MAN2A1

Alpha-mannosidase 2 is an enzyme that in humans is encoded by the MAN2A1 gene.

MAN2A1
Identifiers
Aliases	MAN2A1, AMan II, GOLIM7, MANA2, MANII, mannosidase alpha class 2A member 1
External IDs	OMIM: 154582; MGI: 104669; HomoloGene: 1777; GeneCards: MAN2A1; OMA:MAN2A1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q21.3 Start 109,689,927 bp End 109,869,625 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17|17 E1.1 Start 64,907,731 bp End 65,062,105 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus callosum Achilles tendon jejunal mucosa inferior ganglion of vagus nerve stromal cell of endometrium retinal pigment epithelium endothelial cell C1 segment mucosa of sigmoid colon duodenum Top expressed in stroma of bone marrow lacrimal gland decidua seminal vesicula gastrula vestibular membrane of cochlear duct efferent ductule left lobe of liver Paneth cell dermis More reference expression data BioGPS n/a
Gene ontology Molecular function mannosidase activity hydrolase activity, hydrolyzing N-glycosyl compounds hydrolase activity, acting on glycosyl bonds metal ion binding catalytic activity mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity hydrolase activity carbohydrate binding alpha-mannosidase activity Cellular component integral component of membrane Golgi apparatus membrane Golgi membrane cis-Golgi network extracellular exosome extracellular space Golgi medial cisterna Biological process N-glycan processing mitochondrion organization vacuole organization in utero embryonic development protein deglycosylation respiratory gaseous exchange by respiratory system positive regulation of neurogenesis retina morphogenesis in camera-type eye protein glycosylation liver development lung alveolus development metabolism mannose metabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4124 17158 Ensembl ENSG00000112893 ENSMUSG00000024085 UniProt Q16706 P27046 RefSeq (mRNA) NM_002372 NM_008549 RefSeq (protein) NP_002363 NP_032575 Location (UCSC) Chr 5: 109.69 – 109.87 Mb Chr 17: 64.91 – 65.06 Mb PubMed search
Wikidata
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Function

This gene encodes a protein which is a member of family 38 of the glycosyl hydrolases. The protein is located in the Golgi apparatus and catalyzes the final hydrolytic step in the asparagine-linked oligosaccharide (N-linked glycosylation) maturation pathway. Mutations in the mouse homolog of this gene have been shown to cause a systemic autoimmune disease similar to human systemic lupus erythematosus.

Further reading

• 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.
• 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.
• Moremen KW, Touster O, Robbins PW (Sep 1991). "Novel purification of the catalytic domain of Golgi alpha-mannosidase II. Characterization and comparison with the intact enzyme". The Journal of Biological Chemistry. 266 (25): 16876–85. doi:10.1016/S0021-9258(18)55384-9. PMID 1885615.
• 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.
• 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.
• 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.
• 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.
• Moremen KW, Touster O (Jun 1985). "Biosynthesis and modification of Golgi mannosidase II in HeLa and 3T3 cells". The Journal of Biological Chemistry. 260 (11): 6654–62. doi:10.1016/S0021-9258(18)88830-5. PMID 3922977.
• Fenouillet E, Jones I, Powell B, Schmitt D, Kieny MP, Gluckman JC (Jan 1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". Journal of Virology. 67 (1): 150–60. doi:10.1128/jvi.67.1.150-160.1993. PMC 237347. PMID 8093218.
• Yeh JC, Seals JR, Murphy CI, van Halbeek H, Cummings RD (Oct 1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
• Velasco A, Hendricks L, Moremen KW, Tulsiani DR, Touster O, Farquhar MG (Jul 1993). "Cell type-dependent variations in the subcellular distribution of alpha-mannosidase I and II". The Journal of Cell Biology. 122 (1): 39–51. doi:10.1083/jcb.122.1.39. PMC 2119607. PMID 8314846.
• Misago M, Liao YF, Kudo S, Eto S, Mattei MG, Moremen KW, Fukuda MN (Dec 1995). "Molecular cloning and expression of cDNAs encoding human alpha-mannosidase II and a previously unrecognized alpha-mannosidase IIx isozyme". Proceedings of the National Academy of Sciences of the United States of America. 92 (25): 11766–70. Bibcode:1995PNAS...9211766M. doi:10.1073/pnas.92.25.11766. PMC 40483. PMID 8524845.
• Bolmstedt A, Sjölander S, Hansen JE, Akerblom L, Hemming A, Hu SL, Morein B, Olofsson S (Jul 1996). "Influence of N-linked glycans in V4-V5 region of human immunodeficiency virus type 1 glycoprotein gp160 on induction of a virus-neutralizing humoral response". Journal of Acquired Immune Deficiency Syndromes and Human Retrovirology. 12 (3): 213–20. doi:10.1097/00042560-199607000-00001. PMID 8673525.
• Hu H, Shioda T, Moriya C, Xin X, Hasan MK, Miyake K, Shimada T, Nagai Y (Nov 1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". Journal of Virology. 70 (11): 7462–70. doi:10.1128/jvi.70.11.7462-7470.1996. PMC 190813. PMID 8892864.