UniProtKB - O43451 (MGA_HUMAN)
Maltase-glucoamylase
MGAM
Functioni
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:18356321, PubMed:27480812, PubMed:18036614, PubMed:22058037).
Mainly hydrolyzes short length oligomaltoses having two to seven glucose residues (PubMed:12547908, PubMed:18356321, PubMed:27480812, PubMed:18036614, PubMed:22058037).
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).
5 PublicationsMiscellaneous
Catalytic activityi
- Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.5 Publications EC:3.2.1.20
Activity regulationi
Kineticsi
- KM=8.7 mM for maltose (with ntMGAM)1 Publication
- KM=27.1 mM for nigerose (with ntMGAM)1 Publication
- KM=11.6 mM for kojibiose (with ntMGAM)1 Publication
- KM=6.40 mM for maltose (with ntMGAM)1 Publication
- KM=4.44 mM for maltotriose (with ntMGAM)1 Publication
- KM=3.39 mM for maltotetraose (with ntMGAM)1 Publication
- KM=9.14 mM for maltopentaose (with ntMGAM)1 Publication
- KM=9.76 mM for maltohexaose (with ntMGAM)1 Publication
- KM=13.12 mM for maltoheptaose (with ntMGAM)1 Publication
- KM=5.67 mM for maltose (with ctMGAM)1 Publication
- KM=0.91 mM for maltotriose (with ctMGAM)1 Publication
- KM=0.96 mM for maltotetraose (with ctMGAM)1 Publication
- KM=0.61 mM for maltopentaose (with ctMGAM)1 Publication
- KM=1.05 mM for maltohexaose (with ctMGAM)1 Publication
- KM=2.27 mM for maltoheptaose (with ctMGAM)1 Publication
- KM=4.34 mM for maltopentaose (with ntMGAM)1 Publication
- KM=7 mM for maltopentaose (with ntMGAM)1 Publication
- Vmax=8.2 µmol/min/mg enzyme toward maltose (with ntMGAM)1 Publication
- Vmax=9.58 µmol/min/mg enzyme toward maltotriose (with ntMGAM)1 Publication
- Vmax=7.65 µmol/min/mg enzyme toward maltotetraose (with ntMGAM)1 Publication
- Vmax=6.97 µmol/min/mg enzyme toward maltopentaose (with ntMGAM)1 Publication
- Vmax=7.51 µmol/min/mg enzyme toward maltodextrin (with ntMGAM)1 Publication
- Vmax=11 µmol/min/mg enzyme toward alpha-limit dextrin (with ntMGAM)1 Publication
pH dependencei
: Carbohydrate degradation Pathwayi
This protein is involved in Carbohydrate degradation.3 PublicationsView all proteins of this organism that are known to be involved in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 289 | Acarbose1 Publication | 1 | |
Binding sitei | 413 | Acarbose1 Publication | 1 | |
Active sitei | 529 | NucleophilePROSITE-ProRule annotation | 1 | |
Active sitei | 532 | By similarity | 1 | |
Binding sitei | 612 | Acarbose1 Publication | 1 | |
Binding sitei | 628 | Acarbose1 Publication | 1 | |
Binding sitei | 686 | Acarbose1 Publication | 1 | |
Active sitei | 1420 | NucleophilePROSITE-ProRule annotation | 1 | |
Active sitei | 1423 | By similarity | 1 | |
Active sitei | 1526 | Proton donorBy similarity | 1 |
GO - Molecular functioni
- alpha-1,4-glucosidase activity Source: UniProtKB
- carbohydrate binding Source: InterPro
- catalytic activity Source: ProtInc
- glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
- hydrolase activity, hydrolyzing O-glycosyl compounds Source: GO_Central
- maltose alpha-glucosidase activity Source: UniProtKB-EC
GO - Biological processi
- dextrin catabolic process Source: UniProtKB
- maltose catabolic process Source: UniProtKB
- starch catabolic process Source: ProtInc
Keywordsi
Molecular function | Glycosidase, Hydrolase, Multifunctional enzyme |
Enzyme and pathway databases
BRENDAi | 3.2.1.20, 2681 3.2.1.3, 2681 |
PathwayCommonsi | O43451 |
Reactomei | R-HSA-189085, Digestion of dietary carbohydrate R-HSA-6798695, Neutrophil degranulation |
SignaLinki | O43451 |
Protein family/group databases
CAZyi | GH31, Glycoside Hydrolase Family 31 |
Names & Taxonomyi
Protein namesi | Recommended name: Maltase-glucoamylase1 PublicationAlternative name(s): Alpha-1,4-glucosidase (EC:3.2.1.204 Publications) |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:7043, MGAM |
MIMi | 154360, gene |
neXtProti | NX_O43451 |
VEuPathDBi | HostDB:ENSG00000257335 |
Subcellular locationi
Plasma membrane
Note: Brush border.1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- plasma membrane Source: Reactome
