ID   MOGS_HUMAN              Reviewed;         837 AA.
AC   Q13724; A8K938; F5H6D0; Q17RN9; Q8TCT5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 5.
DT   27-MAR-2024, entry version 206.
DE   RecName: Full=Mannosyl-oligosaccharide glucosidase {ECO:0000305|PubMed:7635146};
DE            EC=3.2.1.106 {ECO:0000269|PubMed:7635146};
DE   AltName: Full=Processing A-glucosidase I {ECO:0000305|PubMed:7635146};
GN   Name=MOGS {ECO:0000312|HGNC:HGNC:24862};
GN   Synonyms=GCS1 {ECO:0000312|HGNC:HGNC:24862};
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), FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP   ASN-657, AND VARIANTS GLN-236; ASN-239 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 OF PUBMED:7635146.
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., 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   [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., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., 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., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., 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., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   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., 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   [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 project:
RT   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., 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11]
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., Vliegenthart J.F.G.,
RA   Breuer W., Kamerling J.P., Espeel M.F., Martin J.-J., De Paepe A.M.,
RA   Chan N.W.C., Dacremont G.A., 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   [12]
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 glucosidase I
RT   deficiency (CDG type IIb).";
RL   Glycobiology 12:473-483(2002).
CC   -!- FUNCTION: In the context of N-glycan degradation, cleaves the distal
CC       alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2)
CC       oligosaccharide precursor in a highly specific manner.
CC       {ECO:0000269|PubMed:7635146}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-
CC         (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose +
CC         N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-
CC         D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-
CC         beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-
CC         [protein]; Xref=Rhea:RHEA:55988, Rhea:RHEA-COMP:12806, Rhea:RHEA-
CC         COMP:14355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:59082,
CC         ChEBI:CHEBI:132537; EC=3.2.1.106;
CC         Evidence={ECO:0000269|PubMed:7635146};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55989;
CC         Evidence={ECO:0000269|PubMed:7635146};
CC   -!- ACTIVITY REGULATION: Inhibited by 1-deoxynojirimycin (40% inhibition)
CC       and N,N-dimethyl-deoxynojirimycin (85% inhibition).
CC       {ECO:0000269|PubMed:7635146}.
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000269|PubMed:7635146}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:7635146}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O88941}.
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   -!- 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 prominent
CC       occiput, short palpebral fissures, retrognathia, high arched palate,
CC       generalized edema, and hypoplastic genitalia. Symptoms of the infant
CC       included hepatomegaly, hypoventilation, feeding problems and seizures.
CC       The clinical course was progressive and the infant did not survive more
CC       than a few months. {ECO:0000269|PubMed:10788335}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 63 family. {ECO:0000305}.
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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   CCDS; CCDS42700.1; -. [Q13724-1]
DR   CCDS; CCDS54370.1; -. [Q13724-2]
DR   PIR; S66258; S66258.
DR   RefSeq; NP_001139630.1; NM_001146158.1. [Q13724-2]
DR   RefSeq; NP_006293.2; NM_006302.2. [Q13724-1]
DR   AlphaFoldDB; Q13724; -.
DR   SMR; Q13724; -.
DR   BioGRID; 113599; 215.
DR   ELM; Q13724; -.
DR   IntAct; Q13724; 47.
DR   MINT; Q13724; -.
DR   STRING; 9606.ENSP00000410992; -.
DR   ChEMBL; CHEMBL4684; -.
DR   CAZy; GH63; Glycoside Hydrolase Family 63.
DR   GlyConnect; 1489; 6 N-Linked glycans (1 site).
DR   GlyCosmos; Q13724; 1 site, 7 glycans.
DR   GlyGen; Q13724; 2 sites, 7 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q13724; -.
DR   PhosphoSitePlus; Q13724; -.
DR   SwissPalm; Q13724; -.
DR   BioMuta; MOGS; -.
DR   DMDM; 116242490; -.
DR   EPD; Q13724; -.
DR   jPOST; Q13724; -.
DR   MassIVE; Q13724; -.
DR   MaxQB; Q13724; -.
DR   PaxDb; 9606-ENSP00000233616; -.
DR   PeptideAtlas; Q13724; -.
DR   ProteomicsDB; 27150; -.
DR   ProteomicsDB; 59667; -. [Q13724-1]
DR   Pumba; Q13724; -.
DR   Antibodypedia; 2372; 198 antibodies from 25 providers.
DR   DNASU; 7841; -.
DR   Ensembl; ENST00000448666.7; ENSP00000410992.3; ENSG00000115275.15. [Q13724-1]
DR   Ensembl; ENST00000452063.7; ENSP00000388201.2; ENSG00000115275.15. [Q13724-2]
DR   GeneID; 7841; -.
DR   KEGG; hsa:7841; -.
DR   MANE-Select; ENST00000448666.7; ENSP00000410992.3; NM_006302.3; NP_006293.2.
DR   UCSC; uc010ffi.4; human. [Q13724-1]
DR   AGR; HGNC:24862; -.
DR   CTD; 7841; -.
DR   DisGeNET; 7841; -.
DR   GeneCards; MOGS; -.
DR   GeneReviews; MOGS; -.
DR   HGNC; HGNC:24862; MOGS.
DR   HPA; ENSG00000115275; Low tissue specificity.
