ID   GANC_MOUSE              Reviewed;         898 AA.
AC   Q8BVW0; Q8BH03;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Neutral alpha-glucosidase C;
DE            EC=3.2.1.20;
GN   Name=Ganc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Diencephalon, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Has alpha-glucosidase activity. {ECO:0000250}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BVW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BVW0-2; Sequence=VSP_010619, VSP_010620, VSP_010621;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC36303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK034155; BAC28611.1; -; mRNA.
DR   EMBL; AK036238; BAC29357.1; -; mRNA.
DR   EMBL; AK076333; BAC36303.1; ALT_INIT; mRNA.
DR   RefSeq; NP_766260.2; NM_172672.2.
DR   AlphaFoldDB; Q8BVW0; -.
DR   SMR; Q8BVW0; -.
DR   IntAct; Q8BVW0; 1.
DR   MINT; Q8BVW0; -.
DR   STRING; 10090.ENSMUSP00000116898; -.
DR   BindingDB; Q8BVW0; -.
DR   ChEMBL; CHEMBL3635; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   iPTMnet; Q8BVW0; -.
DR   PhosphoSitePlus; Q8BVW0; -.
DR   MaxQB; Q8BVW0; -.
DR   PaxDb; Q8BVW0; -.
DR   PRIDE; Q8BVW0; -.
DR   ProteomicsDB; 268845; -. [Q8BVW0-1]
DR   ProteomicsDB; 268846; -. [Q8BVW0-2]
DR   DNASU; 76051; -.
DR   GeneID; 76051; -.
DR   KEGG; mmu:76051; -.
DR   CTD; 2595; -.
DR   MGI; MGI:1923301; Ganc.
DR   eggNOG; KOG1066; Eukaryota.
DR   InParanoid; Q8BVW0; -.
DR   OrthoDB; 100626at2759; -.
DR   BioGRID-ORCS; 76051; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Ganc; mouse.
DR   PRO; PR:Q8BVW0; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8BVW0; protein.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:MGI.
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:0006006; P:glucose metabolic process; IC:MGI.
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   1: Evidence at protein level;
KW   Alternative splicing; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..898
FT                   /note="Neutral alpha-glucosidase C"
FT                   /id="PRO_0000185366"
FT   REGION          154..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        495
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        571
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         95
FT                   /note="R -> RYEVPDVINSKLGTVR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010619"
FT   VAR_SEQ         154..199
FT                   /note="QRATKGNGQNTPAATSQENQEDLGLWEEKFGKFVDVKANGPSSVGL -> LY
FT                   TLLALKIYLNGACLEYQLPWTRVFTLAQQMPYCLSFLPFPPTRL (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010620"
FT   VAR_SEQ         200..898
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010621"
SQ   SEQUENCE   898 AA;  102008 MW;  6AE5A1EBADBA52C0 CRC64;
     MEAAEKEEIS VEDEAVDKTI FKDCGKIAFY RRQKQQLTKT TTYQALLGSV DTEQDSTRFQ
     IISEATKIPL VAEVYGIEKD IFRLKINEET PLKPRLVCSG DTGSLILTNR KGDLKCHVSA
     NPFKIDLLSK NEAVISINSL GQLYFEHLQV PHKQRATKGN GQNTPAATSQ ENQEDLGLWE
     EKFGKFVDVK ANGPSSVGLD FSLHGFEHLY GIPQHAESHQ LKNTRDGDAY RLYNLDVYGY
     QVHDKMGIYG SVPYLLAHKQ GRTVGIFWLN ASETLVEINT EPAVEYTLTQ MGPAAAKPKV
     RCRTDVHWMS ESGIIDVFLL TGPTPADVFK QYSYITGTQA MPPLFSLGYH QCRWNYEDEQ
     DVKAVDAGFD EHDIPYDVMW LDIEHTEDKK YFTWDKKRFA NPKRMQELLR SKKRKLVVIS
     DPHIKVDPDY TVYAQAKEQG FFVKNPEGGD FEGVCWPGLS SYLDFTNPKV REWYSSLFAF
     PVYQGSTDIL FLWNDMNEPS VFRGPELTMH KSAVHYGDWE HRELHNIYGF YQQMATAEGL
     IQRSKGKERP FVLSRSFFAG SQKYGAVWTG DNKAEWSYLK ISIPMLLTLS VSGISFCGAD
     VGGFIGNPEA ELLVRWYQAG AYQPFFRGHA TMNTKRREPW LFGEEYTQLI REAIRQRYAL
     LPYLYSLFYH THVSSQPVMR PLWVEYPDDL ETFAVEDEYM LGSALLVHPV TDPQTATIDV
     FLPGSDEVWY DSKTFAYWKG GCTVKIPVTL DTIPVFQRGG SVVPVKTTVG TSTGWMADSP
     YELRVALSTQ GSAVGELYLD DGHSFQYLHQ NQFLYRKFLF CSSVLTNRCA NEKGHYPSKC
     IVEQILVLGL KKKPSSVTTH LSDGRAQPAA FTYCAETSAL RLEKLSLRIG EDWEVRVG