Other locations
- ficolin-1-rich granule membrane Source: Reactome
- integral component of membrane Source: UniProtKB-KW
- tertiary granule membrane Source: Reactome
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 13 | CytoplasmicSequence analysisAdd BLAST | 13 | |
Transmembranei | 14 – 34 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 21 | |
Topological domaini | 35 – 2753 | LumenalSequence analysisAdd BLAST | 2719 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 385 | Y → W: Decreases alpha-1,4-glucosidase activity toward maltose. 1 Publication | 1 | |
Mutagenesisi | 529 | D → A: Loss of alpha-1,4-glucosidase activity toward maltose. 1 Publication | 1 | |
Mutagenesisi | 1251 | Y → W: Decreases alpha-1,4-glucosidase activity toward maltose. 1 Publication | 1 | |
Mutagenesisi | 1357 – 1377 | Missing : Decreases alpha-1,4-glucosidase activity toward long oligomaltose substrates having four to seven D-glucose residues. 1 PublicationAdd BLAST | 21 |
Organism-specific databases
DisGeNETi | 8972 |
OpenTargetsi | ENSG00000257335 |
PharmGKBi | PA30778 |
Miscellaneous databases
Pharosi | O43451, Tclin |
Chemistry databases
ChEMBLi | CHEMBL2074 |
DrugBanki | DB00284, Acarbose DB00491, Miglitol DB04878, Voglibose |
DrugCentrali | O43451 |
GuidetoPHARMACOLOGYi | 2627 |
Genetic variation databases
BioMutai | MGAM |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000185363 | 1 – 2753 | Maltase-glucoamylaseAdd BLAST | 2753 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 90 ↔ 118 | PROSITE-ProRule annotation | ||
Disulfide bondi | 101 ↔ 117 | PROSITE-ProRule annotation1 Publication | ||
Disulfide bondi | 112 ↔ 130 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 135 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 295 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Modified residuei | 416 | SulfotyrosineSequence analysis | 1 | |
Modified residuei | 425 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 457 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 458 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 479 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 659 ↔ 670 | PROSITE-ProRule annotation1 Publication | ||
Glycosylationi | 707 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 749 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 827 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 885 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 912 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 966 ↔ 983 | PROSITE-ProRule annotation | ||
Glycosylationi | 977 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 978 ↔ 996 | PROSITE-ProRule annotation | ||
Glycosylationi | 989 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1255 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1282 | SulfotyrosineSequence analysis | 1 | |
Glycosylationi | 1323 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1364 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1388 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1862 ↔ 1879 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1874 ↔ 1892 | PROSITE-ProRule annotation | ||
Glycosylationi | 2499 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2568 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2738 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2743 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, SulfationProteomic databases
jPOSTi | O43451 |
MassIVEi | O43451 |
PaxDbi | O43451 |
PeptideAtlasi | O43451 |
PRIDEi | O43451 |
ProteomicsDBi | 48955 |
PTM databases
GlyConnecti | 1958, 24 N-Linked glycans (6 sites) |
GlyGeni | O43451, 24 sites, 24 N-linked glycans (6 sites), 4 O-linked glycans (4 sites) |
iPTMneti | O43451 |
PhosphoSitePlusi | O43451 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000257335, Expressed in jejunal mucosa and 144 other tissues |
ExpressionAtlasi | O43451, baseline and differential |
Genevisiblei | O43451, HS |
Organism-specific databases
HPAi | ENSG00000257335, Tissue enhanced (epididymis, intestine) |
Interactioni
Subunit structurei
Monomer.
