GANC_HUMAN
ID GANC_HUMAN Reviewed; 914 AA.
AC Q8TET4; Q52LQ4; Q8IWZ0; Q8IZM4; Q8IZM5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Neutral alpha-glucosidase C;
DE EC=3.2.1.20;
GN Name=GANC;
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], VARIANTS VAL-11; ARG-44; MET-153; GLU-443;
RP SER-845 AND ARG-848, AND FUNCTION.
RC TISSUE=Lymphoid tissue;
RX PubMed=12370436; DOI=10.1073/pnas.202383599;
RA Hirschhorn R., Huie M.L., Kasper J.S.;
RT "Computer assisted cloning of human neutral alpha glucosidase C (GANC): a
RT new paralog in the glycosyl hydrolase gene family 31.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13642-13646(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-11 AND ARG-44.
RC TISSUE=Spleen;
RA Ohara O., Nagase T., Kikuno R., Okumura K.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-11 AND ARG-44.
RC TISSUE=Colon, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 146-914.
RC TISSUE=Erythroid cell;
RA Ben-Asher E.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has alpha-glucosidase activity.
CC {ECO:0000269|PubMed:12370436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84863.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF545044; AAN74755.1; -; mRNA.
DR EMBL; AF545045; AAN74756.1; -; mRNA.
DR EMBL; AF545046; AAN74757.1; -; mRNA.
DR EMBL; AK074037; BAB84863.1; ALT_INIT; mRNA.
DR EMBL; AC012651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059406; AAH59406.1; -; mRNA.
DR EMBL; BC093833; AAH93833.1; -; mRNA.
DR EMBL; AF525397; AAO14993.1; -; mRNA.
DR CCDS; CCDS10084.1; -.
DR RefSeq; NP_937784.2; NM_198141.2.
DR AlphaFoldDB; Q8TET4; -.
DR SMR; Q8TET4; -.
DR BioGRID; 108866; 3.
DR IntAct; Q8TET4; 2.
DR STRING; 9606.ENSP00000326227; -.
DR BindingDB; Q8TET4; -.
DR ChEMBL; CHEMBL2520; -.
DR DrugBank; DB00491; Miglitol.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR iPTMnet; Q8TET4; -.
DR PhosphoSitePlus; Q8TET4; -.
DR BioMuta; GANC; -.
DR DMDM; 296439340; -.
DR EPD; Q8TET4; -.
DR MassIVE; Q8TET4; -.
DR MaxQB; Q8TET4; -.
DR PaxDb; Q8TET4; -.
DR PeptideAtlas; Q8TET4; -.
DR PRIDE; Q8TET4; -.
DR ProteomicsDB; 74496; -.
DR Antibodypedia; 1713; 112 antibodies from 21 providers.
DR DNASU; 2595; -.
DR Ensembl; ENST00000318010.13; ENSP00000326227.8; ENSG00000214013.10.
DR GeneID; 2595; -.
DR KEGG; hsa:2595; -.
DR MANE-Select; ENST00000318010.13; ENSP00000326227.8; NM_198141.3; NP_937784.2.
DR UCSC; uc001zpi.4; human.
DR CTD; 2595; -.
DR DisGeNET; 2595; -.
DR GeneCards; GANC; -.
DR HGNC; HGNC:4139; GANC.
DR HPA; ENSG00000214013; Low tissue specificity.
DR MIM; 104180; gene.
DR neXtProt; NX_Q8TET4; -.
DR OpenTargets; ENSG00000214013; -.
DR PharmGKB; PA28552; -.
DR VEuPathDB; HostDB:ENSG00000214013; -.
DR eggNOG; KOG1066; Eukaryota.
DR GeneTree; ENSGT00940000159230; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; Q8TET4; -.
DR OMA; GRSTGWM; -.
DR OrthoDB; 100626at2759; -.
DR PhylomeDB; Q8TET4; -.
DR TreeFam; TF300337; -.
DR PathwayCommons; Q8TET4; -.
DR SignaLink; Q8TET4; -.
DR BioGRID-ORCS; 2595; 7 hits in 1075 CRISPR screens.
DR ChiTaRS; GANC; human.
DR GeneWiki; GANC; -.
DR GenomeRNAi; 2595; -.
