Neutral alpha-glucosidase AB

Details

Name
Neutral alpha-glucosidase AB
Synonyms
  • 3.2.1.84
  • Alpha-glucosidase 2
  • G2AN
  • Glucosidase II subunit alpha
  • KIAA0088
Gene Name
GANAB
Organism
Humans
Amino acid sequence
>lcl|BSEQ0008549|Neutral alpha-glucosidase AB
MAAVAAVAARRRRSWASLVLAFLGVCLGITLAVDRSNFKTCEESSFCKRQRSIRPGLSPY
RALLDSLQLGPDSLTVHLIHEVTKVLLVLELQGLQKNMTRFRIDELEPRRPRYRVPDVLV
ADPPIARLSVSGRDENSVELTMAEGPYKIILTARPFRLDLLEDRSLLLSVNARGLLEFEH
QRAPRVSQGSKDPAEGDGAQPEETPRDGDKPEETQGKAEKDEPGAWEETFKTHSDSKPYG
PMSVGLDFSLPGMEHVYGIPEHADNLRLKVTEGGEPYRLYNLDVFQYELYNPMALYGSVP
VLLAHNPHRDLGIFWLNAAETWVDISSNTAGKTLFGKMMDYLQGSGETPQTDVRWMSETG
IIDVFLLLGPSISDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHN
LPCDVIWLDIEHADGKRYFTWDPSRFPQPRTMLERLASKRRKLVAIVDPHIKVDSGYRVH
EELRNLGLYVKTRDGSDYEGWCWPGSAGYPDFTNPTMRAWWANMFSYDNYEGSAPNLFVW
NDMNEPSVFNGPEVTMLKDAQHYGGWEHRDVHNIYGLYVHMATADGLRQRSGGMERPFVL
ARAFFAGSQRFGAVWTGDNTAEWDHLKISIPMCLSLGLVGLSFCGADVGGFFKNPEPELL
VRWYQMGAYQPFFRAHAHLDTGRREPWLLPSQHNDIIRDALGQRYSLLPFWYTLLYQAHR
EGIPVMRPLWVQYPQDVTTFNIDDQYLLGDALLVHPVSDSGAHGVQVYLPGQGEVWYDIQ
SYQKHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSECMKDDPITLFVALSPQGTA
QGELFLDDGHTFNYQTRQEFLLRRFSFSGNTLVSSSADPEGHFETPIWIERVVIIGAGKP
AAVVLQTKGSPESRLSFQHDPETSVLVLRKPGINVASDWSIHLR
Number of residues
944
Molecular Weight
106873.125
Theoretical pI
Not Available
GO Classification
Functions
carbohydrate binding / glucan 1,3-alpha-glucosidase activity / poly(A) RNA binding
Processes
cellular protein metabolic process / post-translational protein modification / protein folding / protein N-linked glycosylation via asparagine
Components
endoplasmic reticulum lumen / extracellular exosome / Golgi apparatus / melanosome / membrane
General Function
Poly(a) rna binding
Specific Function
Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Endoplasmic reticulum
Gene sequence
>lcl|BSEQ0019619|Neutral alpha-glucosidase AB (GANAB)
ATGGCGGCGGTAGCGGCAGTGGCGGCGCGTAGGAGGCGGCTTTCTGTCTCTGGTCGTGAT
GAGAACAGTGTGGAGTTAACCATGGCTGAGGGACCCTACAAGATCATCTTGACAGCACGG
CCATTCCGCCTTGACCTACTAGAGGACCGAAGTCTTTTGCTTAGTGTCAATGCCCGAGGA
CTCTTGGAGTTTGAGCATCAGAGGGCCCCTAGGGTCTCTTTCTCGGATAAGGTTAATCTC
ACGCTTGGTAGCATATGGGATAAGATCAAGAACCTTTTCTCTAGGCAAGGATCAAAAGAC
CCAGCTGAGGGCGATGGGGCCCAGCCTGAGGAAACACCCAGGGATGGCGACAAGCCAGAG
GAGACTCAGGGGAAGGCAGAGAAAGATGAGCCAGGAGCCTGGGAGGAGACATTCAAAACT
CACTCTGACAGCAAGCCGTATGGCCCCATGTCTGTGGGTTTGGACTTCTCTCTGCCAGGC
ATGGAGCATGTCTATGGGATCCCTGAGCATGCAGACAACCTGAGGCTGAAGGTCACTGAG
GGTGGGGAGCCATATCGCCTCTACAATTTGGATGTGTTCCAGTATGAGCTGTACAACCCA
ATGGCCTTGTATGGGTCTGTGCCTGTGCTCCTGGCACACAACCCTCATCGCGACTTGGGC
ATCTTCTGGCTCAATGCTGCAGAGACCTGGGTTGATATATCTTCCAACACTGCCGGGAAG
ACCCTGTTTGGGAAGATGATGGACTACCTGCAGGGCTCTGGGGAGACCCCACAGACAGAT
GTTCGCTGGATGTCAGAGACTGGCATCATTGACGTCTTCCTGCTGCTGGGGCCCTCCATC
