful pregnancy and delivery. Marked generalized
hypotonia and hypomotility were noticed, as were dysmorphic features,
including a prominent occiput, short palpebral fissures, long eyelashes,
broad nose, retrognathia, high-arched palate, generalized edema, and
hypoplastic genitalia. Her hands were clenched and her fingers
overlapped, second over third and fifth over fourth. A band of alopecia
was seen on both parietal areas of the skull. A thoracic scoliosis was
present. The clinical course was progressive and was characterized by
the occurrence of hepatomegaly, hypoventilation, feeding problems,
seizures, and fatal outcome at age 74 days. The accumulation of a
tetrasaccharide in the patient's urine indicated a glycosylation defect.
Enzymologic studies on liver tissue and cultured skin fibroblasts
revealed severe glucosidase I deficiency. Residual activity was less
than 3% of control values. Glucosidase I activities in cultured skin
fibroblasts from both parents was found to be 50% of those of controls.
MOLECULAR GENETICS
In a patient with CDG2B, De Praeter et al. (2000) identified compound
heterozygosity for 2 mutations in the GCS1 gene
(601336.0001-601336.0002).
*FIELD* RF
1. De Praeter, C. M.; Gerwig, G. J.; Bause, E.; Nuytinck, L. K.; Vliegenthart,
J. F. G.; Breuer, W.; Kamerling, J. P.; Espeel, M. F.; Martin, J.-J.
R.; De Paepe, A. M.; Chan, N. W. C.; Dacremont, G. A.; Van Coster,
R. N.: A novel disorder caused by defective biosynthesis of N-linked
oligosaccharides due to glucosidase I deficiency. Am. J. Hum. Genet. 66:
1744-1756, 2000.
*FIELD* CS
INHERITANCE:
Autosomal recessive
HEAD AND NECK:
[Head];
Prominent occiput;
[Face];
Retrognathia;
[Eyes];
Short palpebral fissures;
Long eyelashes;
[Nose];
Broad nose;
[Mouth];
High-arched palate
RESPIRATORY:
Hypoventilation
ABDOMEN:
[Liver];
Hepatomegaly;
[Gastrointestinal];
Feeding problems
SKELETAL:
[Spine];
Thoracic scoliosis;
[Hands];
Clenched hands;
Overlapping fingers
NEUROLOGIC:
[Central nervous system];
Hypotonia;
Seizures
LABORATORY ABNORMALITIES:
Glucosidase I deficiency in liver and fibroblasts;
Normal isoelectric focusing of serum transferrin;
Abnormal urinary oligosaccharides
MOLECULAR BASIS:
Caused by mutation in the glucosidase I gene (GCS1, 601336.0001)
*FIELD* CD
Kelly A. Przylepa: 4/11/2002
*FIELD* ED
joanna: 04/11/2002
*FIELD* CD
Victor A. McKusick: 6/22/2001
*FIELD* ED
carol: 06/27/2007
ckniffin: 6/22/2007
carol: 7/6/2004
joanna: 4/11/2002
carol: 6/22/2001
*RECORD*
*FIELD* NO
606056
*FIELD* TI
#606056 CONGENITAL DISORDER OF GLYCOSYLATION, TYPE IIb; CDG2B
;;CDG IIb; CDGIIb;;
GLUCOSIDASE I DEFICIENCY
read more*FIELD* TX
A number sign (#) is used with this entry because the disorder is caused
by mutation in the gene encoding glucosidase I (GCS1; 601336).
For an overview of congenital disorders of glycosylation (CDG), see
CDG1A (212065) and CDG2A (212066).
CLINICAL FEATURES
De Praeter et al. (2000) reported a neonate with severe generalized
hypotonia and dysmorphic features. The patient was born at 36 weeks'
gestation after an uneventful pregnancy and delivery. Marked generalized
hypotonia and hypomotility were noticed, as were dysmorphic features,
including a prominent occiput, short palpebral fissures, long eyelashes,
broad nose, retrognathia, high-arched palate, generalized edema, and
hypoplastic genitalia. Her hands were clenched and her fingers
overlapped, second over third and fifth over fourth. A band of alopecia
was seen on both parietal areas of the skull. A thoracic scoliosis was
present. The clinical course was progressive and was characterized by
the occurrence of hepatomegaly, hypoventilation, feeding problems,
seizures, and fatal outcome at age 74 days. The accumulation of a
tetrasaccharide in the patient's urine indicated a glycosylation defect.
Enzymologic studies on liver tissue and cultured skin fibroblasts
revealed severe glucosidase I deficiency. Residual activity was less
than 3% of control values. Glucosidase I activities in cultured skin
fibroblasts from both parents was found to be 50% of those of controls.
MOLECULAR GENETICS
In a patient with CDG2B, De Praeter et al. (2000) identified compound
heterozygosity for 2 mutations in the GCS1 gene
(601336.0001-601336.0002).
*FIELD* RF
1. De Praeter, C. M.; Gerwig, G. J.; Bause, E.; Nuytinck, L. K.; Vliegenthart,
J. F. G.; Breuer, W.; Kamerling, J. P.; Espeel, M. F.; Martin, J.-J.
R.; De Paepe, A. M.; Chan, N. W. C.; Dacremont, G. A.; Van Coster,
R. N.: A novel disorder caused by defective biosynthesis of N-linked
oligosaccharides due to glucosidase I deficiency. Am. J. Hum. Genet. 66:
1744-1756, 2000.
*FIELD* CS
INHERITANCE:
Autosomal recessive
HEAD AND NECK:
[Head];
Prominent occiput;
[Face];
Retrognathia;
[Eyes];
Short palpebral fissures;
Long eyelashes;
[Nose];
Broad nose;
[Mouth];
High-arched palate
RESPIRATORY:
Hypoventilation
ABDOMEN:
[Liver];
Hepatomegaly;
[Gastrointestinal];
Feeding problems
SKELETAL:
[Spine];
Thoracic scoliosis;
[Hands];
Clenched hands;
Overlapping fingers
NEUROLOGIC:
[Central nervous system];
Hypotonia;
Seizures
LABORATORY ABNORMALITIES:
Glucosidase I deficiency in liver and fibroblasts;
Normal isoelectric focusing of serum transferrin;
Abnormal urinary oligosaccharides
MOLECULAR BASIS:
Caused by mutation in the glucosidase I gene (GCS1, 601336.0001)
*FIELD* CD
Kelly A. Przylepa: 4/11/2002
*FIELD* ED
joanna: 04/11/2002
*FIELD* CD
Victor A. McKusick: 6/22/2001
*FIELD* ED
carol: 06/27/2007
ckniffin: 6/22/2007
carol: 7/6/2004
joanna: 4/11/2002
carol: 6/22/2001