1 PublicationBinary interactionsi
O43451
Protein-protein interaction databases
BioGRIDi | 114462, 9 interactors |
CORUMi | O43451 |
IntActi | O43451, 11 interactors |
MINTi | O43451 |
STRINGi | 9606.ENSP00000447378 |
Chemistry databases
BindingDBi | O43451 |
Miscellaneous databases
RNActi | O43451, protein |
Structurei
Secondary structure
3D structure databases
SMRi | O43451 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O43451 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 88 – 134 | P-type 1PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 954 – 1000 | P-type 2PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 1850 – 1896 | P-type 3PROSITE-ProRule annotationAdd BLAST | 47 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 41 – 87 | DisorderedSequence analysisAdd BLAST | 47 | |
Regioni | 356 – 737 | Maltase1 PublicationAdd BLAST | 382 | |
Regioni | 1221 – 1632 | Glucoamylase1 PublicationAdd BLAST | 412 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 42 – 87 | Polar residuesSequence analysisAdd BLAST | 46 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1065, Eukaryota |
GeneTreei | ENSGT00940000161540 |
HOGENOMi | CLU_000631_3_0_1 |
InParanoidi | O43451 |
OMAi | TPISAEC |
OrthoDBi | 151244at2759 |
PhylomeDBi | O43451 |
TreeFami | TF314577 |
Family and domain databases
CDDi | cd00111, Trefoil, 2 hits |
Gene3Di | 2.60.40.1180, 4 hits 4.10.110.10, 2 hits |
InterProi | View protein in InterPro IPR031727, Gal_mutarotase_N IPR011013, Gal_mutarotase_sf_dom IPR000322, Glyco_hydro_31 IPR030458, Glyco_hydro_31_AS IPR030459, Glyco_hydro_31_CS IPR013780, Glyco_hydro_b IPR017853, Glycoside_hydrolase_SF IPR017957, P_trefoil_CS IPR000519, P_trefoil_dom IPR044913, P_trefoil_dom_sf |
Pfami | View protein in Pfam PF01055, Glyco_hydro_31, 2 hits PF16863, NtCtMGAM_N, 2 hits PF00088, Trefoil, 2 hits |
SMARTi | View protein in SMART SM00018, PD, 2 hits |
SUPFAMi | SSF51445, SSF51445, 2 hits SSF74650, SSF74650, 2 hits |
PROSITEi | View protein in PROSITE PS00129, GLYCOSYL_HYDROL_F31_1, 2 hits PS00707, GLYCOSYL_HYDROL_F31_2, 1 hit PS00025, P_TREFOIL_1, 1 hit PS51448, P_TREFOIL_2, 2 hits |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MARKKLKKFT TLEIVLSVLL LVLFIISIVL IVLLAKESLK STAPDPGTTG
60 70 80 90 100
TPDPGTTGTP DPGTTGTTHA RTTGPPDPGT TGTTPVSAEC PVVNELERIN
110 120 130 140 150
CIPDQPPTKA TCDQRGCCWN PQGAVSVPWC YYSKNHSYHV EGNLVNTNAG
160 170 180 190 200
FTARLKNLPS SPVFGSNVDN VLLTAEYQTS NRFHFKLTDQ TNNRFEVPHE
210 220 230 240 250
HVQSFSGNAA ASLTYQVEIS RQPFSIKVTR RSNNRVLFDS SIGPLLFADQ
