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{{Infobox_gene}}
{{PBB_Controls
'''Neutral alpha-glucosidase C''' is an [[enzyme]] that in humans is encoded by the ''GANC'' [[gene]].<ref name="pmid6995030">{{cite journal | vauthors = Martiniuk F, Hirschhorn R, Smith M | title = Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15 | journal = Cytogenetics and Cell Genetics | volume = 27 | issue = 2-3 | pages = 168–75 | date = Oct 1980 | pmid = 6995030 | pmc =  | doi = 10.1159/000131478 }}</ref><ref name="pmid12370436">{{cite journal | vauthors = Hirschhorn R, Huie ML, Kasper JS | title = Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 21 | pages = 13642–6 | date = Oct 2002 | pmid = 12370436 | pmc = 129728 | doi = 10.1073/pnas.202383599 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GANC glucosidase, alpha; neutral C| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595| accessdate = }}</ref>
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Glucosidase, alpha; neutral C
| HGNCid = 4139
| Symbol = GANC
| AltSymbols =; MGC138256
| OMIM = 104180
| ECnumber = 
| Homologene = 25627
| MGIid = 
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0004558 |text = alpha-glucosidase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2595
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_937784
    | Hs_RefseqmRNA = NM_198141
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Glucosidase, alpha; neutral C''', also known as '''GANC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GANC glucosidase, alpha; neutral C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Glycoside hydrolase]] enzymes hydrolyse the [[glycosidic bond]] between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. This gene encodes a member of glycosyl hydrolases family 31. This enzyme hydrolyses terminal, non-reducing 1,4-linked alpha-D-glucose residues and releases alpha-D-glucose. This is a key enzyme in glycogen metabolism and its gene localizes to a chromosomal region (15q15) that is associated with susceptibility to diabetes.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Glycosyl hydrolase enzymes hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. This gene encodes a member of glycosyl hydrolases family 31. This enzyme hydrolyses terminal, non-reducing 1,4-linked alpha-D-glucose residues and releases alpha-D-glucose. This is a key enzyme in glycogen metabolism and its gene localizes to a chromosomal region (15q15) that is associated with susceptibility to diabetes.<ref name="entrez">{{cite web | title = Entrez Gene: GANC glucosidase, alpha; neutral C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2595| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
{{Clear}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Feizi T, Larkin M | title = AIDS and glycosylation | journal = Glycobiology | volume = 1 | issue = 1 | pages = 17–23 | date = Sep 1990 | pmid = 2136376 | doi = 10.1093/glycob/1.1.17 }}
| citations =
* {{cite journal | vauthors = Land A, Braakman I | title = Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum | journal = Biochimie | volume = 83 | issue = 8 | pages = 783–90 | date = Aug 2001 | pmid = 11530211 | doi = 10.1016/S0300-9084(01)01314-1 }}
*{{cite journal | author=Feizi T, Larkin M |title=AIDS and glycosylation. |journal=Glycobiology |volume=1 |issue= 1 |pages= 17-23 |year= 1992 |pmid= 2136376 |doi= }}
* {{cite journal | vauthors = Kamimura H, Ogata H, Takahara H | title = Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases | journal = Drug Metabolism and Disposition | volume = 20 | issue = 2 | pages = 309–15 | year = 1992 | pmid = 1352226 | doi =  }}
*{{cite journal | author=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. |journal=Biochimie |volume=83 |issue= 8 |pages= 783-90 |year= 2001 |pmid= 11530211 |doi= }}
* {{cite journal | vauthors = Fenouillet E, Gluckman JC | title = Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein | journal = The Journal of General Virology | volume = 72 | issue = 8 | pages = 1919–26 | date = Aug 1991 | pmid = 1678778 | doi = 10.1099/0022-1317-72-8-1919 }}
*{{cite journal | author=Kamimura H, Ogata H, Takahara H |title=Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases. |journal=Drug Metab. Dispos. |volume=20 |issue= 2 |pages= 309-15 |year= 1992 |pmid= 1352226 |doi=  }}
* {{cite journal | vauthors = Ratner L, vander Heyden N, Dedera D | title = Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity | journal = Virology | volume = 181 | issue = 1 | pages = 180–92 | date = Mar 1991 | pmid = 1704656 | doi = 10.1016/0042-6822(91)90483-R }}
*{{cite journal | author=Fenouillet E, Gluckman JC |title=Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. |journal=J. Gen. Virol. |volume=72 ( Pt 8) |issue= |pages= 1919-26 |year= 1991 |pmid= 1678778 |doi= }}
* {{cite journal | vauthors = Dedera DA, Gu RL, Ratner L | title = Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function | journal = Virology | volume = 187 | issue = 1 | pages = 377–82 | date = Mar 1992 | pmid = 1736542 | doi = 10.1016/0042-6822(92)90331-I }}
*{{cite journal | author=Ratner L, vander Heyden N, Dedera D |title=Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity. |journal=Virology |volume=181 |issue= 1 |pages= 180-92 |year= 1991 |pmid= 1704656 |doi= }}
* {{cite journal | vauthors = Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E | title = Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding | journal = Genetic Analysis, Techniques and Applications | volume = 7 | issue = 6 | pages = 160–71 | date = Oct 1990 | pmid = 2076345 | doi = 10.1016/0735-0651(90)90030-J }}
*{{cite journal | author=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. |journal=Virology |volume=187 |issue= 1 |pages= 377-82 |year= 1992 |pmid= 1736542 |doi= }}
* {{cite journal | vauthors = Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG | title = Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 | journal = AIDS Research and Human Retroviruses | volume = 6 | issue = 3 | pages = 371–80 | date = Mar 1990 | pmid = 2187500 | doi = 10.1089/aid.1990.6.371 }}
*{{cite journal | author=Murphy CI, Lennick M, Lehar SM, ''et al.'' |title=Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding. |journal=Genet. Anal. Tech. Appl. |volume=7 |issue= 6 |pages= 160-71 |year= 1991 |pmid= 2076345 |doi= }}
* {{cite journal | vauthors = Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T | title = Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins | journal = Japanese Journal of Medical Science & Biology | volume = 43 | issue = 3 | pages = 75–87 | date = Jun 1990 | pmid = 2283726 | doi = 10.7883/yoken1952.43.75 }}
*{{cite journal | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi= }}
* {{cite journal | vauthors = Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ | title = Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells | journal = The Journal of Biological Chemistry | volume = 265 | issue = 18 | pages = 10373–82 | date = Jun 1990 | pmid = 2355006 | doi =  }}
*{{cite journal | author=Shimizu H, Tsuchie H, Honma H, ''et al.'' |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins. |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75-87 |year= 1991 |pmid= 2283726 |doi= }}
* {{cite journal | vauthors = Pal R, Hoke GM, Sarngadharan MG | title = Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 9 | pages = 3384–8 | date = May 1989 | pmid = 2541446 | pmc = 287137 | doi = 10.1073/pnas.86.9.3384 }}
*{{cite journal | author=Leonard CK, Spellman MW, Riddle L, ''et al.'' |title=Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373-82 |year= 1990 |pmid= 2355006 |doi=  }}
* {{cite journal | vauthors = Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP | title = Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport | journal = Journal of Virology | volume = 63 | issue = 6 | pages = 2452–6 | date = Jun 1989 | pmid = 2542563 | pmc = 250699 | doi =  }}
*{{cite journal | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi= }}
* {{cite journal | vauthors = Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M | title = Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein | journal = Journal of Acquired Immune Deficiency Syndromes | volume = 2 | issue = 2 | pages = 163–9 | year = 1989 | pmid = 2649653 | doi =  }}
*{{cite journal | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi=  }}
* {{cite journal | vauthors = Walker BD, Kowalski M, Goh WC, Kozarsky K, Krieger M, Rosen C, Rohrschneider L, Haseltine WA, Sodroski J | title = Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 22 | pages = 8120–4 | date = Nov 1987 | pmid = 2825177 | pmc = 299490 | doi = 10.1073/pnas.84.22.8120 }}
*{{cite journal | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi=  }}
* {{cite journal | vauthors = Robinson WE, Montefiori DC, Mitchell WM | title = Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis | journal = AIDS Research and Human Retroviruses | volume = 3 | issue = 3 | pages = 265–82 | year = 1988 | pmid = 2829950 | doi = 10.1089/aid.1987.3.265 }}
*{{cite journal | author=Walker BD, Kowalski M, Goh WC, ''et al.'' |title=Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 8120-4 |year= 1987 |pmid= 2825177 |doi= }}
* {{cite journal | vauthors = Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG, Miedema F, Ploegh HL | title = Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase | journal = Nature | volume = 330 | issue = 6143 | pages = 74–7 | year = 1987 | pmid = 2959866 | doi = 10.1038/330074a0 }}
*{{cite journal | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi= }}
* {{cite journal | vauthors = Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L | title = Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins | journal = Biochemical and Biophysical Research Communications | volume = 141 | issue = 1 | pages = 33–8 | date = Nov 1986 | pmid = 3099781 | doi = 10.1016/S0006-291X(86)80330-8 }}
*{{cite journal | author=Gruters RA, Neefjes JJ, Tersmette M, ''et al.'' |title=Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase. |journal=Nature |volume=330 |issue= 6143 |pages= 74-7 |year= 1987 |pmid= 2959866 |doi= 10.1038/330074a0 }}
* {{cite journal | vauthors = Usuki F, Ishiura S, Nonaka I, Sugita H | title = alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles | journal = Muscle & Nerve | volume = 11 | issue = 4 | pages = 365–71 | date = Apr 1988 | pmid = 3135493 | doi = 10.1002/mus.880110413 }}
*{{cite journal | author=Blough HA, Pauwels R, De Clercq E, ''et al.'' |title=Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins. |journal=Biochem. Biophys. Res. Commun. |volume=141 |issue= 1 |pages= 33-8 |year= 1987 |pmid= 3099781 |doi= }}
* {{cite journal | vauthors = Montefiori DC, Robinson WE, Mitchell WM | title = Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 23 | pages = 9248–52 | date = Dec 1988 | pmid = 3264072 | pmc = 282716 | doi = 10.1073/pnas.85.23.9248 }}
*{{cite journal | author=Usuki F, Ishiura S, Nonaka I, Sugita H |title=alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles. |journal=Muscle Nerve |volume=11 |issue= 4 |pages= 365-71 |year= 1988 |pmid= 3135493 |doi= 10.1002/mus.880110413 }}
*{{cite journal | author=Montefiori DC, Robinson WE, Mitchell WM |title=Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9248-52 |year= 1988 |pmid= 3264072 |doi= }}
}}
{{refend}}
{{refend}}
{{Sugar hydrolases}}


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{{WikiDoc Sources}}

Latest revision as of 08:38, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.[1][2][3]

Function

Glycoside hydrolase enzymes hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. This gene encodes a member of glycosyl hydrolases family 31. This enzyme hydrolyses terminal, non-reducing 1,4-linked alpha-D-glucose residues and releases alpha-D-glucose. This is a key enzyme in glycogen metabolism and its gene localizes to a chromosomal region (15q15) that is associated with susceptibility to diabetes.[3]

References

  1. ↑ Martiniuk F, Hirschhorn R, Smith M (Oct 1980). "Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15". Cytogenetics and Cell Genetics. 27 (2–3): 168–75. doi:10.1159/000131478. PMID 6995030.
  2. ↑ Hirschhorn R, Huie ML, Kasper JS (Oct 2002). "Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31". Proceedings of the National Academy of Sciences of the United States of America. 99 (21): 13642–6. doi:10.1073/pnas.202383599. PMC 129728. PMID 12370436.
  3. ↑ 3.0 3.1 "Entrez Gene: GANC glucosidase, alpha; neutral C".

Further reading


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