DR Pharos; Q8TET4; Tchem.
DR PRO; PR:Q8TET4; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8TET4; protein.
DR Bgee; ENSG00000214013; Expressed in sural nerve and 127 other tissues.
DR ExpressionAtlas; Q8TET4; baseline and differential.
DR Genevisible; Q8TET4; HS.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IBA:GO_Central.
DR GO; GO:0090599; F:alpha-glucosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 2: Evidence at transcript level;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..914
FT /note="Neutral alpha-glucosidase C"
FT /id="PRO_0000185364"
FT ACT_SITE 511
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 514
FT /evidence="ECO:0000250"
FT ACT_SITE 587
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT VARIANT 11
FT /note="L -> V (in dbSNP:rs8043515)"
FT /evidence="ECO:0000269|PubMed:12370436,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_018984"
FT VARIANT 44
FT /note="Q -> R (in dbSNP:rs8024732)"
FT /evidence="ECO:0000269|PubMed:12370436,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_018985"
FT VARIANT 153
FT /note="I -> M (in dbSNP:rs75876980)"
FT /evidence="ECO:0000269|PubMed:12370436"
FT /id="VAR_018986"
FT VARIANT 166
FT /note="I -> V (in dbSNP:rs16973015)"
FT /id="VAR_056237"
FT VARIANT 443
FT /note="D -> E (in dbSNP:rs2578652)"
FT /evidence="ECO:0000269|PubMed:12370436"
FT /id="VAR_018987"
FT VARIANT 845
FT /note="F -> S (in dbSNP:rs7181742)"
FT /evidence="ECO:0000269|PubMed:12370436"
FT /id="VAR_018988"
FT VARIANT 848
FT /note="Q -> R (in dbSNP:rs7180279)"
FT /evidence="ECO:0000269|PubMed:12370436"
FT /id="VAR_018989"
FT CONFLICT 180
FT /note="T -> A (in Ref. 5; AAO14993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 104334 MW; 7AA10E180DA7FDC2 CRC64;
MEAAVKEEIS LEDEAVDKNI FRDCNKIAFY RRQKQWLSKK STYQALLDSV TTDEDSTRFQ
IINEASKVPL LAEIYGIEGN IFRLKINEET PLKPRFEVPD VLTSKPSTVR LISCSGDTGS
LILADGKGDL KCHITANPFK VDLVSEEEVV ISINSLGQLY FEHLQILHKQ RAAKENEEET
SVDTSQENQE DLGLWEEKFG KFVDIKANGP SSIGLDFSLH GFEHLYGIPQ HAESHQLKNT
GDGDAYRLYN LDVYGYQIYD KMGIYGSVPY LLAHKLGRTI GIFWLNASET LVEINTEPAV
EYTLTQMGPV AAKQKVRSRT HVHWMSESGI IDVFLLTGPT PSDVFKQYSH LTGTQAMPPL
FSLGYHQCRW NYEDEQDVKA VDAGFDEHDI PYDAMWLDIE HTEGKRYFTW DKNRFPNPKR
MQELLRSKKR KLVVISDPHI KIDPDYSVYV KAKDQGFFVK NQEGEDFEGV CWPGLSSYLD
FTNPKVREWY SSLFAFPVYQ GSTDILFLWN DMNEPSVFRG PEQTMQKNAI HHGNWEHREL
HNIYGFYHQM ATAEGLIKRS KGKERPFVLT RSFFAGSQKY GAVWTGDNTA EWSNLKISIP
MLLTLSITGI SFCGADIGGF IGNPETELLV RWYQAGAYQP FFRGHATMNT KRREPWLFGE
EHTRLIREAI RERYGLLPYW YSLFYHAHVA SQPVMRPLWV EFPDELKTFD MEDEYMLGSA
LLVHPVTEPK ATTVDVFLPG SNEVWYDYKT FAHWEGGCTV KIPVALDTIP VFQRGGSVIP
IKTTVGKSTG WMTESSYGLR VALSTKGSSV GELYLDDGHS FQYLHQKQFL HRKFSFCSSV
LINSFADQRG HYPSKCVVEK ILVLGFRKEP SSVTTHSSDG KDQPVAFTYC AKTSILSLEK
LSLNIATDWE VRII