260 270 280 290 300
FLQLSTRLPS TNVYGLGEHV HQQYRHDMNW KTWPIFNRDT TPNGNGTNLY
310 320 330 340 350
GAQTFFLCLE DASGLSFGVF LMNSNAMEVV LQPAPAITYR TIGGILDFYV
360 370 380 390 400
FLGNTPEQVV QEYLELIGRP ALPSYWALGF HLSRYEYGTL DNMREVVERN
410 420 430 440 450
RAAQLPYDVQ HADIDYMDER RDFTYDSVDF KGFPEFVNEL HNNGQKLVII
460 470 480 490 500
VDPAISNNSS SSKPYGPYDR GSDMKIWVNS SDGVTPLIGE VWPGQTVFPD
510 520 530 540 550
YTNPNCAVWW TKEFELFHNQ VEFDGIWIDM NEVSNFVDGS VSGCSTNNLN
560 570 580 590 600
NPPFTPRILD GYLFCKTLCM DAVQHWGKQY DIHNLYGYSM AVATAEAAKT
610 620 630 640 650
VFPNKRSFIL TRSTFAGSGK FAAHWLGDNT ATWDDLRWSI PGVLEFNLFG
660 670 680 690 700
IPMVGPDICG FALDTPEELC RRWMQLGAFY PFSRNHNGQG YKDQDPASFG
710 720 730 740 750
ADSLLLNSSR HYLNIRYTLL PYLYTLFFRA HSRGDTVARP LLHEFYEDNS
760 770 780 790 800
TWDVHQQFLW GPGLLITPVL DEGAEKVMAY VPDAVWYDYE TGSQVRWRKQ
810 820 830 840 850
KVEMELPGDK IGLHLRGGYI FPTQQPNTTT LASRKNPLGL IIALDENKEA
860 870 880 890 900
KGELFWDNGE TKDTVANKVY LLCEFSVTQN RLEVNISQST YKDPNNLAFN
910 920 930 940 950
EIKILGTEEP SNVTVKHNGV PSQTSPTVTY DSNLKVAIIT DIDLLLGEAY
960 970 980 990 1000
TVEWSIKIRD EEKIDCYPDE NGASAENCTA RGCIWEASNS SGVPFCYFVN
1010 1020 1030 1040 1050
DLYSVSDVQY NSHGATADIS LKSSVYANAF PSTPVNPLRL DVTYHKNEML
1060 1070 1080 1090 1100
QFKIYDPNKN RYEVPVPLNI PSMPSSTPEG QLYDVLIKKN PFGIEIRRKS
1110 1120 1130 1140 1150
TGTIIWDSQL LGFTFSDMFI RISTRLPSKY LYGFGETEHR SYRRDLEWHT
1160 1170 1180 1190 1200
WGMFSRDQPP GYKKNSYGVH PYYMGLEEDG SAHGVLLLNS NAMDVTFQPL
1210 1220 1230 1240 1250
PALTYRTTGG VLDFYVFLGP TPELVTQQYT ELIGRPVMVP YWSLGFQLCR
1260 1270 1280 1290 1300
YGYQNDSEIA SLYDEMVAAQ IPYDVQYSDI DYMERQLDFT LSPKFAGFPA
1310 1320 1330 1340 1350
LINRMKADGM RVILILDPAI SGNETQPYPA FTRGVEDDVF IKYPNDGDIV
1360 1370 1380 1390 1400
WGKVWPDFPD VVVNGSLDWD SQVELYRAYV AFPDFFRNST AKWWKREIEE
1410 1420 1430 1440 1450
LYNNPQNPER SLKFDGMWID MNEPSSFVNG AVSPGCRDAS LNHPPYMPHL
1460 1470 1480 1490 1500
ESRDRGLSSK TLCMESQQIL PDGSLVQHYN VHNLYGWSQT RPTYEAVQEV
1510 1520 1530 1540 1550
TGQRGVVITR STFPSSGRWA GHWLGDNTAA WDQLKKSIIG MMEFSLFGIS
1560 1570 1580 1590 1600
YTGADICGFF QDAEYEMCVR WMQLGAFYPF SRNHNTIGTR RQDPVSWDAA
1610 1620 1630 1640 1650
FVNISRNVLQ TRYTLLPYLY TLMQKAHTEG VTVVRPLLHE FVSDQVTWDI
1660 1670 1680 1690 1700
DSQFLLGPAF LVSPVLERNA RNVTAYFPRA RWYDYYTGVD INARGEWKTL
1710 1720 1730 1740 1750
PAPLDHINLH VRGGYILPWQ EPALNTHLSR KNPLGLIIAL DENKEAKGEL
1760 1770 1780 1790 1800
FWDDGQTKDT VAKKVYLLCE FSVTQNHLEV TISQSTYKDP NNLAFNEIKI
1810 1820 1830 1840 1850
LGMEEPSNVT VKHNGVPSQT SPTVTYDSNL KVAIITDINL FLGEAYTVEW
1860 1870 1880 1890 1900
SIKIRDEEKI DCYPDENGDS AENCTARGCI WEASNSSGVP FCYFVNDLYS