TCTGATGTTTTCCGGCAATATGCTAGTCTCACAGGAACCCAGGCGTTGCCCCCACTCTTC
TCCCTCGGCTACCACCAGAGCCGTTGGAACTACCGGGACGAGGCTGATGTGCTGGAAGTG
GATCAGGGCTTTGATGATCACAACCTGCCCTGTGATGTCATCTGGCTAGACATTGAACAT
GCTGATGGCAAGCGGTATTTCACCTGGGACCCCAGTCGCTTCCCTCAGCCCCGCACCATG
CTTGAGCGCTTGGCTTCTAAGAGGCGGAAGCTGGTGGCCATCGTAGACCCCCACATCAAG
GTGGACTCCGGCTACCGAGTTCACGAGGAGCTGCGGAACCTGGGGCTGTATGTTAAAACC
CGGGATGGCTCTGACTATGAGGGCTGGTGCTGGCCAGGCTCAGCTGGTTACCCTGACTTC
ACTAATCCCACGATGAGGGCCTGGTGGGCTAACATGTTCAGCTATGACAATTATGAGGGC
TCAGCTCCCAACCTCTTTGTCTGGAATGACATGAACGAACCATCTGTGTTCAATGGTCCT
GAGGTCACCATGCTCAAGGATGCCCAGCATTATGGGGGCTGGGAGCACCGGGATGTGCAT
AACATCTATGGCCTTTATGTGCACATGGCGACTGCTGATGGGCTGAGACAGCGCTCTGGG
GGCATGGAACGCCCCTTTGTCCTGGCCAGGGCCTTCTTCGCTGGCTCCCAGCGCTTTGGA
GCCGTGTGGACAGGGGACAACACTGCCGAGTGGGACCATTTGAAGATCTCTATTCCTATG
TGTCTCAGCTTGGGGCTGGTGGGACTTTCCTTCTGTGGGGCGGATGTGGGTGGCTTCTTC
AAAAACCCAGAGCCAGAGCTGCTTGTGCGCTGGTACCAGATGGGTGCTTACCAGCCATTC
TTCCGGGCACATGCCCACTTGGACACTGGGCGACGAGAGCCATGGCTGTTACCATCTCAG
CACAATGATATAATCCGAGATGCCTTGGGCCAGCGATATTCTTTGCTGCCCTTCTGGTAC
ACCCTCTTATATCAGGCCCATCGGGAAGGCATTCCTGTCATGAGGCCCCTGTGGGTGCAG
TACCCTCAGGATGTGACTACCTTCAATATAGATGATCAGTACTTGCTTGGGGATGCGTTG
CTGGTTCACCCTGTATCAGACTCTGGAGCCCATGGTGTCCAGGTCTATCTGCCTGGCCAA
GGGGAGGTGTGGTATGACATTCAAAGCTACCAGAAGCATCATGGTCCCCAGACCCTGTAC
CTGCCTGTAACTCTAAGCAGTATCCCTGTGTTCCAGCGTGGAGGGACAATCGTGCCTCGA
TGGATGCGAGTGCGGCGGTCTTCAGAATGTATGAAGGATGACCCCATCACTCTCTTTGTT
GCACTTAGCCCTCAGGGTACAGCTCAAGGAGAGCTCTTTCTGGATGATGGGCACACGTTC
AACTATCAGACTCGCCAAGAGTTCCTGCTGCGTCGATTCTCATTCTCTGGCAACACCCTT
GTCTCCAGCTCAGCAGACCCTGAAGGACACTTTGAGACACCAATCTGGATTGAGCGGGTG
GTGATAATAGGGGCTGGAAAGCCAGCAGCTGTGGTACTCCAGACAAAAGGATCTCCAGAA
AGCCGCCTGTCCTTCCAGCATGACCCTGAGACCTCTGTGTTGGTCCTGCGCAAGCCTGGC
ATCAATGTGGCATCTGATTGGAGTATTCACCTGCGATAA
Chromosome Location
11
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ14697
UniProtKB Entry NameGANAB_HUMAN
HGNC IDHGNC:4138
General References
  1. Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY: The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology. 2000 Aug;10(8):815-27. [Article]
  2. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [Article]
  3. Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Martiniuk F, Ellenbogen A, Hirschhorn R: Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies. J Biol Chem. 1985 Jan 25;260(2):1238-42. [Article]
  6. Trombetta ES, Simons JF, Helenius A: Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem. 1996 Nov 1;271(44):27509-16. [Article]
  7. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [Article]
  8. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  9. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  10. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00491MiglitolapprovedyesantagonistDetails