GANC

Identifiers

GANC, glucosidase alpha, neutral C

External IDs

OMIM: 104180 MGI: 1923301 HomoloGene: 25627 GeneCards: GANC

Gene location (Human)

Chr.	Chromosome 15 (human)^[1]

Band	15q15.1	Start	42,273,233 bp^[1]
Band	15q15.1	End	42,356,935 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2\|2 E5	Start	120,234,377 bp^[2]
Band	2\|2 E5	End	120,292,181 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

sural nerve

monocyte

right lung

bone marrow cells

Achilles tendon

rectum

upper lobe of left lung

right coronary artery

smooth muscle tissue

ascending aorta

Top expressed in

spermatocyte

secondary oocyte

spermatid

brown adipose tissue

skeletal muscle tissue

superior frontal gyrus

proximal tubule

temporal muscle

thymus

duodenum

More reference expression data

BioGPS

n/a

Orthologs

Species

Human

Mouse

Entrez


2595


76051

Ensembl


ENSG00000214013


ENSMUSG00000062646

UniProt


Q8TET4


Q8BVW0

RefSeq (mRNA)


NM_198141 NM_001301409 NM_001301410


NM_172672

RefSeq (protein)


NP_001288338 NP_001288339 NP_937784


NP_766260

Location (UCSC)

Chr 15: 42.27 – 42.36 Mb

Chr 2: 120.23 – 120.29 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.^[5]^[6]^[7]

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.^[7]

References

Feizi T, Larkin M (Sep 1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID 2136376.
Land A, Braakman I (Aug 2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl:1874/5091. PMID 11530211. S2CID 13576808.
Kamimura H, Ogata H, Takahara H (1992). "Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases". Drug Metabolism and Disposition. 20 (2): 309–15. PMID 1352226.
Fenouillet E, Gluckman JC (Aug 1991). "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". The Journal of General Virology. 72 (8): 1919–26. doi:10.1099/0022-1317-72-8-1919. PMID 1678778.
Ratner L, vander Heyden N, Dedera D (Mar 1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology. 181 (1): 180–92. doi:10.1016/0042-6822(91)90483-R. PMID 1704656.
Dedera DA, Gu RL, Ratner L (Mar 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology. 187 (1): 377–82. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.
Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E (Oct 1990). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genetic Analysis, Techniques and Applications. 7 (6): 160–71. doi:10.1016/0735-0651(90)90030-J. PMID 2076345.
Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (Mar 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T (Jun 1990). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Japanese Journal of Medical Science & Biology. 43 (3): 75–87. doi:10.7883/yoken1952.43.75. PMID 2283726.
Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ (Jun 1990). "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". The Journal of Biological Chemistry. 265 (18): 10373–82. doi:10.1016/S0021-9258(18)86956-3. PMID 2355006.
Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 86 (9): 3384–8. Bibcode:1989PNAS...86.3384P. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (Jun 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452–6. doi:10.1128/jvi.63.6.2452-2456.1989. PMC 250699. PMID 2542563.
Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes. 2 (2): 163–9. PMID 2649653.
Walker BD, Kowalski M, Goh WC, Kozarsky K, Krieger M, Rosen C, Rohrschneider L, Haseltine WA, Sodroski J (Nov 1987). "Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine". Proceedings of the National Academy of Sciences of the United States of America. 84 (22): 8120–4. Bibcode:1987PNAS...84.8120W. doi:10.1073/pnas.84.22.8120. PMC 299490. PMID 2825177.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Research and Human Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG, Miedema F, Ploegh HL (1987). "Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase". Nature. 330 (6143): 74–7. Bibcode:1987Natur.330...74G. doi:10.1038/330074a0. PMID 2959866. S2CID 4270139.
Blough HA, Pauwels R, De Clercq E, Cogniaux J, Sprecher-Goldberger S, Thiry L (Nov 1986). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochemical and Biophysical Research Communications. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
Usuki F, Ishiura S, Nonaka I, Sugita H (Apr 1988). "alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles". Muscle & Nerve. 11 (4): 365–71. doi:10.1002/mus.880110413. PMID 3135493. S2CID 43090032.
Montefiori DC, Robinson WE, Mitchell WM (Dec 1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 85 (23): 9248–52. Bibcode:1988PNAS...85.9248M. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase
Glucosidases	Cellulase Alpha-glucosidase Acid Neutral AB Neutral C Beta-glucosidase cytosolic Debranching enzyme
Other	Amylase Alpha-amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha-Mannosidase Glucuronidase Klotho Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha-N-acetylgalactosaminidase NAGA Alpha-N-acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

Function

References

Further reading