1910 1920 1930 1940 1950
VSDVQYNSHG ATADISLKSS VHANAFPSTP VNPLRLDVTY HKNEMLQFKI
1960 1970 1980 1990 2000
YDPNNNRYEV PVPLNIPSVP SSTPEGQLYD VLIKKNPFGI EIRRKSTGTI
2010 2020 2030 2040 2050
IWDSQLLGFT FNDMFIRIST RLPSKYLYGF GETEHTSYRR DLEWHTWGMF
2060 2070 2080 2090 2100
SRDQPPGYKK NSYGVHPYYM GLEEDGSAHG VLLLNSNAMD VTFQPLPALT
2110 2120 2130 2140 2150
YRTTGGVLDF YVFLGPTPEL VTQQYTELIG RPVMVPYWSL GFQLCRYGYQ
2160 2170 2180 2190 2200
NDSEISSLYD EMVAAQIPYD VQYSDIDYME RQLDFTLSPK FAGFPALINR
2210 2220 2230 2240 2250
MKADGMRVIL ILDPAISGNE TQPYPAFTRG VEDDVFIKYP NDGDIVWGKV
2260 2270 2280 2290 2300
WPDFPDVVVN GSLDWDSQVE LYRAYVAFPD FFRNSTAKWW KREIEELYNN
2310 2320 2330 2340 2350
PQNPERSLKF DGMWIDMNEP SSFVNGAVSP GCRDASLNHP PYMPYLESRD
2360 2370 2380 2390 2400
RGLSSKTLCM ESQQILPDGS PVQHYNVHNL YGWSQTRPTY EAVQEVTGQR
2410 2420 2430 2440 2450
GVVITRSTFP SSGRWAGHWL GDNTAAWDQL KKSIIGMMEF SLFGISYTGA
2460 2470 2480 2490 2500
DICGFFQDAE YEMCVRWMQL GAFYPFSRNH NTIGTRRQDP VSWDVAFVNI
2510 2520 2530 2540 2550
SRTVLQTRYT LLPYLYTLMH KAHTEGVTVV RPLLHEFVSD QVTWDIDSQF
2560 2570 2580 2590 2600
LLGPAFLVSP VLERNARNVT AYFPRARWYD YYTGVDINAR GEWKTLPAPL
2610 2620 2630 2640 2650
DHINLHVRGG YILPWQEPAL NTHLSRQKFM GFKIALDDEG TAGGWLFWDD
2660 2670 2680 2690 2700
GQSIDTYGKG LYYLASFSAS QNTMQSHIIF NNYITGTNPL KLGYIEIWGV
2710 2720 2730 2740 2750
GSVPVTSVSI SVSGMVITPS FNNDPTTQVL SIDVTDRNIS LHNFTSLTWI
STL
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE7EW87 | E7EW87_HUMAN | Maltase-glucoamylase, intestinal | MGAM | 185 | Annotation score: | ||
A0A0J9YVZ3 | A0A0J9YVZ3_HUMAN | Maltase-glucoamylase, intestinal | MGAM | 2,012 | Annotation score: | ||
A0A0J9YX77 | A0A0J9YX77_HUMAN | Maltase-glucoamylase, intestinal | MGAM | 1,114 | Annotation score: | ||
E9PEQ5 | E9PEQ5_HUMAN | Maltase-glucoamylase, intestinal | MGAM | 143 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 854 | L → P in AAI20873 (PubMed:15489334).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_047350 | 404 | Q → H. Corresponds to variant dbSNP:rs2272330Ensembl. | 1 | |
Natural variantiVAR_047351 | 542 | S → L. Corresponds to variant dbSNP:rs10266732Ensembl. | 1 | |
Natural variantiVAR_047352 | 858 | N → D2 PublicationsCorresponds to variant dbSNP:rs2960746Ensembl. | 1 | |
Natural variantiVAR_047353 | 2534 | L → I. Corresponds to variant dbSNP:rs9655651Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_061364 | 1594 – 2489 | Missing in isoform 1. 1 PublicationAdd BLAST | 896 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF016833 mRNA Translation: AAC39568.2 AC091684 Genomic DNA Translation: AAP21875.1 AC073647 Genomic DNA Translation: AAS07445.1 AC091742 Genomic DNA No translation available. BC120872 mRNA Translation: AAI20873.1 |
CCDSi | CCDS47727.1 |
RefSeqi | NP_004659.2, NM_004668.2 |
Genome annotation databases
Ensembli | ENST00000549489; ENSP00000447378; ENSG00000257335 ENST00000620571; ENSP00000482292; ENSG00000257335 |
GeneIDi | 8972 |
KEGGi | hsa:8972 |
MANE-Selecti | ENST00000475668.6; ENSP00000417515.2; NM_001365693.1; NP_001352622.1 |
UCSCi | uc003vwy.4, human |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF016833 mRNA Translation: AAC39568.2 AC091684 Genomic DNA Translation: AAP21875.1 AC073647 Genomic DNA Translation: AAS07445.1 AC091742 Genomic DNA No translation available. BC120872 mRNA Translation: AAI20873.1 |
CCDSi | CCDS47727.1 |
RefSeqi | NP_004659.2, NM_004668.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QLY | X-ray | 2.00 | A | 87-954 | [»] | |
2QMJ | X-ray | 1.90 | A | 87-954 | [»] | |
3CTT | X-ray | 2.10 | A | 87-954 | [»] | |
3L4T | X-ray | 1.90 | A | 87-954 | [»] | |
3L4U | X-ray | 1.90 | A | 87-954 | [»] | |
3L4V | X-ray | 2.10 | A | 87-954 | [»] | |
3L4W | X-ray | 2.00 | A | 87-954 | [»] | |
3L4X | X-ray | 1.90 | A | 87-954 | [»] | |
3L4Y | X-ray | 1.80 | A | 87-954 | [»] | |
3L4Z | X-ray | 2.00 | A | 87-954 | [»] | |
3TON | X-ray | 2.95 | A/B | 960-1853 | [»] | |
3TOP | X-ray | 2.88 | A/B | 960-1853 | [»] | |
SMRi | O43451 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 114462, 9 interactors |
CORUMi | O43451 |
IntActi | O43451, 11 interactors |
MINTi | O43451 |
STRINGi | 9606.ENSP00000447378 |
Chemistry databases
BindingDBi | O43451 |
ChEMBLi | CHEMBL2074 |
DrugBanki | DB00284, Acarbose DB00491, Miglitol DB04878, Voglibose |
DrugCentrali | O43451 |
GuidetoPHARMACOLOGYi | 2627 |
Protein family/group databases
CAZyi | GH31, Glycoside Hydrolase Family 31 |
PTM databases
GlyConnecti | 1958, 24 N-Linked glycans (6 sites) |
GlyGeni | O43451, 24 sites, 24 N-linked glycans (6 sites), 4 O-linked glycans (4 sites) |
iPTMneti | O43451 |
PhosphoSitePlusi | O43451 |
Genetic variation databases
BioMutai | MGAM |
Proteomic databases
jPOSTi | O43451 |
MassIVEi | O43451 |
PaxDbi | O43451 |
PeptideAtlasi | O43451 |
PRIDEi | O43451 |
ProteomicsDBi | 48955 |
Protocols and materials databases
Antibodypediai | 50132, 38 antibodies from 14 providers |
DNASUi | 8972 |
Genome annotation databases
Ensembli | ENST00000549489; ENSP00000447378; ENSG00000257335 ENST00000620571; ENSP00000482292; ENSG00000257335 |
GeneIDi | 8972 |
KEGGi | hsa:8972 |
MANE-Selecti | ENST00000475668.6; ENSP00000417515.2; NM_001365693.1; NP_001352622.1 |
UCSCi | uc003vwy.4, human |
Organism-specific databases
CTDi | 8972 |
DisGeNETi | 8972 |
GeneCardsi | MGAM |
HGNCi | HGNC:7043, MGAM |
HPAi | ENSG00000257335, Tissue enhanced (epididymis, intestine) |
MIMi | 154360, gene |
neXtProti | NX_O43451 |
OpenTargetsi | ENSG00000257335 |
PharmGKBi | PA30778 |
VEuPathDBi | HostDB:ENSG00000257335 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1065, Eukaryota |
GeneTreei | ENSGT00940000161540 |
HOGENOMi | CLU_000631_3_0_1 |
InParanoidi | O43451 |
OMAi | TPISAEC |
OrthoDBi | 151244at2759 |
PhylomeDBi | O43451 |
TreeFami | TF314577 |
Enzyme and pathway databases
BRENDAi | 3.2.1.20, 2681 3.2.1.3, 2681 |
PathwayCommonsi | O43451 |
Reactomei | R-HSA-189085, Digestion of dietary carbohydrate R-HSA-6798695, Neutrophil degranulation |
SignaLinki | O43451 |
Miscellaneous databases
BioGRID-ORCSi | 8972, 7 hits in 1038 CRISPR screens |
EvolutionaryTracei | O43451 |
GeneWikii | Maltase-glucoamylase |
GenomeRNAii | 8972 |
Pharosi | O43451, Tclin |
PROi | PR:O43451 |
RNActi | O43451, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000257335, Expressed in jejunal mucosa and 144 other tissues |
ExpressionAtlasi | O43451, baseline and differential |
Genevisiblei | O43451, HS |
Family and domain databases
CDDi | cd00111, Trefoil, 2 hits |
Gene3Di | 2.60.40.1180, 4 hits 4.10.110.10, 2 hits |
InterProi | View protein in InterPro IPR031727, Gal_mutarotase_N IPR011013, Gal_mutarotase_sf_dom IPR000322, Glyco_hydro_31 IPR030458, Glyco_hydro_31_AS IPR030459, Glyco_hydro_31_CS IPR013780, Glyco_hydro_b IPR017853, Glycoside_hydrolase_SF IPR017957, P_trefoil_CS IPR000519, P_trefoil_dom IPR044913, P_trefoil_dom_sf |
Pfami | View protein in Pfam PF01055, Glyco_hydro_31, 2 hits PF16863, NtCtMGAM_N, 2 hits PF00088, Trefoil, 2 hits |
SMARTi | View protein in SMART SM00018, PD, 2 hits |
SUPFAMi | SSF51445, SSF51445, 2 hits SSF74650, SSF74650, 2 hits |
PROSITEi | View protein in PROSITE PS00129, GLYCOSYL_HYDROL_F31_1, 2 hits PS00707, GLYCOSYL_HYDROL_F31_2, 1 hit PS00025, P_TREFOIL_1, 1 hit PS51448, P_TREFOIL_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | MGA_HUMAN | |
Accessioni | O43451Primary (citable) accession number: O43451 Secondary accession number(s): E7ER45 Q86UM5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | February 23, 2022 | |
Last modified: | February 23, 2022 | |
This is version 185 of the entry and version 6 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families