DR   MalaCards; MOGS; -.
DR   MIM; 601336; gene.
DR   MIM; 606056; phenotype.
DR   neXtProt; NX_Q13724; -.
DR   OpenTargets; ENSG00000115275; -.
DR   Orphanet; 79330; MOGS-CDG.
DR   PharmGKB; PA164723075; -.
DR   VEuPathDB; HostDB:ENSG00000115275; -.
DR   eggNOG; KOG2161; Eukaryota.
DR   GeneTree; ENSGT00390000017452; -.
DR   HOGENOM; CLU_007380_1_0_1; -.
DR   InParanoid; Q13724; -.
DR   OMA; FNWYNTT; -.
DR   OrthoDB; 1571at2759; -.
DR   PhylomeDB; Q13724; -.
DR   TreeFam; TF300749; -.
DR   BioCyc; MetaCyc:HS03863-MONOMER; -.
DR   PathwayCommons; Q13724; -.
DR   Reactome; R-HSA-4793954; Defective MOGS causes CDG-2b.
DR   Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-HSA-9683686; Maturation of spike protein.
DR   Reactome; R-HSA-9694548; Maturation of spike protein.
DR   SignaLink; Q13724; -.
DR   UniPathway; UPA00280; -.
DR   BioGRID-ORCS; 7841; 69 hits in 1168 CRISPR screens.
DR   ChiTaRS; MOGS; human.
DR   GeneWiki; GCS1; -.
DR   GenomeRNAi; 7841; -.
DR   Pharos; Q13724; Tbio.
DR   PRO; PR:Q13724; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q13724; Protein.
DR   Bgee; ENSG00000115275; Expressed in body of pancreas and 123 other cell types or tissues.
DR   ExpressionAtlas; Q13724; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004573; F:Glc3Man9GlcNAc2 oligosaccharide glucosidase activity; IBA:GO_Central.
DR   GO; GO:0015926; F:glucosidase activity; TAS:ProtInc.
DR   GO; GO:0009311; P:oligosaccharide metabolic process; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; TAS:Reactome.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.110; Glycosyl hydrolase family 63, N-terminal domain; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR031335; Glyco_hydro_63_C.
DR   InterPro; IPR031631; Glyco_hydro_63N.
DR   InterPro; IPR038518; Glyco_hydro_63N_sf.
DR   InterPro; IPR004888; Glycoside_hydrolase_63.
DR   PANTHER; PTHR10412; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   PANTHER; PTHR10412:SF11; MANNOSYL-OLIGOSACCHARIDE GLUCOSIDASE; 1.
DR   Pfam; PF03200; Glyco_hydro_63; 1.
DR   Pfam; PF16923; Glyco_hydro_63N; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q13724; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW   Glycosidase; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..837
FT                   /note="Mannosyl-oligosaccharide glucosidase"
FT                   /id="PRO_0000057710"
FT   TOPO_DOM        1..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..837
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..137
FT                   /note="Required for endoplasmic reticulum targeting"
FT                   /evidence="ECO:0000250"
FT   MOTIF           3..9
FT                   /note="Endoplasmic reticulum targeting"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        583
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q80UM7"
FT   ACT_SITE        807
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q80UM7"
FT   CARBOHYD        657
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7635146"
FT   VAR_SEQ         1..106
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046921"
FT   VARIANT         222
FT                   /note="G -> R (in dbSNP:rs3213671)"
FT                   /id="VAR_049233"
FT   VARIANT         236
FT                   /note="E -> Q (in dbSNP:rs1063587)"
FT                   /evidence="ECO:0000269|PubMed:7635146"
FT                   /id="VAR_019361"
FT   VARIANT         239
FT                   /note="D -> N (in dbSNP:rs1063588)"
FT                   /evidence="ECO:0000269|PubMed:7635146"
FT                   /id="VAR_019362"
FT   VARIANT         293
FT                   /note="P -> S (in dbSNP:rs2268416)"
FT                   /evidence="ECO:0000269|PubMed:7635146"
FT                   /id="VAR_049234"
FT   VARIANT         486
FT                   /note="R -> T (in CDGIIb; loss of activity;
FT                   dbSNP:rs121909291)"
FT                   /evidence="ECO:0000269|PubMed:10788335,
FT                   ECO:0000269|PubMed:12145188"
FT                   /id="VAR_018966"
FT   VARIANT         495
FT                   /note="R -> P (in dbSNP:rs34075781)"
FT                   /id="VAR_049235"
FT   VARIANT         652
FT                   /note="F -> L (in CDGIIb; loss of activity;
FT                   dbSNP:rs121909292)"
FT                   /evidence="ECO:0000269|PubMed:10788335,
FT                   ECO:0000269|PubMed:12145188"
FT                   /id="VAR_018967"
FT   VARIANT         785
FT                   /note="G -> S (in dbSNP:rs35533773)"
FT                   /id="VAR_049236"
FT   CONFLICT        330
FT                   /note="I -> F (in Ref. 1; CAA60683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="V -> A (in Ref. 1; CAA60683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        605
FT                   /note="A -> G (in Ref. 1; CAA60683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        818
FT                   /note="Missing (in Ref. 1; CAA60683)"
FT                   /evidence="ECO:0000305"
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
//