MGAM
entrez
8972
canonical
uniprot
O43451
canonical
ensembl
ENSG00000257335
resolver
ensp
ENSP00000417515
resolver
ensp
ENSP00000447378
resolver
genesymbol
MGAM
resolver
genesymbol_syn
MGA
resolver
genesymbol_syn
MGAML
resolver
hgnc
HGNC:7043
resolver
uniprot
E7ER45
resolver
uniprot
Q0VAX6
resolver
uniprot
Q75ME7
resolver
uniprot
Q86UM5
resolver
uniprot_entry
MGA_HUMAN
resolver
uniprot_sec
E7ER45
resolver
uniprot_sec
Q0VAX6
resolver
uniprot_sec
Q75ME7
resolver
uniprot_sec
Q86UM5
resolver
activity_regulation
ACTIVITY REGULATION: Down-regulated at high oligomaltose concentration as it occurs during the mealtime (PubMed:18356321). Down-regulated by anti-diabetic drug acarbose (PubMed:18036614, PubMed:22058037). {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037}.
uniprot
proteins
amino_acid_sequence
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDEEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIASLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDAAFVNISRNVLQTRYTLLPYLYTLMQKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRKNPLGLIIALDENKEAKGELFWDDGQTKDTVAKKVYLLCEFSVTQNHLEVTISQSTYKDPNNLAFNEIKILGMEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDINLFLGEAYTVEWSIKIRDEEKIDCYPDENGDSAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVHANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNNNRYEVPVPLNIPSVPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFNDMFIRISTRLPSKYLYGFGETEHTSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEISSLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPYLESRDRGLSSKTLCMESQQILPDGSPVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYTLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALDDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEIWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
uniprot
proteins
ec_number
3.2.1.20
uniprot
proteins
function
FUNCTION: Alpha-(1,4) exo-glucosidase involved in breakdown of dietary starch oligosaccharides in small intestine. Cleaves the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins with retention of anomeric center stereochemistry (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Mainly hydrolyzes short length oligomaltoses having two to seven glucose residues (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Can cleave alpha-(1,2), alpha-(1,3) and alpha-(1,6) glycosidic linkages with lower efficiency, whereas beta glycosidic linkages are usually not hydrolyzed (PubMed:27480812). {ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}.
uniprot
proteins
mass_dalton
312022
uniprot
proteins
mutagenesis
MUTAGEN 385; /note="Y->W: Decreases alpha-1,4-glucosidase activity toward maltose."; /evidence="ECO:0000269|PubMed:22058037"; MUTAGEN 529; /note="D->A: Loss of alpha-1,4-glucosidase activity toward maltose."; /evidence="ECO:0000269|PubMed:12547908"; MUTAGEN 1251; /note="Y->W: Decreases alpha-1,4-glucosidase activity toward maltose."; /evidence="ECO:0000269|PubMed:22058037"; MUTAGEN 1357..1377; /note="Missing: Decreases alpha-1,4-glucosidase activity toward long oligomaltose substrates having four to seven D-glucose residues."; /evidence="ECO:0000269|PubMed:22058037
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}.
uniprot
proteins
post_translational_modification
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:3143729}.; PTM: Does not undergo intracellular or extracellular proteolytic cleavage. {ECO:0000269|PubMed:3143729}.; PTM: Sulfated. {ECO:0000250}.
uniprot
proteins
protein_family
Glycosyl hydrolase 31 family
uniprot
proteins
pubmed
12547908
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18036614
uniprot
proteins
pubmed
18356321
uniprot
proteins
pubmed
22058037
uniprot
proteins
pubmed
24309898
uniprot
proteins
pubmed
27480812
uniprot
proteins
pubmed
3121301
uniprot
proteins
pubmed
3143729
uniprot
proteins
pubmed
9446624
uniprot
proteins
sequence_length
2753
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. {ECO:0000269|PubMed:3143729}.
uniprot
proteins
transmembrane_region
TRANSMEM 14..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins